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Volumn 22, Issue 1, 2016, Pages 85-99

Neutrophil proteolytic activation cascades: A possible mechanistic link between chronic periodontitis and coronary heart disease

Author keywords

Aggregatibacter actinomycetemcomitans; cardiovascular disease; coronary artery disease; gingival crevicular fluids; hypochlorous acid; lipopolysaccharide; matrix metalloproteinases; myeloperoxidase; neutrophils; oral infections; periodontal diseases; Porphyromonas gingivalis; tissue inhibitor of matrix metalloproteinases

Indexed keywords

CHEMOKINE; CYTOKINE; DOXYCYCLINE; GELATINASE B; LEUKOCYTE ELASTASE; MATRILYSIN; MATRIX METALLOPROTEINASE; NEUTROPHIL COLLAGENASE; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 84949678824     PISSN: 17534259     EISSN: 17534267     Source Type: Journal    
DOI: 10.1177/1753425915617521     Document Type: Article
Times cited : (49)

References (259)
  • 1
    • 0037266312 scopus 로고    scopus 로고
    • Neutrophil-mediated tissue injury in periodontal disease pathogenesis: Findings from localized aggressive periodontitis
    • Kantarci A, Oyaizu K, Van Dyke TE,. Neutrophil-mediated tissue injury in periodontal disease pathogenesis: findings from localized aggressive periodontitis. J Periodontol 2003; 74: 66-75.
    • (2003) J Periodontol , vol.74 , pp. 66-75
    • Kantarci, A.1    Oyaizu, K.2    Van Dyke, T.E.3
  • 2
    • 84855521783 scopus 로고    scopus 로고
    • Neutrophils in periodontal inflammation
    • Scott DA, Krauss J,. Neutrophils in periodontal inflammation. Front Oral Biol 2012; 15: 56-83.
    • (2012) Front Oral Biol , vol.15 , pp. 56-83
    • Scott, D.A.1    Krauss, J.2
  • 3
    • 0032175358 scopus 로고    scopus 로고
    • Neutrophil migration into the gingival sulcus is associated with transepithelial gradients of interleukin-8 and ICAM-1
    • Tonetti MS, Imboden MA, Lang NP,. Neutrophil migration into the gingival sulcus is associated with transepithelial gradients of interleukin-8 and ICAM-1. J Periodontol 1998; 69: 1139-1147.
    • (1998) J Periodontol , vol.69 , pp. 1139-1147
    • Tonetti, M.S.1    Imboden, M.A.2    Lang, N.P.3
  • 4
    • 0037736599 scopus 로고    scopus 로고
    • Periodontal disease and diabetes mellitus. Bidirectional relationship
    • Mealey BL, Rethman MP,. Periodontal disease and diabetes mellitus. Bidirectional relationship. Dent Today 2003; 22: 107-113.
    • (2003) Dent Today , vol.22 , pp. 107-113
    • Mealey, B.L.1    Rethman, M.P.2
  • 6
    • 67649933829 scopus 로고    scopus 로고
    • Short-term effects of non-surgical periodontal treatment on plasma level of reactive oxygen metabolites in patients with chronic periodontitis
    • Tamaki N, Tomofuji T, Ekuni D, et al. Short-term effects of non-surgical periodontal treatment on plasma level of reactive oxygen metabolites in patients with chronic periodontitis. J Periodontol 2009; 80: 901-906.
    • (2009) J Periodontol , vol.80 , pp. 901-906
    • Tamaki, N.1    Tomofuji, T.2    Ekuni, D.3
  • 7
    • 13444265872 scopus 로고    scopus 로고
    • Periodontal microbiota and carotid intima-media thickness: The Oral Infections and Vascular Disease Epidemiology Study (INVEST)
    • Desvarieux M, Demmer RT, Rundek T, et al. Periodontal microbiota and carotid intima-media thickness: the Oral Infections and Vascular Disease Epidemiology Study (INVEST). Circulation 2005; 111: 576-582.
    • (2005) Circulation , vol.111 , pp. 576-582
    • Desvarieux, M.1    Demmer, R.T.2    Rundek, T.3
  • 9
    • 0038050412 scopus 로고    scopus 로고
    • New bacterial species associated with chronic periodontitis
    • Kumar PS, Griffen AL, Barton JA, et al. New bacterial species associated with chronic periodontitis. J Dent Res 2003; 82: 338-344.
    • (2003) J Dent Res , vol.82 , pp. 338-344
    • Kumar, P.S.1    Griffen, A.L.2    Barton, J.A.3
  • 10
    • 84873708523 scopus 로고    scopus 로고
    • The oral microbiome in health and disease
    • Wade WG,. The oral microbiome in health and disease. Pharmacol Res 2013; 69: 137-143.
    • (2013) Pharmacol Res , vol.69 , pp. 137-143
    • Wade, W.G.1
  • 11
    • 79955531353 scopus 로고    scopus 로고
    • Diet, commensals and the intestine as sources of pathogen-associated molecular patterns in atherosclerosis, type 2 diabetes and non-alcoholic fatty liver disease
    • Erridge C,. Diet, commensals and the intestine as sources of pathogen-associated molecular patterns in atherosclerosis, type 2 diabetes and non-alcoholic fatty liver disease. Atherosclerosis 2011; 216: 1-6.
    • (2011) Atherosclerosis , vol.216 , pp. 1-6
    • Erridge, C.1
  • 12
    • 33646685234 scopus 로고    scopus 로고
    • Incidence of bacteremia after chewing, tooth brushing and scaling in individuals with periodontal inflammation
    • Forner L, Larsen T, Kilian M, et al. Incidence of bacteremia after chewing, tooth brushing and scaling in individuals with periodontal inflammation. J Clin Periodontol 2006; 33: 401-407.
    • (2006) J Clin Periodontol , vol.33 , pp. 401-407
    • Forner, L.1    Larsen, T.2    Kilian, M.3
  • 13
    • 8344241095 scopus 로고    scopus 로고
    • Severe periodontitis enhances macrophage activation via increased serum lipopolysaccharide
    • Pussinen PJ, Vilkuna-Rautiainen T, Alfthan G, et al. Severe periodontitis enhances macrophage activation via increased serum lipopolysaccharide. Arterioscler Thromb Vasc Biol 2004; 24: 2174-2180.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 2174-2180
    • Pussinen, P.J.1    Vilkuna-Rautiainen, T.2    Alfthan, G.3
  • 14
    • 0036193459 scopus 로고    scopus 로고
    • Systemic release of endotoxins induced by gentle mastication: Association with periodontitis severity
    • Geerts SO, Nys M, De MP, et al. Systemic release of endotoxins induced by gentle mastication: association with periodontitis severity. J Periodontol 2002; 73: 73-78.
    • (2002) J Periodontol , vol.73 , pp. 73-78
    • Geerts, S.O.1    Nys, M.2    De, M.P.3
  • 15
    • 0035058921 scopus 로고    scopus 로고
    • Distribution and kinetics of lipoprotein-bound endotoxin
    • Levels JH, Abraham PR, van den Ende A, et al. Distribution and kinetics of lipoprotein-bound endotoxin. Infect Immun 2001; 69: 2821-2828.
    • (2001) Infect Immun , vol.69 , pp. 2821-2828
    • Levels, J.H.1    Abraham, P.R.2    Van Den Ende, A.3
  • 16
    • 58949100579 scopus 로고    scopus 로고
    • Lipopolysaccharide associates with pro-atherogenic lipoproteins in periodontitis patients
    • Kallio KA, Buhlin K, Jauhiainen M, et al. Lipopolysaccharide associates with pro-atherogenic lipoproteins in periodontitis patients. Innate Immun 2008; 14: 247-253.
    • (2008) Innate Immun , vol.14 , pp. 247-253
    • Kallio, K.A.1    Buhlin, K.2    Jauhiainen, M.3
  • 17
    • 37349101204 scopus 로고    scopus 로고
    • Aggregatibacter actinomycetemcomitans induces MMP-9 expression and proatherogenic lipoprotein profile in apoE-deficient mice
    • Tuomainen AM, Jauhiainen M, Kovanen PT, et al. Aggregatibacter actinomycetemcomitans induces MMP-9 expression and proatherogenic lipoprotein profile in apoE-deficient mice. Microb Pathog 2008; 44: 111-117.
    • (2008) Microb Pathog , vol.44 , pp. 111-117
    • Tuomainen, A.M.1    Jauhiainen, M.2    Kovanen, P.T.3
  • 18
    • 84876677359 scopus 로고    scopus 로고
    • Very low density lipoproteins derived from periodontitis patients facilitate macrophage activation via lipopolysaccharide function
    • Kallio KAE, Hyvärinen K, Kovanen PT, et al. Very low density lipoproteins derived from periodontitis patients facilitate macrophage activation via lipopolysaccharide function. Metabolism 2013; 62: 661-668.
    • (2013) Metabolism , vol.62 , pp. 661-668
    • Kallio, K.A.E.1    Hyvärinen, K.2    Kovanen, P.T.3
  • 19
    • 84940000810 scopus 로고    scopus 로고
    • Endotoxemia, nutrition, and cardiometabolic disorders
    • Kallio KA, Hätonen KA, Lehto M, et al. Endotoxemia, nutrition, and cardiometabolic disorders. Acta Diabetol 2015; 52: 395-404.
    • (2015) Acta Diabetol , vol.52 , pp. 395-404
    • Kallio, K.A.1    Hätonen, K.A.2    Lehto, M.3
  • 20
    • 84856009496 scopus 로고    scopus 로고
    • Bacterial endotoxin activity in human serum is associated with dyslipidemia, insulin resistance, obesity, and chronic inflammation
    • Lassenius MI, Pietiläinen KH, Kaartinen K, et al. Bacterial endotoxin activity in human serum is associated with dyslipidemia, insulin resistance, obesity, and chronic inflammation. Diabetes Care 2011; 34: 1809-1815.
    • (2011) Diabetes Care , vol.34 , pp. 1809-1815
    • Lassenius, M.I.1    Pietiläinen, K.H.2    Kaartinen, K.3
  • 21
    • 84884606817 scopus 로고    scopus 로고
    • Metabolic endotoxemia: A molecular link between obesity and cardiovascular risk
    • Neves AL, Coelho J, Couto L, et al. Metabolic endotoxemia: a molecular link between obesity and cardiovascular risk. J Mol Endocrinol 2013; 51: R51-R64.
    • (2013) J Mol Endocrinol , vol.51 , pp. R51-R64
    • Neves, A.L.1    Coelho, J.2    Couto, L.3
  • 22
    • 69549088235 scopus 로고    scopus 로고
    • Serum lipopolysaccharide activity is associated with the progression of kidney disease in finnish patients with type 1 diabetes
    • Nymark M, Pussinen PJ, Tuomainen AM, et al. Serum lipopolysaccharide activity is associated with the progression of kidney disease in finnish patients with type 1 diabetes. Diabetes Care 2009; 32: 1689-1693.
    • (2009) Diabetes Care , vol.32 , pp. 1689-1693
    • Nymark, M.1    Pussinen, P.J.2    Tuomainen, A.M.3
  • 23
    • 79951702804 scopus 로고    scopus 로고
    • Endotoxemia is associated with an increased risk of incident diabetes
    • Pussinen PJ, Havulinna AS, Lehto M, et al. Endotoxemia is associated with an increased risk of incident diabetes. Diabetes Care 2011; 34: 392-397.
    • (2011) Diabetes Care , vol.34 , pp. 392-397
    • Pussinen, P.J.1    Havulinna, A.S.2    Lehto, M.3
  • 24
    • 34249277445 scopus 로고    scopus 로고
    • Endotoxemia, immune response to periodontal pathogens, and systemic inflammation associate with incident cardiovascular disease events
    • Pussinen PJ, Tuomisto K, Jousilahti P, et al. Endotoxemia, immune response to periodontal pathogens, and systemic inflammation associate with incident cardiovascular disease events. Arterioscler Thromb Vasc Biol 2007; 27: 1433-1439.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 1433-1439
    • Pussinen, P.J.1    Tuomisto, K.2    Jousilahti, P.3
  • 25
    • 0037022910 scopus 로고    scopus 로고
    • Inflammation and atherosclerosis
    • Libby P, Ridker PM, Maseri A,. Inflammation and atherosclerosis. Circulation 2002; 105: 1135-1143.
    • (2002) Circulation , vol.105 , pp. 1135-1143
    • Libby, P.1    Ridker, P.M.2    Maseri, A.3
  • 26
    • 0032693599 scopus 로고    scopus 로고
    • Atherosclerosis is an inflammatory disease
    • Ross R,. Atherosclerosis is an inflammatory disease. Am Heart J 1999; 138: S419-S420.
    • (1999) Am Heart J , vol.138 , pp. S419-S420
    • Ross, R.1
  • 27
    • 0037059560 scopus 로고    scopus 로고
    • The multiple mechanisms by which infection may contribute to atherosclerosis development and course
    • Epstein SE,. The multiple mechanisms by which infection may contribute to atherosclerosis development and course. Circ Res 2002; 90: 2-4.
    • (2002) Circ Res , vol.90 , pp. 2-4
    • Epstein, S.E.1
  • 28
    • 70450189795 scopus 로고    scopus 로고
    • Inflammation in atherosclerosis: From pathophysiology to practice
    • Libby P, Ridker PM, Hansson GK, et al. Inflammation in atherosclerosis: from pathophysiology to practice. J Am Coll Cardiol 2009; 54: 2129-2138.
    • (2009) J Am Coll Cardiol , vol.54 , pp. 2129-2138
    • Libby, P.1    Ridker, P.M.2    Hansson, G.K.3
  • 29
    • 23944471031 scopus 로고    scopus 로고
    • Human atherosclerotic plaque contains viable invasive Actinobacillus actinomycetemcomitans and Porphyromonas gingivalis
    • Kozarov EV, Dorn BR, Shelburne CE, et al. Human atherosclerotic plaque contains viable invasive Actinobacillus actinomycetemcomitans and Porphyromonas gingivalis. Arterioscler Thromb Vasc Biol 2005; 25: e17-e18.
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. e17-e18
    • Kozarov, E.V.1    Dorn, B.R.2    Shelburne, C.E.3
  • 30
    • 0024511197 scopus 로고
    • Association between dental health and acute myocardial infarction
    • Mattila KJ, Nieminen MS, Valtonen VV, et al. Association between dental health and acute myocardial infarction. BMJ 1989; 298: 779-781.
    • (1989) BMJ , vol.298 , pp. 779-781
    • Mattila, K.J.1    Nieminen, M.S.2    Valtonen, V.V.3
  • 31
    • 27744573022 scopus 로고    scopus 로고
    • Defining the normal bacterial flora of the oral cavity
    • Aas JA, Paster BJ, Stokes LN, et al. Defining the normal bacterial flora of the oral cavity. J Clin Microbiol 2005; 43: 5721-5732.
    • (2005) J Clin Microbiol , vol.43 , pp. 5721-5732
    • Aas, J.A.1    Paster, B.J.2    Stokes, L.N.3
  • 32
    • 35448998937 scopus 로고    scopus 로고
    • The prevalence and incidence of coronary heart disease is significantly increased in periodontitis: A meta-analysis
    • Bahekar AA, Singh S, Saha S, et al. The prevalence and incidence of coronary heart disease is significantly increased in periodontitis: a meta-analysis. Am Heart J 2007; 154: 830-837.
    • (2007) Am Heart J , vol.154 , pp. 830-837
    • Bahekar, A.A.1    Singh, S.2    Saha, S.3
  • 33
    • 57249094305 scopus 로고    scopus 로고
    • Periodontal disease and coronary heart disease incidence: A systematic review and meta-analysis
    • Humphrey LL, Fu R, Buckley DI, et al. Periodontal disease and coronary heart disease incidence: a systematic review and meta-analysis. J Gen Intern Med 2008; 23: 2079-2086.
    • (2008) J Gen Intern Med , vol.23 , pp. 2079-2086
    • Humphrey, L.L.1    Fu, R.2    Buckley, D.I.3
  • 35
    • 4644287889 scopus 로고    scopus 로고
    • Periodontal diseases and the risk of coronary heart and cerebrovascular diseases: A meta-analysis
    • Khader YS, Albashaireh ZS, Alomari MA,. Periodontal diseases and the risk of coronary heart and cerebrovascular diseases: a meta-analysis. J Periodontol 2004; 75: 1046-1053.
    • (2004) J Periodontol , vol.75 , pp. 1046-1053
    • Khader, Y.S.1    Albashaireh, Z.S.2    Alomari, M.A.3
  • 36
    • 84877011268 scopus 로고    scopus 로고
    • Periodontitis and systemic diseases: A record of discussions of working group 4 of the Joint EFP/AAP Workshop on Periodontitis and Systemic Diseases
    • Group 4 Of Joint Efp/aap Workshop W (Suppl. 14)
    • Linden GJ, Herzberg MC, Working group 4 of joint EFP/AAP workshop,. Periodontitis and systemic diseases: a record of discussions of working group 4 of the Joint EFP/AAP Workshop on Periodontitis and Systemic Diseases. J Clin Periodontol 2013; 40 (Suppl. 14): S20-S23.
    • (2013) J Clin Periodontol , vol.40 , pp. S20-S23
    • Linden, G.J.1    Herzberg, M.C.2
  • 37
    • 84861336354 scopus 로고    scopus 로고
    • Periodontal disease and atherosclerotic vascular disease: Does the evidence support an independent association?: A scientific statement from the American Heart Association
    • Lockhart PB, Bolger AF, Papapanou PN, et al. Periodontal disease and atherosclerotic vascular disease: does the evidence support an independent association?: a scientific statement from the American Heart Association. Circulation 2012; 125: 2520-2544.
    • (2012) Circulation , vol.125 , pp. 2520-2544
    • Lockhart, P.B.1    Bolger, A.F.2    Papapanou, P.N.3
  • 38
    • 37649023661 scopus 로고    scopus 로고
    • Markers of systemic bacterial exposure in periodontal disease and cardiovascular disease risk: A systematic review and meta-analysis
    • Mustapha IZ, Debrey S, Oladubu M, et al. Markers of systemic bacterial exposure in periodontal disease and cardiovascular disease risk: a systematic review and meta-analysis. J Periodontol 2007; 78: 2289-2302.
    • (2007) J Periodontol , vol.78 , pp. 2289-2302
    • Mustapha, I.Z.1    Debrey, S.2    Oladubu, M.3
  • 39
    • 1442351868 scopus 로고    scopus 로고
    • Associations between periodontal disease and risk for atherosclerosis, cardiovascular disease, and stroke. A systematic review
    • Scannapieco FA, Bush RB, Paju S,. Associations between periodontal disease and risk for atherosclerosis, cardiovascular disease, and stroke. A systematic review. Ann Periodontol 2003; 8: 38-53.
    • (2003) Ann Periodontol , vol.8 , pp. 38-53
    • Scannapieco, F.A.1    Bush, R.B.2    Paju, S.3
  • 40
    • 80052649292 scopus 로고    scopus 로고
    • Periodontopathogen- and host-derived immune response in acute coronary syndrome
    • Alfakry H, Paju S, Sinisalo J, et al. Periodontopathogen- and host-derived immune response in acute coronary syndrome. Scand J Immunol 2011; 74: 383-389.
    • (2011) Scand J Immunol , vol.74 , pp. 383-389
    • Alfakry, H.1    Paju, S.2    Sinisalo, J.3
  • 41
    • 0033227214 scopus 로고    scopus 로고
    • Effect of periodontitis and smoking on blood leukocytes and acute-phase proteins
    • Fredriksson MI, Figueredo CM, Gustafsson A, et al. Effect of periodontitis and smoking on blood leukocytes and acute-phase proteins. J Periodontol 1999; 70: 1355-1360.
    • (1999) J Periodontol , vol.70 , pp. 1355-1360
    • Fredriksson, M.I.1    Figueredo, C.M.2    Gustafsson, A.3
  • 42
    • 15744389578 scopus 로고    scopus 로고
    • Molecular interactions between matrilysin and the matrix metalloproteinase inhibitor doxycycline investigated by deuterium exchange mass spectrometry
    • Garcia RA, Pantazatos DP, Gessner CR, et al. Molecular interactions between matrilysin and the matrix metalloproteinase inhibitor doxycycline investigated by deuterium exchange mass spectrometry. Mol Pharmacol 2005; 67: 1128-1136.
    • (2005) Mol Pharmacol , vol.67 , pp. 1128-1136
    • Garcia, R.A.1    Pantazatos, D.P.2    Gessner, C.R.3
  • 43
    • 79957969674 scopus 로고    scopus 로고
    • Mechanisms involved in the association between periodontal diseases and cardiovascular disease
    • Teles R, Wang CY,. Mechanisms involved in the association between periodontal diseases and cardiovascular disease. Oral Dis 2011; 17: 450-461.
    • (2011) Oral Dis , vol.17 , pp. 450-461
    • Teles, R.1    Wang, C.Y.2
  • 44
    • 84859364426 scopus 로고    scopus 로고
    • Recognition of Porphyromonas gingivalis gingipain epitopes by natural IgM binding to malondialdehyde modified low-density lipoprotein
    • Turunen SP, Kummu O, Harila K, et al. Recognition of Porphyromonas gingivalis gingipain epitopes by natural IgM binding to malondialdehyde modified low-density lipoprotein. PLoS One 2012; 7: e34910-e34910.
    • (2012) PLoS One , vol.7 , pp. e34910-e34910
    • Turunen, S.P.1    Kummu, O.2    Harila, K.3
  • 45
    • 70349434791 scopus 로고    scopus 로고
    • Periodontal treatment influences risk markers for atherosclerosis in patients with severe periodontitis
    • Buhlin K, Hultin M, Norderyd O, et al. Periodontal treatment influences risk markers for atherosclerosis in patients with severe periodontitis. Atherosclerosis 2009; 206: 518-522.
    • (2009) Atherosclerosis , vol.206 , pp. 518-522
    • Buhlin, K.1    Hultin, M.2    Norderyd, O.3
  • 46
    • 84877065825 scopus 로고    scopus 로고
    • Evidence that periodontal treatment improves biomarkers and CVD outcomes
    • D'Aiuto F, Orlandi M, Gunsolley JC,. Evidence that periodontal treatment improves biomarkers and CVD outcomes. J Periodontol 2013; 84: S85-S105.
    • (2013) J Periodontol , vol.84 , pp. S85-S105
    • D'Aiuto, F.1    Orlandi, M.2    Gunsolley, J.C.3
  • 47
    • 84890548357 scopus 로고    scopus 로고
    • Treatment of periodontitis improves the atherosclerotic profile: A systematic review and meta-analysis
    • Teeuw WJ, Slot DE, Susanto H, et al. Treatment of periodontitis improves the atherosclerotic profile: a systematic review and meta-analysis. J Clin Periodontol 2014; 41: 70-79.
    • (2014) J Clin Periodontol , vol.41 , pp. 70-79
    • Teeuw, W.J.1    Slot, D.E.2    Susanto, H.3
  • 48
    • 53049095044 scopus 로고    scopus 로고
    • Update on bacteraemia related to dental procedures
    • Olsen I,. Update on bacteraemia related to dental procedures. Transfus Apher Sci 2008; 39: 173-178.
    • (2008) Transfus Apher Sci , vol.39 , pp. 173-178
    • Olsen, I.1
  • 50
    • 84901624762 scopus 로고    scopus 로고
    • Dissemination of periodontal pathogens in the bloodstream after periodontal procedures: A systematic review
    • Horliana AC, Chambrone L, Foz AM, et al. Dissemination of periodontal pathogens in the bloodstream after periodontal procedures: a systematic review. PLoS One 2014; 9: e98271-e98271.
    • (2014) PLoS One , vol.9 , pp. e98271-e98271
    • Horliana, A.C.1    Chambrone, L.2    Foz, A.M.3
  • 51
    • 80051553681 scopus 로고    scopus 로고
    • Impact of monocytic cells on recovery of uncultivable bacteria from atherosclerotic lesions
    • Rafferty B, Jonsson D, Kalachikov S, et al. Impact of monocytic cells on recovery of uncultivable bacteria from atherosclerotic lesions. J Intern Med 2011; 270: 273-280.
    • (2011) J Intern Med , vol.270 , pp. 273-280
    • Rafferty, B.1    Jonsson, D.2    Kalachikov, S.3
  • 52
    • 0034305658 scopus 로고    scopus 로고
    • Identification of periodontal pathogens in atheromatous plaques
    • Haraszthy VI, Zambon JJ, Trevisan M, et al. Identification of periodontal pathogens in atheromatous plaques. J Periodontol 2000; 71: 1554-1560.
    • (2000) J Periodontol , vol.71 , pp. 1554-1560
    • Haraszthy, V.I.1    Zambon, J.J.2    Trevisan, M.3
  • 53
    • 84555190776 scopus 로고    scopus 로고
    • Bacterial invasion of vascular cell types: Vascular infectology and atherogenesis
    • Kozarov E,. Bacterial invasion of vascular cell types: vascular infectology and atherogenesis. Future Cardiol 2012; 8: 123-138.
    • (2012) Future Cardiol , vol.8 , pp. 123-138
    • Kozarov, E.1
  • 54
    • 84877012129 scopus 로고    scopus 로고
    • Periodontal bacterial invasion and infection: Contribution to atherosclerotic pathology
    • (Suppl. 14)
    • Reyes L, Herrera D, Kozarov E, et al. Periodontal bacterial invasion and infection: contribution to atherosclerotic pathology. J Clin Periodontol 2013; 40 (Suppl. 14): S30-S50.
    • (2013) J Clin Periodontol , vol.40 , pp. S30-S50
    • Reyes, L.1    Herrera, D.2    Kozarov, E.3
  • 55
    • 0034304221 scopus 로고    scopus 로고
    • Elevation of systemic markers related to cardiovascular diseases in the peripheral blood of periodontitis patients
    • Loos BG, Craandijk J, Hoek FJ, et al. Elevation of systemic markers related to cardiovascular diseases in the peripheral blood of periodontitis patients. J Periodontol 2000; 71: 1528-1534.
    • (2000) J Periodontol , vol.71 , pp. 1528-1534
    • Loos, B.G.1    Craandijk, J.2    Hoek, F.J.3
  • 56
    • 0035459554 scopus 로고    scopus 로고
    • Periodontal infections contribute to elevated systemic C-reactive protein level
    • Noack B, Genco RJ, Trevisan M, et al. Periodontal infections contribute to elevated systemic C-reactive protein level. J Periodontol 2001; 72: 1221-1227.
    • (2001) J Periodontol , vol.72 , pp. 1221-1227
    • Noack, B.1    Genco, R.J.2    Trevisan, M.3
  • 57
    • 35448957718 scopus 로고    scopus 로고
    • Serum microbial- and host-derived markers of periodontal diseases: A review
    • Pussinen PJ, Paju S, Mäntyla P, et al. Serum microbial- and host-derived markers of periodontal diseases: a review. Curr Med Chem 2007; 14: 2402-2412.
    • (2007) Curr Med Chem , vol.14 , pp. 2402-2412
    • Pussinen, P.J.1    Paju, S.2    Mäntyla, P.3
  • 58
    • 84877038665 scopus 로고    scopus 로고
    • Inflammatory mechanisms linking periodontal diseases to cardiovascular diseases
    • (Suppl. 14)
    • Schenkein HA, Loos BG,. Inflammatory mechanisms linking periodontal diseases to cardiovascular diseases. J Clin Periodontol 2013; 40 (Suppl. 14): S51-S69.
    • (2013) J Clin Periodontol , vol.40 , pp. S51-S69
    • Schenkein, H.A.1    Loos, B.G.2
  • 59
    • 79953144925 scopus 로고    scopus 로고
    • Cardiovascular disease and the role of oral bacteria
    • Leishman SJ, Do HL, Ford PJ,. Cardiovascular disease and the role of oral bacteria. J Oral Microbiol 2010; 2: 1-13.
    • (2010) J Oral Microbiol , vol.2 , pp. 1-13
    • Leishman, S.J.1    Do, H.L.2    Ford, P.J.3
  • 60
    • 0842326172 scopus 로고    scopus 로고
    • Periodontitis decreases the antiatherogenic potency of high density lipoprotein
    • Pussinen PJ, Jauhiainen M, Vilkuna-Rautiainen T, et al. Periodontitis decreases the antiatherogenic potency of high density lipoprotein. J Lipid Res 2004; 45: 139-147.
    • (2004) J Lipid Res , vol.45 , pp. 139-147
    • Pussinen, P.J.1    Jauhiainen, M.2    Vilkuna-Rautiainen, T.3
  • 61
    • 33750564770 scopus 로고    scopus 로고
    • Reactions of myeloperoxidase-derived oxidants with biological substrates: Gaining chemical insight into human inflammatory diseases
    • Pattison DI, Davies MJ,. Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases. Curr Med Chem 2006; 13: 3271-3290.
    • (2006) Curr Med Chem , vol.13 , pp. 3271-3290
    • Pattison, D.I.1    Davies, M.J.2
  • 62
    • 0028292033 scopus 로고
    • Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions
    • Daugherty A, Dunn JL, Rateri DL, et al. Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions. J Clin Invest 1994; 94: 437-444.
    • (1994) J Clin Invest , vol.94 , pp. 437-444
    • Daugherty, A.1    Dunn, J.L.2    Rateri, D.L.3
  • 63
    • 0035861922 scopus 로고    scopus 로고
    • Hypochlorite-modified (lipo)proteins are present in rabbit lesions in response to dietary cholesterol
    • Malle E, Wag G, Thiery J, et al. Hypochlorite-modified (lipo)proteins are present in rabbit lesions in response to dietary cholesterol. Biochem Biophys Res Commun 2001; 289: 894-900.
    • (2001) Biochem Biophys Res Commun , vol.289 , pp. 894-900
    • Malle, E.1    Wag, G.2    Thiery, J.3
  • 64
    • 0001059250 scopus 로고    scopus 로고
    • 2/halide system in human atherosclerotic lesions: Colocalization of myeloperoxidase and hypochlorite-modified proteins
    • 2/halide system in human atherosclerotic lesions: colocalization of myeloperoxidase and hypochlorite-modified proteins. Eur J Biochem 2000; 267: 4495-4503.
    • (2000) Eur J Biochem , vol.267 , pp. 4495-4503
    • Malle, E.1    Waeg, G.2    Schreiber, R.3
  • 65
    • 0031024294 scopus 로고    scopus 로고
    • Immunological evidence for hypochlorite-modified proteins in human kidney
    • Malle E, Woenckhaus C, Waeg G, et al. Immunological evidence for hypochlorite-modified proteins in human kidney. Am J Pathol 1997; 150: 603-615.
    • (1997) Am J Pathol , vol.150 , pp. 603-615
    • Malle, E.1    Woenckhaus, C.2    Waeg, G.3
  • 66
    • 0036143434 scopus 로고    scopus 로고
    • Immunohistochemical detection of hypochlorite-modified proteins in glomeruli of human membranous glomerulonephritis
    • Grone HJ, Grone EF, Malle E,. Immunohistochemical detection of hypochlorite-modified proteins in glomeruli of human membranous glomerulonephritis. Lab Invest 2002; 82: 5-14.
    • (2002) Lab Invest , vol.82 , pp. 5-14
    • Grone, H.J.1    Grone, E.F.2    Malle, E.3
  • 67
    • 0344514747 scopus 로고    scopus 로고
    • Myeloperoxidase in kidney disease
    • Malle E, Buch T, Grone HJ,. Myeloperoxidase in kidney disease. Kidney Int 2003; 64: 1956-1967.
    • (2003) Kidney Int , vol.64 , pp. 1956-1967
    • Malle, E.1    Buch, T.2    Grone, H.J.3
  • 68
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase H, Visse R, Murphy G,. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 2006; 69: 562-573.
    • (2006) Cardiovasc Res , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 69
    • 33748638853 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Contribution to pathogenesis, diagnosis and treatment of periodontal inflammation
    • Sorsa T, Tjäderhane L, Konttinen YT, et al. Matrix metalloproteinases: contribution to pathogenesis, diagnosis and treatment of periodontal inflammation. Ann Med 2006; 38: 306-321.
    • (2006) Ann Med , vol.38 , pp. 306-321
    • Sorsa, T.1    Tjäderhane, L.2    Konttinen, Y.T.3
  • 70
    • 9444232274 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) in oral diseases
    • Sorsa T, Tjäderhane L, Salo T,. Matrix metalloproteinases (MMPs) in oral diseases. Oral Dis 2004; 10: 311-318.
    • (2004) Oral Dis , vol.10 , pp. 311-318
    • Sorsa, T.1    Tjäderhane, L.2    Salo, T.3
  • 71
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • Visse R, Nagase H,. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res 2003; 92: 827-839.
    • (2003) Circ Res , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 72
    • 84942818262 scopus 로고    scopus 로고
    • Matrix metalloproteinases in inflammation
    • Nissinen L, Kahari VM,. Matrix metalloproteinases in inflammation. Biochim Biophys Acta 2014; 1840: 2571-2580.
    • (2014) Biochim Biophys Acta , vol.1840 , pp. 2571-2580
    • Nissinen, L.1    Kahari, V.M.2
  • 73
    • 15444347160 scopus 로고    scopus 로고
    • Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells. Regulation by tumor necrosis factor-alpha and doxycycline
    • Hanemaaijer R, Sorsa T, Konttinen YT, et al. Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells. Regulation by tumor necrosis factor-alpha and doxycycline. J Biol Chem 1997; 272: 31504-31509.
    • (1997) J Biol Chem , vol.272 , pp. 31504-31509
    • Hanemaaijer, R.1    Sorsa, T.2    Konttinen, Y.T.3
  • 74
    • 0034993141 scopus 로고    scopus 로고
    • In vivo collagenase-2 (MMP-8) expression by human bronchial epithelial cells and monocytes/macrophages in bronchiectasis
    • Prikk K, Maisi P, Pirilä E, et al. In vivo collagenase-2 (MMP-8) expression by human bronchial epithelial cells and monocytes/macrophages in bronchiectasis. J Pathol 2001; 194: 232-238.
    • (2001) J Pathol , vol.194 , pp. 232-238
    • Prikk, K.1    Maisi, P.2    Pirilä, E.3
  • 75
    • 84983157331 scopus 로고    scopus 로고
    • Expression and induction of collagenases (MMP-8 and -13) in plasma cells associated with bone-destructive lesions
    • Wahlgren J, Maisi P, Sorsa T, et al. Expression and induction of collagenases (MMP-8 and -13) in plasma cells associated with bone-destructive lesions. J Pathol 2001; 194: 217-224.
    • (2001) J Pathol , vol.194 , pp. 217-224
    • Wahlgren, J.1    Maisi, P.2    Sorsa, T.3
  • 76
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss SJ,. Tissue destruction by neutrophils. N Engl J Med 1989; 320: 365-376.
    • (1989) N Engl J Med , vol.320 , pp. 365-376
    • Weiss, S.J.1
  • 77
    • 15244338619 scopus 로고    scopus 로고
    • Collagenases in cancer
    • Ala-aho R, Kahari VM,. Collagenases in cancer. Biochimie 2005; 87: 273-286.
    • (2005) Biochimie , vol.87 , pp. 273-286
    • Ala-Aho, R.1    Kahari, V.M.2
  • 78
    • 0023202438 scopus 로고
    • The collagen substrate specificity of human neutrophil collagenase
    • Hasty KA, Jeffrey JJ, Hibbs MS, et al. The collagen substrate specificity of human neutrophil collagenase. J Biol Chem 1987; 262: 10048-10052.
    • (1987) J Biol Chem , vol.262 , pp. 10048-10052
    • Hasty, K.A.1    Jeffrey, J.J.2    Hibbs, M.S.3
  • 79
    • 0033056463 scopus 로고    scopus 로고
    • The cell biology of leukocyte-mediated proteolysis
    • Owen CA, Campbell EJ,. The cell biology of leukocyte-mediated proteolysis. J Leukoc Biol 1999; 65: 137-150.
    • (1999) J Leukoc Biol , vol.65 , pp. 137-150
    • Owen, C.A.1    Campbell, E.J.2
  • 80
    • 33646171585 scopus 로고    scopus 로고
    • Collagenases in gingival crevicular fluid in type 1 diabetes mellitus
    • Safkan-Seppalä B, Sorsa T, Tervahartiala T, et al. Collagenases in gingival crevicular fluid in type 1 diabetes mellitus. J Periodontol 2006; 77: 189-194.
    • (2006) J Periodontol , vol.77 , pp. 189-194
    • Safkan-Seppalä, B.1    Sorsa, T.2    Tervahartiala, T.3
  • 81
    • 0035899898 scopus 로고    scopus 로고
    • Expression of neutrophil collagenase (matrix metalloproteinase-8) in human atheroma: A novel collagenolytic pathway suggested by transcriptional profiling
    • Herman MP, Sukhova GK, Libby P, et al. Expression of neutrophil collagenase (matrix metalloproteinase-8) in human atheroma: a novel collagenolytic pathway suggested by transcriptional profiling. Circulation 2001; 104: 1899-1904.
    • (2001) Circulation , vol.104 , pp. 1899-1904
    • Herman, M.P.1    Sukhova, G.K.2    Libby, P.3
  • 82
    • 84931362972 scopus 로고    scopus 로고
    • Matrix metalloproteinase 8 degrades apolipoprotein A-I and reduces its cholesterol efflux capacity
    • Salminen A, Åstrom P, Metso J, et al. Matrix metalloproteinase 8 degrades apolipoprotein A-I and reduces its cholesterol efflux capacity. FASEB J 2015; 29: 1435-1445.
    • (2015) FASEB J , vol.29 , pp. 1435-1445
    • Salminen, A.1    Åstrom, P.2    Metso, J.3
  • 83
    • 3242691404 scopus 로고    scopus 로고
    • Unstable carotid plaques exhibit raised matrix metalloproteinase-8 activity
    • Molloy KJ, Thompson MM, Jones JL, et al. Unstable carotid plaques exhibit raised matrix metalloproteinase-8 activity. Circulation 2004; 110: 337-343.
    • (2004) Circulation , vol.110 , pp. 337-343
    • Molloy, K.J.1    Thompson, M.M.2    Jones, J.L.3
  • 84
    • 33644874476 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 is associated with stable and matrix metalloproteinases 8 and 9 with vulnerable carotid atherosclerotic lesions: A study in human endarterectomy specimen pointing to a role for different extracellular matrix metalloproteinase inducer glycosylation forms
    • Sluijter JP, Pulskens WP, Schoneveld AH, et al. Matrix metalloproteinase 2 is associated with stable and matrix metalloproteinases 8 and 9 with vulnerable carotid atherosclerotic lesions: a study in human endarterectomy specimen pointing to a role for different extracellular matrix metalloproteinase inducer glycosylation forms. Stroke 2006; 37: 235-239.
    • (2006) Stroke , vol.37 , pp. 235-239
    • Sluijter, J.P.1    Pulskens, W.P.2    Schoneveld, A.H.3
  • 85
    • 79251644601 scopus 로고    scopus 로고
    • Collagenase-2 (MMP-8) as a point-of-care biomarker in periodontitis and cardiovascular diseases. Therapeutic response to non-antimicrobial properties of tetracyclines
    • Sorsa T, Tervahartiala T, Leppilahti J, et al. Collagenase-2 (MMP-8) as a point-of-care biomarker in periodontitis and cardiovascular diseases. Therapeutic response to non-antimicrobial properties of tetracyclines. Pharmacol Res 2011; 63: 108-113.
    • (2011) Pharmacol Res , vol.63 , pp. 108-113
    • Sorsa, T.1    Tervahartiala, T.2    Leppilahti, J.3
  • 86
    • 57149094082 scopus 로고    scopus 로고
    • Increased matrix metalloproteinase-8 and -9 activity in patients with infarct rupture after myocardial infarction
    • van den Borne SW, Cleutjens JP, Hanemaaijer R, et al. Increased matrix metalloproteinase-8 and -9 activity in patients with infarct rupture after myocardial infarction. Cardiovasc Pathol 2009; 18: 37-43.
    • (2009) Cardiovasc Pathol , vol.18 , pp. 37-43
    • Van Den Borne, S.W.1    Cleutjens, J.P.2    Hanemaaijer, R.3
  • 87
    • 0028944471 scopus 로고
    • Enhanced expression of vascular matrix metalloproteinases induced in vitro by cytokines and in regions of human atherosclerotic lesions
    • Galis ZS, Muszynski M, Sukhova GK, et al. Enhanced expression of vascular matrix metalloproteinases induced in vitro by cytokines and in regions of human atherosclerotic lesions. Ann N Y Acad Sci 1995; 748: 501-507.
    • (1995) Ann N y Acad Sci , vol.748 , pp. 501-507
    • Galis, Z.S.1    Muszynski, M.2    Sukhova, G.K.3
  • 88
    • 0028063408 scopus 로고
    • Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques
    • Galis ZS, Sukhova GK, Lark MW, et al. Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques. J Clin Invest 1994; 94: 2493-2503.
    • (1994) J Clin Invest , vol.94 , pp. 2493-2503
    • Galis, Z.S.1    Sukhova, G.K.2    Lark, M.W.3
  • 89
    • 33744526254 scopus 로고    scopus 로고
    • Intraplaque MMP-8 levels are increased in asymptomatic patients with carotid plaque progression on ultrasound
    • Turu MM, Krupinski J, Catena E, et al. Intraplaque MMP-8 levels are increased in asymptomatic patients with carotid plaque progression on ultrasound. Atherosclerosis 2006; 187: 161-169.
    • (2006) Atherosclerosis , vol.187 , pp. 161-169
    • Turu, M.M.1    Krupinski, J.2    Catena, E.3
  • 90
    • 77049109629 scopus 로고    scopus 로고
    • High plasma levels of matrix metalloproteinase-8 in patients with unstable angina
    • Momiyama Y, Ohmori R, Tanaka N, et al. High plasma levels of matrix metalloproteinase-8 in patients with unstable angina. Atherosclerosis 2010; 209: 206-210.
    • (2010) Atherosclerosis , vol.209 , pp. 206-210
    • Momiyama, Y.1    Ohmori, R.2    Tanaka, N.3
  • 91
    • 27744591678 scopus 로고    scopus 로고
    • Plasma matrix metalloproteinase-8 concentrations are associated with the presence and severity of coronary artery disease
    • Kato R, Momiyama Y, Ohmori R, et al. Plasma matrix metalloproteinase-8 concentrations are associated with the presence and severity of coronary artery disease. Circ J 2005; 69: 1035-1040.
    • (2005) Circ J , vol.69 , pp. 1035-1040
    • Kato, R.1    Momiyama, Y.2    Ohmori, R.3
  • 92
    • 61849120499 scopus 로고    scopus 로고
    • Implications of serum matrix metalloproteinase-8 elevation in patients with acute coronary syndrome
    • Qiang H, Zhou ZX, Ma AQ, et al. [Implications of serum matrix metalloproteinase-8 elevation in patients with acute coronary syndrome]. Nan Fang Yi Ke Da Xue Xue Bao 2007; 27: 831-833.
    • (2007) Nan Fang Yi Ke da Xue Xue Bao , vol.27 , pp. 831-833
    • Qiang, H.1    Zhou, Z.X.2    Ma, A.Q.3
  • 93
    • 84879069722 scopus 로고    scopus 로고
    • The balance of serum matrix metalloproteinase-8 and its tissue inhibitor in acute coronary syndrome and its recurrence
    • Pussinen PJ, Sarna S, Puolakkainen M, et al. The balance of serum matrix metalloproteinase-8 and its tissue inhibitor in acute coronary syndrome and its recurrence. Int J Cardiol 2013; 167: 362-368.
    • (2013) Int J Cardiol , vol.167 , pp. 362-368
    • Pussinen, P.J.1    Sarna, S.2    Puolakkainen, M.3
  • 94
    • 84902595154 scopus 로고    scopus 로고
    • Serum tissue-degrading proteinases and incident cardiovascular disease events
    • Tuomainen AM, Kormi I, Havulinna AS, et al. Serum tissue-degrading proteinases and incident cardiovascular disease events. Eur J Prev Cardiol 2014; 21: 806-812.
    • (2014) Eur J Prev Cardiol , vol.21 , pp. 806-812
    • Tuomainen, A.M.1    Kormi, I.2    Havulinna, A.S.3
  • 95
    • 36348991408 scopus 로고    scopus 로고
    • Serum matrix metalloproteinase-8 concentrations are associated with cardiovascular outcome in men
    • Tuomainen AM, Nyyssonen K, Laukkanen JA, et al. Serum matrix metalloproteinase-8 concentrations are associated with cardiovascular outcome in men. Arterioscler Thromb Vasc Biol 2007; 27: 2722-2728.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 2722-2728
    • Tuomainen, A.M.1    Nyyssonen, K.2    Laukkanen, J.A.3
  • 96
    • 84856492152 scopus 로고    scopus 로고
    • Serum matrix metalloproteinases in patients resuscitated from cardiac arrest. The association with therapeutic hypothermia
    • Hastbacka J, Tiainen M, Hynninen M, et al. Serum matrix metalloproteinases in patients resuscitated from cardiac arrest. The association with therapeutic hypothermia. Resuscitation 2012; 83: 197-201.
    • (2012) Resuscitation , vol.83 , pp. 197-201
    • Hastbacka, J.1    Tiainen, M.2    Hynninen, M.3
  • 97
    • 0037809423 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinase-8 by membrane type 1-MMP and their expression in human tears after photorefractive keratectomy
    • Holopainen JM, Moilanen JA, Sorsa T, et al. Activation of matrix metalloproteinase-8 by membrane type 1-MMP and their expression in human tears after photorefractive keratectomy. Invest Ophthalmol Vis Sci 2003; 44: 2550-2556.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 2550-2556
    • Holopainen, J.M.1    Moilanen, J.A.2    Sorsa, T.3
  • 98
    • 0025106479 scopus 로고
    • Activation of latent human neutrophil collagenase by reactive oxygen species and serine proteases
    • Saari H, Suomalainen K, Lindy O, et al. Activation of latent human neutrophil collagenase by reactive oxygen species and serine proteases. Biochem Biophys Res Commun 1990; 171: 979-987.
    • (1990) Biochem Biophys Res Commun , vol.171 , pp. 979-987
    • Saari, H.1    Suomalainen, K.2    Lindy, O.3
  • 99
    • 0026495127 scopus 로고
    • Identification of proteases from periodontopathogenic bacteria as activators of latent human neutrophil and fibroblast-type interstitial collagenases
    • Sorsa T, Ingman T, Suomalainen K, et al. Identification of proteases from periodontopathogenic bacteria as activators of latent human neutrophil and fibroblast-type interstitial collagenases. Infect Immun 1992; 60: 4491-4495.
    • (1992) Infect Immun , vol.60 , pp. 4491-4495
    • Sorsa, T.1    Ingman, T.2    Suomalainen, K.3
  • 100
    • 84902584749 scopus 로고    scopus 로고
    • Biomarkers of periodontitis and inflammation in ischemic stroke: A case-control study
    • Palm F, Lahdentausta L, Sorsa T, et al. Biomarkers of periodontitis and inflammation in ischemic stroke: A case-control study. Innate Immun 2014; 20: 511-518.
    • (2014) Innate Immun , vol.20 , pp. 511-518
    • Palm, F.1    Lahdentausta, L.2    Sorsa, T.3
  • 101
    • 78249233559 scopus 로고    scopus 로고
    • Associations between matrix metalloproteinase-8 and -14 and myeloperoxidase in gingival crevicular fluid from subjects with progressive chronic periodontitis: A longitudinal study
    • Hernandez M, Gamonal J, Tervahartiala T, et al. Associations between matrix metalloproteinase-8 and -14 and myeloperoxidase in gingival crevicular fluid from subjects with progressive chronic periodontitis: a longitudinal study. J Periodontol 2010; 81: 1644-1652.
    • (2010) J Periodontol , vol.81 , pp. 1644-1652
    • Hernandez, M.1    Gamonal, J.2    Tervahartiala, T.3
  • 102
    • 84893860600 scopus 로고    scopus 로고
    • Gingival crevicular fluid matrix metalloproteinase-8 levels predict treatment outcome among smokers with chronic periodontitis
    • Leppilahti JM, Kallio MA, Tervahartiala T, et al. Gingival crevicular fluid matrix metalloproteinase-8 levels predict treatment outcome among smokers with chronic periodontitis. J Periodontol 2014; 85: 250-260.
    • (2014) J Periodontol , vol.85 , pp. 250-260
    • Leppilahti, J.M.1    Kallio, M.A.2    Tervahartiala, T.3
  • 103
    • 33750473680 scopus 로고    scopus 로고
    • Monitoring periodontal disease status in smokers and nonsmokers using a gingival crevicular fluid matrix metalloproteinase-8-specific chair-side test
    • Mäntyla P, Stenman M, Kinane D, et al. Monitoring periodontal disease status in smokers and nonsmokers using a gingival crevicular fluid matrix metalloproteinase-8-specific chair-side test. J Periodontal Res 2006; 41: 503-512.
    • (2006) J Periodontal Res , vol.41 , pp. 503-512
    • Mäntyla, P.1    Stenman, M.2    Kinane, D.3
  • 104
    • 0141560401 scopus 로고    scopus 로고
    • Gingival crevicular fluid collagenase-2 (MMP-8) test stick for chair-side monitoring of periodontitis
    • Mäntyla P, Stenman M, Kinane DF, et al. Gingival crevicular fluid collagenase-2 (MMP-8) test stick for chair-side monitoring of periodontitis. J Periodontal Res 2003; 38: 436-439.
    • (2003) J Periodontal Res , vol.38 , pp. 436-439
    • Mäntyla, P.1    Stenman, M.2    Kinane, D.F.3
  • 105
    • 74049098607 scopus 로고    scopus 로고
    • Gingival crevicular fluid levels of MMP-8, MMP-9, TIMP-2, and MPO decrease after periodontal therapy
    • Marcaccini AM, Meschiari CA, Zuardi LR, et al. Gingival crevicular fluid levels of MMP-8, MMP-9, TIMP-2, and MPO decrease after periodontal therapy. J Clin Periodontol 2010; 37: 180-190.
    • (2010) J Clin Periodontol , vol.37 , pp. 180-190
    • Marcaccini, A.M.1    Meschiari, C.A.2    Zuardi, L.R.3
  • 106
    • 70349835147 scopus 로고    scopus 로고
    • Circulating matrix metalloproteinase-8 (MMP-8) and MMP-9 are increased in chronic periodontal disease and decrease after non-surgical periodontal therapy
    • Marcaccini AM, Novaes AB Jr, Meschiari CA, et al. Circulating matrix metalloproteinase-8 (MMP-8) and MMP-9 are increased in chronic periodontal disease and decrease after non-surgical periodontal therapy. Clin Chim Acta 2009; 409: 117-122.
    • (2009) Clin Chim Acta , vol.409 , pp. 117-122
    • Marcaccini, A.M.1    Novaes, A.B.J.2    Meschiari, C.A.3
  • 107
    • 4344715562 scopus 로고    scopus 로고
    • Can nonstandardized bitewing radiographs be used to assess the presence of alveolar bone loss in epidemiologic studies?
    • Merchant AT, Pitiphat W, Parker J, et al. Can nonstandardized bitewing radiographs be used to assess the presence of alveolar bone loss in epidemiologic studies? Community Dent Oral Epidemiol 2004; 32: 271-276.
    • (2004) Community Dent Oral Epidemiol , vol.32 , pp. 271-276
    • Merchant, A.T.1    Pitiphat, W.2    Parker, J.3
  • 108
    • 33845655552 scopus 로고    scopus 로고
    • Handling anticancer drugs: From hazard identification to risk management?
    • Sorsa M, Hameila M, Järviluoma E,. Handling anticancer drugs: from hazard identification to risk management? Ann N Y Acad Sci 2006; 1076: 628-634.
    • (2006) Ann N y Acad Sci , vol.1076 , pp. 628-634
    • Sorsa, M.1    Hameila, M.2    Järviluoma, E.3
  • 109
    • 73649134293 scopus 로고    scopus 로고
    • Detection of gingival crevicular fluid MMP-8 levels with different laboratory and chair-side methods
    • Sorsa T, Hernandez M, Leppilahti J, et al. Detection of gingival crevicular fluid MMP-8 levels with different laboratory and chair-side methods. Oral Dis 2010; 16: 39-45.
    • (2010) Oral Dis , vol.16 , pp. 39-45
    • Sorsa, T.1    Hernandez, M.2    Leppilahti, J.3
  • 110
    • 49149123468 scopus 로고    scopus 로고
    • Subantimicrobial-dose doxycycline modulates gingival crevicular fluid biomarkers of periodontitis in postmenopausal osteopenic women
    • Golub LM, Lee HM, Stoner JA, et al. Subantimicrobial-dose doxycycline modulates gingival crevicular fluid biomarkers of periodontitis in postmenopausal osteopenic women. J Periodontol 2008; 79: 1409-1418.
    • (2008) J Periodontol , vol.79 , pp. 1409-1418
    • Golub, L.M.1    Lee, H.M.2    Stoner, J.A.3
  • 111
    • 10744232672 scopus 로고    scopus 로고
    • Levels and molecular forms of MMP-7 (matrilysin-1) and MMP-8 (collagenase-2) in diseased human peri-implant sulcular fluid
    • Kivelä-Rajamaki M, Maisi P, Srinivas R, et al. Levels and molecular forms of MMP-7 (matrilysin-1) and MMP-8 (collagenase-2) in diseased human peri-implant sulcular fluid. J Periodontal Res 2003; 38: 583-590.
    • (2003) J Periodontal Res , vol.38 , pp. 583-590
    • Kivelä-Rajamaki, M.1    Maisi, P.2    Srinivas, R.3
  • 112
    • 78650892992 scopus 로고    scopus 로고
    • Reduced expression of lipopolysaccharide-induced CXC chemokine in Porphyromonas gingivalis-induced experimental periodontitis in matrix metalloproteinase-8 null mice
    • Hernandez M, Gamonal J, Salo T, et al. Reduced expression of lipopolysaccharide-induced CXC chemokine in Porphyromonas gingivalis-induced experimental periodontitis in matrix metalloproteinase-8 null mice. J Periodontal Res 2011; 46: 58-66.
    • (2011) J Periodontal Res , vol.46 , pp. 58-66
    • Hernandez, M.1    Gamonal, J.2    Salo, T.3
  • 113
    • 60549109675 scopus 로고    scopus 로고
    • Local and systemic responses in matrix metalloproteinase 8-deficient mice during Porphyromonas gingivalis -induced periodontitis
    • Kuula H, Salo T, Pirilä E, et al. Local and systemic responses in matrix metalloproteinase 8-deficient mice during Porphyromonas gingivalis -induced periodontitis. Infect Immun 2009; 77: 850-859.
    • (2009) Infect Immun , vol.77 , pp. 850-859
    • Kuula, H.1    Salo, T.2    Pirilä, E.3
  • 114
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht MD, Werb Z,. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 2001; 17: 463-516.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 115
    • 0032696699 scopus 로고    scopus 로고
    • Matrix metalloproteinase system deficiencies and matrix degradation
    • Lijnen HR, Collen D,. Matrix metalloproteinase system deficiencies and matrix degradation. Thromb Haemost 1999; 82: 837-845.
    • (1999) Thromb Haemost , vol.82 , pp. 837-845
    • Lijnen, H.R.1    Collen, D.2
  • 116
    • 0026681802 scopus 로고
    • Neutrophil elastase in respiratory epithelial lining fluid of individuals with cystic fibrosis induces interleukin-8 gene expression in a human bronchial epithelial cell line
    • Nakamura H, Yoshimura K, McElvaney NG, et al. Neutrophil elastase in respiratory epithelial lining fluid of individuals with cystic fibrosis induces interleukin-8 gene expression in a human bronchial epithelial cell line. J Clin Invest 1992; 89: 1478-1484.
    • (1992) J Clin Invest , vol.89 , pp. 1478-1484
    • Nakamura, H.1    Yoshimura, K.2    McElvaney, N.G.3
  • 117
    • 0026795140 scopus 로고
    • Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties
    • Okada Y, Gonoji Y, Naka K, et al. Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties. J Biol Chem 1992; 267: 21712-21719.
    • (1992) J Biol Chem , vol.267 , pp. 21712-21719
    • Okada, Y.1    Gonoji, Y.2    Naka, K.3
  • 120
    • 0027730572 scopus 로고
    • 92-kd gelatinase is actively expressed by eosinophils and stored by neutrophils in squamous cell carcinoma
    • Stahle-Backdahl M, Parks WC,. 92-kd gelatinase is actively expressed by eosinophils and stored by neutrophils in squamous cell carcinoma. Am J Pathol 1993; 142: 995-1000.
    • (1993) Am J Pathol , vol.142 , pp. 995-1000
    • Stahle-Backdahl, M.1    Parks, W.C.2
  • 121
    • 0035076487 scopus 로고    scopus 로고
    • Matrix metalloproteinase and proinflammatory cytokine production by chondrocytes of human osteoarthritic cartilage: Associations with degenerative changes
    • Tetlow LC, Adlam DJ, Woolley DE,. Matrix metalloproteinase and proinflammatory cytokine production by chondrocytes of human osteoarthritic cartilage: associations with degenerative changes. Arthritis Rheum 2001; 44: 585-594.
    • (2001) Arthritis Rheum , vol.44 , pp. 585-594
    • Tetlow, L.C.1    Adlam, D.J.2    Woolley, D.E.3
  • 122
    • 0038059516 scopus 로고    scopus 로고
    • Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9)
    • Van den Steen PE, Dubois B, Nelissen I, et al. Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9). Crit Rev Biochem Mol Biol 2002; 37: 375-536.
    • (2002) Crit Rev Biochem Mol Biol , vol.37 , pp. 375-536
    • Van Den Steen, P.E.1    Dubois, B.2    Nelissen, I.3
  • 123
    • 0027601224 scopus 로고
    • Role of matrix metalloproteinases in human periodontal diseases
    • Birkedal-Hansen H,. Role of matrix metalloproteinases in human periodontal diseases. J Periodontol 1993; 64: 474-484.
    • (1993) J Periodontol , vol.64 , pp. 474-484
    • Birkedal-Hansen, H.1
  • 124
    • 25444533295 scopus 로고    scopus 로고
    • The paradox of matrix metalloproteinases in infectious disease
    • Elkington PT, O'Kane CM, Friedland JS,. The paradox of matrix metalloproteinases in infectious disease. Clin Exp Immunol 2005; 142: 12-20.
    • (2005) Clin Exp Immunol , vol.142 , pp. 12-20
    • Elkington, P.T.1    O'Kane, C.M.2    Friedland, J.S.3
  • 125
    • 0030307324 scopus 로고    scopus 로고
    • Human neutrophil gelatinase and associated lipocalin in adult and localized juvenile periodontitis
    • Westerlund U, Ingman T, Lukinmaa PL, et al. Human neutrophil gelatinase and associated lipocalin in adult and localized juvenile periodontitis. J Dent Res 1996; 75: 1553-1563.
    • (1996) J Dent Res , vol.75 , pp. 1553-1563
    • Westerlund, U.1    Ingman, T.2    Lukinmaa, P.L.3
  • 126
    • 0024330327 scopus 로고
    • SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages
    • Wilhelm SM, Collier IE, Marmer BL, et al. SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J Biol Chem 1989; 264: 17213-17221.
    • (1989) J Biol Chem , vol.264 , pp. 17213-17221
    • Wilhelm, S.M.1    Collier, I.E.2    Marmer, B.L.3
  • 127
    • 0026701977 scopus 로고
    • The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B
    • Fosang AJ, Neame PJ, Last K, et al. The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B. J Biol Chem 1992; 267: 19470-19474.
    • (1992) J Biol Chem , vol.267 , pp. 19470-19474
    • Fosang, A.J.1    Neame, P.J.2    Last, K.3
  • 128
    • 0025874373 scopus 로고
    • Human 92- and 72-kilodalton type IV collagenases are elastases
    • Senior RM, Griffin GL, Fliszar CJ, et al. Human 92- and 72-kilodalton type IV collagenases are elastases. J Biol Chem 1991; 266: 7870-7875.
    • (1991) J Biol Chem , vol.266 , pp. 7870-7875
    • Senior, R.M.1    Griffin, G.L.2    Fliszar, C.J.3
  • 129
    • 0028853330 scopus 로고
    • The 84-kDa form of human matrix metalloproteinase-9 degrades substance P and gelatin
    • Backstrom JR, Tokes ZA,. The 84-kDa form of human matrix metalloproteinase-9 degrades substance P and gelatin. J Neurochem 1995; 64: 1312-1318.
    • (1995) J Neurochem , vol.64 , pp. 1312-1318
    • Backstrom, J.R.1    Tokes, Z.A.2
  • 130
    • 0030596456 scopus 로고    scopus 로고
    • Degradation of interleukin 1beta by matrix metalloproteinases
    • Ito A, Mukaiyama A, Itoh Y, et al. Degradation of interleukin 1beta by matrix metalloproteinases. J Biol Chem 1996; 271: 14657-14660.
    • (1996) J Biol Chem , vol.271 , pp. 14657-14660
    • Ito, A.1    Mukaiyama, A.2    Itoh, Y.3
  • 131
    • 0028906790 scopus 로고
    • Identification of 92-kD gelatinase in human coronary atherosclerotic lesions. Association of active enzyme synthesis with unstable angina
    • Brown DL, Hibbs MS, Kearney M, et al. Identification of 92-kD gelatinase in human coronary atherosclerotic lesions. Association of active enzyme synthesis with unstable angina. Circulation 1995; 91: 2125-2131.
    • (1995) Circulation , vol.91 , pp. 2125-2131
    • Brown, D.L.1    Hibbs, M.S.2    Kearney, M.3
  • 132
    • 0036843534 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 is necessary for the regulation of smooth muscle cell replication and migration after arterial injury
    • Cho A, Reidy MA,. Matrix metalloproteinase-9 is necessary for the regulation of smooth muscle cell replication and migration after arterial injury. Circ Res 2002; 91: 845-851.
    • (2002) Circ Res , vol.91 , pp. 845-851
    • Cho, A.1    Reidy, M.A.2
  • 133
    • 80054095409 scopus 로고    scopus 로고
    • Non-antibacterial tetracyclines modulate mediators of periodontitis and atherosclerotic cardiovascular disease: A mechanistic link between local and systemic inflammation
    • Gu Y, Lee HM, Sorsa T, et al. Non-antibacterial tetracyclines modulate mediators of periodontitis and atherosclerotic cardiovascular disease: a mechanistic link between local and systemic inflammation. Pharmacol Res 2011; 64: 573-579.
    • (2011) Pharmacol Res , vol.64 , pp. 573-579
    • Gu, Y.1    Lee, H.M.2    Sorsa, T.3
  • 134
    • 0042490523 scopus 로고    scopus 로고
    • Oral infection with a periodontal pathogen accelerates early atherosclerosis in apolipoprotein E-null mice
    • Lalla E, Lamster IB, Hofmann MA, et al. Oral infection with a periodontal pathogen accelerates early atherosclerosis in apolipoprotein E-null mice. Arterioscler Thromb Vasc Biol 2003; 23: 1405-1411.
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. 1405-1411
    • Lalla, E.1    Lamster, I.B.2    Hofmann, M.A.3
  • 135
    • 0033982563 scopus 로고    scopus 로고
    • Increased matrix metalloproteinase-9 activity in unstable carotid plaques. A potential role in acute plaque disruption
    • Loftus IM, Naylor AR, Goodall S, et al. Increased matrix metalloproteinase-9 activity in unstable carotid plaques. A potential role in acute plaque disruption. Stroke 2000; 31: 40-47.
    • (2000) Stroke , vol.31 , pp. 40-47
    • Loftus, I.M.1    Naylor, A.R.2    Goodall, S.3
  • 136
    • 0141753082 scopus 로고    scopus 로고
    • Serum metalloproteinase 9 levels in patients with coronary artery disease: A novel marker of inflammation
    • Ferroni P, Basili S, Martini F, et al. Serum metalloproteinase 9 levels in patients with coronary artery disease: a novel marker of inflammation. J Investig Med 2003; 51: 295-300.
    • (2003) J Investig Med , vol.51 , pp. 295-300
    • Ferroni, P.1    Basili, S.2    Martini, F.3
  • 137
    • 0035147051 scopus 로고    scopus 로고
    • Plasma levels of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 are increased in the coronary circulation in patients with acute coronary syndrome
    • Inokubo Y, Hanada H, Ishizaka H, et al. Plasma levels of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 are increased in the coronary circulation in patients with acute coronary syndrome. Am Heart J 2001; 141: 211-217.
    • (2001) Am Heart J , vol.141 , pp. 211-217
    • Inokubo, Y.1    Hanada, H.2    Ishizaka, H.3
  • 138
    • 3042671516 scopus 로고    scopus 로고
    • Serum matrix metalloproteinase-9 is elevated in men with a history of myocardial infarction
    • Renko J, Kalela A, Jaakkola O, et al. Serum matrix metalloproteinase-9 is elevated in men with a history of myocardial infarction. Scand J Clin Lab Invest 2004; 64: 255-261.
    • (2004) Scand J Clin Lab Invest , vol.64 , pp. 255-261
    • Renko, J.1    Kalela, A.2    Jaakkola, O.3
  • 139
    • 1842527873 scopus 로고    scopus 로고
    • Clinical and biochemical results of the metalloproteinase inhibition with subantimicrobial doses of doxycycline to prevent acute coronary syndromes (MIDAS) pilot trial
    • Brown DL, Desai KK, Vakili BA, et al. Clinical and biochemical results of the metalloproteinase inhibition with subantimicrobial doses of doxycycline to prevent acute coronary syndromes (MIDAS) pilot trial. Arterioscler Thromb Vasc Biol 2004; 24: 733-738.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 733-738
    • Brown, D.L.1    Desai, K.K.2    Vakili, B.A.3
  • 140
    • 4544372896 scopus 로고    scopus 로고
    • The role of matrix metalloproteinase 7 in innate immunity
    • Burke B,. The role of matrix metalloproteinase 7 in innate immunity. Immunobiology 2004; 209: 51-56.
    • (2004) Immunobiology , vol.209 , pp. 51-56
    • Burke, B.1
  • 141
    • 0034043835 scopus 로고    scopus 로고
    • Cloning of MMP-26. A novel matrilysin-like proteinase
    • de Coignac AB, Elson G, Delneste Y, et al. Cloning of MMP-26. A novel matrilysin-like proteinase. Eur J Biochem 2000; 267: 3323-3329.
    • (2000) Eur J Biochem , vol.267 , pp. 3323-3329
    • De Coignac, A.B.1    Elson, G.2    Delneste, Y.3
  • 142
    • 1942509392 scopus 로고    scopus 로고
    • Matrilysin (matrix metalloproteinase-7): A new promising drug target in cancer and inflammation?
    • Wielockx B, Libert C, Wilson C,. Matrilysin (matrix metalloproteinase-7): a new promising drug target in cancer and inflammation? Cytokine Growth Factor Rev 2004; 15: 111-115.
    • (2004) Cytokine Growth Factor Rev , vol.15 , pp. 111-115
    • Wielockx, B.1    Libert, C.2    Wilson, C.3
  • 143
    • 0030061278 scopus 로고    scopus 로고
    • Matrilysin: An epithelial matrix metalloproteinase with potentially novel functions
    • Wilson CL, Matrisian LM,. Matrilysin: an epithelial matrix metalloproteinase with potentially novel functions. Int J Biochem Cell Biol 1996; 28: 123-136.
    • (1996) Int J Biochem Cell Biol , vol.28 , pp. 123-136
    • Wilson, C.L.1    Matrisian, L.M.2
  • 144
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner JF Jr,. Matrix metalloproteinases. J Biol Chem 1999; 274: 21491-21494.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner, J.F.J.2
  • 145
    • 33845762432 scopus 로고    scopus 로고
    • Gingival crevicular fluid matrix metalloproteinase (MMP)-7, extracellular MMP inducer, and tissue inhibitor of MMP-1 levels in periodontal disease
    • Emingil G, Tervahartiala T, Mantyla P, et al. Gingival crevicular fluid matrix metalloproteinase (MMP)-7, extracellular MMP inducer, and tissue inhibitor of MMP-1 levels in periodontal disease. J Periodontol 2006; 77: 2040-2050.
    • (2006) J Periodontol , vol.77 , pp. 2040-2050
    • Emingil, G.1    Tervahartiala, T.2    Mantyla, P.3
  • 146
    • 0037270522 scopus 로고    scopus 로고
    • Proteolytic host cell enzymes in gingival crevice fluid
    • Uitto VJ, Overall CM, McCulloch C,. Proteolytic host cell enzymes in gingival crevice fluid. Periodontol 2000 2003; 31: 77-104.
    • (2003) Periodontol 2000 , vol.31 , pp. 77-104
    • Uitto, V.J.1    Overall, C.M.2    McCulloch, C.3
  • 147
    • 0036528006 scopus 로고    scopus 로고
    • Matrilysin (matrix metalloproteinase-7) expression in human junctional epithelium
    • Uitto VJ, Salonen JI, Firth JD, et al. Matrilysin (matrix metalloproteinase-7) expression in human junctional epithelium. J Dent Res 2002; 81: 241-246.
    • (2002) J Dent Res , vol.81 , pp. 241-246
    • Uitto, V.J.1    Salonen, J.I.2    Firth, J.D.3
  • 148
    • 0029817688 scopus 로고    scopus 로고
    • Matrilysin is expressed by lipid-laden macrophages at sites of potential rupture in atherosclerotic lesions and localizes to areas of versican deposition, a proteoglycan substrate for the enzyme
    • Halpert I, Sires UI, Roby JD, et al. Matrilysin is expressed by lipid-laden macrophages at sites of potential rupture in atherosclerotic lesions and localizes to areas of versican deposition, a proteoglycan substrate for the enzyme. Proc Natl Acad Sci U S A 1996; 93: 9748-9753.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 9748-9753
    • Halpert, I.1    Sires, U.I.2    Roby, J.D.3
  • 149
    • 33746656655 scopus 로고    scopus 로고
    • Increased plasma concentration of matrix metalloproteinase-7 in patients with coronary artery disease
    • Nilsson L, Jonasson L, Nijm J, et al. Increased plasma concentration of matrix metalloproteinase-7 in patients with coronary artery disease. Clin Chem 2006; 52: 1522-1527.
    • (2006) Clin Chem , vol.52 , pp. 1522-1527
    • Nilsson, L.1    Jonasson, L.2    Nijm, J.3
  • 150
    • 33748649665 scopus 로고    scopus 로고
    • Matrix metalloproteinase (MMP)-7 activates MMP-8 but not MMP-13
    • Dozier S, Escobar GP, Lindsey ML,. Matrix metalloproteinase (MMP)-7 activates MMP-8 but not MMP-13. Med Chem 2006; 2: 523-526.
    • (2006) Med Chem , vol.2 , pp. 523-526
    • Dozier, S.1    Escobar, G.P.2    Lindsey, M.L.3
  • 151
    • 0034445775 scopus 로고    scopus 로고
    • The in vivo expression of the collagenolytic matrix metalloproteinases (MMP-2, -8, -13, and -14) and matrilysin (MMP-7) in adult and localized juvenile periodontitis
    • Tervahartiala T, Pirilä E, Ceponis A, et al. The in vivo expression of the collagenolytic matrix metalloproteinases (MMP-2, -8, -13, and -14) and matrilysin (MMP-7) in adult and localized juvenile periodontitis. J Dent Res 2000; 79: 1969-1977.
    • (2000) J Dent Res , vol.79 , pp. 1969-1977
    • Tervahartiala, T.1    Pirilä, E.2    Ceponis, A.3
  • 152
    • 1642443944 scopus 로고    scopus 로고
    • Matrix metalloproteinases, inflammation and atherosclerosis: Therapeutic perspectives
    • Beaudeux JL, Giral P, Bruckert E, et al. Matrix metalloproteinases, inflammation and atherosclerosis: therapeutic perspectives. Clin Chem Lab Med 2004; 42: 121-131.
    • (2004) Clin Chem Lab Med , vol.42 , pp. 121-131
    • Beaudeux, J.L.1    Giral, P.2    Bruckert, E.3
  • 153
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Evolution, structure and function
    • Brew K, Dinakarpandian D, Nagase H,. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim Biophys Acta 2000; 1477: 267-283.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 154
    • 48849107531 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases in cell signaling: Metalloproteinase-independent biological activities
    • Stetler-Stevenson WG,. Tissue inhibitors of metalloproteinases in cell signaling: metalloproteinase-independent biological activities. Sci Signal 2008; 1: re6-re6.
    • (2008) Sci Signal , vol.1 , pp. re6-re6
    • Stetler-Stevenson, W.G.1
  • 155
    • 0028792509 scopus 로고
    • Matrix metalloproteinases and cardiovascular disease
    • Dollery CM, McEwan JR, Henney AM,. Matrix metalloproteinases and cardiovascular disease. Circ Res 1995; 77: 863-868.
    • (1995) Circ Res , vol.77 , pp. 863-868
    • Dollery, C.M.1    McEwan, J.R.2    Henney, A.M.3
  • 156
    • 0022362769 scopus 로고
    • Human alveolar macrophages produce a fibroblast-like collagenase and collagenase inhibitor
    • Welgus HG, Campbell EJ, Bar-Shavit Z, et al. Human alveolar macrophages produce a fibroblast-like collagenase and collagenase inhibitor. J Clin Invest 1985; 76: 219-224.
    • (1985) J Clin Invest , vol.76 , pp. 219-224
    • Welgus, H.G.1    Campbell, E.J.2    Bar-Shavit, Z.3
  • 157
    • 33646091277 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-1 (TIMP-1) is an independent predictor of all-cause mortality, cardiac mortality, and myocardial infarction
    • e1101-e1108
    • Cavusoglu E, Ruwende C, Chopra V, et al. Tissue inhibitor of metalloproteinase-1 (TIMP-1) is an independent predictor of all-cause mortality, cardiac mortality, and myocardial infarction. Am Heart J 2006; 151: 1101 e1101-e1108.
    • (2006) Am Heart J , vol.151 , pp. 1101
    • Cavusoglu, E.1    Ruwende, C.2    Chopra, V.3
  • 158
    • 30344484237 scopus 로고    scopus 로고
    • Prognostic value of tissue inhibitor of metalloproteinase-1 for cardiovascular death among patients with cardiovascular disease: Results from the AtheroGene study
    • Lubos E, Schnabel R, Rupprecht HJ, et al. Prognostic value of tissue inhibitor of metalloproteinase-1 for cardiovascular death among patients with cardiovascular disease: results from the AtheroGene study. Eur Heart J 2006; 27: 150-156.
    • (2006) Eur Heart J , vol.27 , pp. 150-156
    • Lubos, E.1    Schnabel, R.2    Rupprecht, H.J.3
  • 159
    • 0345166873 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their inhibitors in gingival mast cells in persons with and without human immunodeficiency virus infection
    • Naesse EP, Schreurs O, Helgeland K, et al. Matrix metalloproteinases and their inhibitors in gingival mast cells in persons with and without human immunodeficiency virus infection. J Periodontal Res 2003; 38: 575-582.
    • (2003) J Periodontal Res , vol.38 , pp. 575-582
    • Naesse, E.P.1    Schreurs, O.2    Helgeland, K.3
  • 160
    • 77952339586 scopus 로고    scopus 로고
    • Salivary MMP-8, TIMP-1, and ICTP as markers of advanced periodontitis
    • Gursoy UK, Könönen E, Pradhan-Palikhe P, et al. Salivary MMP-8, TIMP-1, and ICTP as markers of advanced periodontitis. J Clin Periodontol 2010; 37: 487-493.
    • (2010) J Clin Periodontol , vol.37 , pp. 487-493
    • Gursoy, U.K.1    Könönen, E.2    Pradhan-Palikhe, P.3
  • 161
    • 0030338160 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their inhibitors in gingival crevicular fluid and saliva of periodontitis patients
    • Ingman T, Tervahartiala T, Ding Y, et al. Matrix metalloproteinases and their inhibitors in gingival crevicular fluid and saliva of periodontitis patients. J Clin Periodontol 1996; 23: 1127-1132.
    • (1996) J Clin Periodontol , vol.23 , pp. 1127-1132
    • Ingman, T.1    Tervahartiala, T.2    Ding, Y.3
  • 162
    • 79953861737 scopus 로고    scopus 로고
    • The effect of subantimicrobial-dose-doxycycline periodontal therapy on serum biomarkers of systemic inflammation: A randomized, double-masked, placebo-controlled clinical trial
    • Payne JB, Golub LM, Stoner JA, et al. The effect of subantimicrobial-dose-doxycycline periodontal therapy on serum biomarkers of systemic inflammation: a randomized, double-masked, placebo-controlled clinical trial. J Am Dent Assoc 2011; 142: 262-273.
    • (2011) J Am Dent Assoc , vol.142 , pp. 262-273
    • Payne, J.B.1    Golub, L.M.2    Stoner, J.A.3
  • 163
    • 0034682860 scopus 로고    scopus 로고
    • Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase
    • Belaaouaj A, Kim KS, Shapiro SD,. Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase. Science 2000; 289: 1185-1188.
    • (2000) Science , vol.289 , pp. 1185-1188
    • Belaaouaj, A.1    Kim, K.S.2    Shapiro, S.D.3
  • 164
    • 0031729271 scopus 로고    scopus 로고
    • Neutrophil serine proteinases and defensins in chronic obstructive pulmonary disease: Effects on pulmonary epithelium
    • Hiemstra PS, van Wetering S, Stolk J,. Neutrophil serine proteinases and defensins in chronic obstructive pulmonary disease: effects on pulmonary epithelium. Eur Respir J 1998; 12: 1200-1208.
    • (1998) Eur Respir J , vol.12 , pp. 1200-1208
    • Hiemstra, P.S.1    Van Wetering, S.2    Stolk, J.3
  • 165
    • 0031041367 scopus 로고    scopus 로고
    • Activation of MMP-9 by neutrophil elastase in an in vivo model of acute lung injury
    • Ferry G, Lonchampt M, Pennel L, et al. Activation of MMP-9 by neutrophil elastase in an in vivo model of acute lung injury. FEBS Lett 1997; 402: 111-115.
    • (1997) FEBS Lett , vol.402 , pp. 111-115
    • Ferry, G.1    Lonchampt, M.2    Pennel, L.3
  • 166
    • 0024323967 scopus 로고
    • Activation of matrix metalloproteinase 3 (stromelysin) and matrix metalloproteinase 2 ('gelatinase') by human neutrophil elastase and cathepsin G
    • Okada Y, Nakanishi I,. Activation of matrix metalloproteinase 3 (stromelysin) and matrix metalloproteinase 2 ('gelatinase') by human neutrophil elastase and cathepsin G. FEBS Lett 1989; 249: 353-356.
    • (1989) FEBS Lett , vol.249 , pp. 353-356
    • Okada, Y.1    Nakanishi, I.2
  • 167
    • 43049166916 scopus 로고    scopus 로고
    • Human neutrophil elastase: Mediator and therapeutic target in atherosclerosis
    • Henriksen PA, Sallenave JM,. Human neutrophil elastase: mediator and therapeutic target in atherosclerosis. Int J Biochem Cell Biol 2008; 40: 1095-1100.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1095-1100
    • Henriksen, P.A.1    Sallenave, J.M.2
  • 168
    • 0037782348 scopus 로고    scopus 로고
    • Neutrophil elastase in human atherosclerotic plaques: Production by macrophages
    • Dollery CM, Owen CA, Sukhova GK, et al. Neutrophil elastase in human atherosclerotic plaques: production by macrophages. Circulation 2003; 107: 2829-2836.
    • (2003) Circulation , vol.107 , pp. 2829-2836
    • Dollery, C.M.1    Owen, C.A.2    Sukhova, G.K.3
  • 169
    • 0033794893 scopus 로고    scopus 로고
    • Tissue plasminogen activator and leucocyte elastase as predictors of cardiovascular events in subjects with angina pectoris: Edinburgh Artery Study
    • Smith FB, Fowkes FG, Rumley A, et al. Tissue plasminogen activator and leucocyte elastase as predictors of cardiovascular events in subjects with angina pectoris: Edinburgh Artery Study. Eur Heart J 2000; 21: 1607-1613.
    • (2000) Eur Heart J , vol.21 , pp. 1607-1613
    • Smith, F.B.1    Fowkes, F.G.2    Rumley, A.3
  • 170
    • 37249010527 scopus 로고    scopus 로고
    • Involvement of intraplaque hemorrhage in atherothrombosis evolution via neutrophil protease enrichment
    • Leclercq A, Houard X, Philippe M, et al. Involvement of intraplaque hemorrhage in atherothrombosis evolution via neutrophil protease enrichment. J Leukoc Biol 2007; 82: 1420-1429.
    • (2007) J Leukoc Biol , vol.82 , pp. 1420-1429
    • Leclercq, A.1    Houard, X.2    Philippe, M.3
  • 171
    • 34250180610 scopus 로고    scopus 로고
    • Neutrophil elastase is involved in the initial destruction of human periodontal ligament
    • Ujiie Y, Oida S, Gomi K, et al. Neutrophil elastase is involved in the initial destruction of human periodontal ligament. J Periodontal Res 2007; 42: 325-330.
    • (2007) J Periodontal Res , vol.42 , pp. 325-330
    • Ujiie, Y.1    Oida, S.2    Gomi, K.3
  • 172
    • 84864285073 scopus 로고    scopus 로고
    • Increased systemic elastase and C-reactive protein in aggressive periodontitis (CLOI-D-00160R2)
    • Wohlfeil M, Scharf S, Siegelin Y, et al. Increased systemic elastase and C-reactive protein in aggressive periodontitis (CLOI-D-00160R2). Clin Oral Investig 2012; 16: 1199-1207.
    • (2012) Clin Oral Investig , vol.16 , pp. 1199-1207
    • Wohlfeil, M.1    Scharf, S.2    Siegelin, Y.3
  • 173
    • 84875231261 scopus 로고    scopus 로고
    • Non-surgical periodontal therapy decreases serum elastase levels in aggressive but not in chronic periodontitis
    • Eickholz P, Siegelin Y, Scharf S, et al. Non-surgical periodontal therapy decreases serum elastase levels in aggressive but not in chronic periodontitis. J Clin Periodontol 2013; 40: 327-333.
    • (2013) J Clin Periodontol , vol.40 , pp. 327-333
    • Eickholz, P.1    Siegelin, Y.2    Scharf, S.3
  • 174
    • 84877794345 scopus 로고    scopus 로고
    • Myeloperoxidase: Expressing inflammation and oxidative stress in cardiovascular disease
    • Anatoliotakis N, Deftereos S, Bouras G, et al. Myeloperoxidase: expressing inflammation and oxidative stress in cardiovascular disease. Curr Top Med Chem 2013; 13: 115-138.
    • (2013) Curr Top Med Chem , vol.13 , pp. 115-138
    • Anatoliotakis, N.1    Deftereos, S.2    Bouras, G.3
  • 176
    • 0141727730 scopus 로고    scopus 로고
    • Myeloperoxidase serum levels predict risk in patients with acute coronary syndromes
    • Baldus S, Heeschen C, Meinertz T, et al. Myeloperoxidase serum levels predict risk in patients with acute coronary syndromes. Circulation 2003; 108: 1440-1445.
    • (2003) Circulation , vol.108 , pp. 1440-1445
    • Baldus, S.1    Heeschen, C.2    Meinertz, T.3
  • 177
    • 77749310803 scopus 로고    scopus 로고
    • Myeloperoxidase and C-reactive protein have combined utility for long-term prediction of cardiovascular mortality after coronary angiography
    • Heslop CL, Frohlich JJ, Hill JS,. Myeloperoxidase and C-reactive protein have combined utility for long-term prediction of cardiovascular mortality after coronary angiography. J Am Coll Cardiol 2010; 55: 1102-1109.
    • (2010) J Am Coll Cardiol , vol.55 , pp. 1102-1109
    • Heslop, C.L.1    Frohlich, J.J.2    Hill, J.S.3
  • 178
    • 84901194381 scopus 로고    scopus 로고
    • Association of myeloperoxidase with total and cardiovascular mortality in individuals undergoing coronary angiography - The LURIC study
    • Scharnagl H, Kleber ME, Genser B, et al. Association of myeloperoxidase with total and cardiovascular mortality in individuals undergoing coronary angiography-the LURIC study. Int J Cardiol 2014; 174: 96-105.
    • (2014) Int J Cardiol , vol.174 , pp. 96-105
    • Scharnagl, H.1    Kleber, M.E.2    Genser, B.3
  • 179
    • 0035824162 scopus 로고    scopus 로고
    • Association between myeloperoxidase levels and risk of coronary artery disease
    • Zhang R, Brennan ML, Fu X, et al. Association between myeloperoxidase levels and risk of coronary artery disease. JAMA 2001; 286: 2136-2142.
    • (2001) JAMA , vol.286 , pp. 2136-2142
    • Zhang, R.1    Brennan, M.L.2    Fu, X.3
  • 180
    • 0035108136 scopus 로고    scopus 로고
    • Macrophage myeloperoxidase regulation by granulocyte macrophage colony-stimulating factor in human atherosclerosis and implications in acute coronary syndromes
    • Sugiyama S, Okada Y, Sukhova GK, et al. Macrophage myeloperoxidase regulation by granulocyte macrophage colony-stimulating factor in human atherosclerosis and implications in acute coronary syndromes. Am J Pathol 2001; 158: 879-891.
    • (2001) Am J Pathol , vol.158 , pp. 879-891
    • Sugiyama, S.1    Okada, Y.2    Sukhova, G.K.3
  • 181
    • 84905007179 scopus 로고    scopus 로고
    • Myeloperoxidase in human neutrophil host defence
    • Nauseef WM,. Myeloperoxidase in human neutrophil host defence. Cell Microbiol 2014; 16: 1146-1155.
    • (2014) Cell Microbiol , vol.16 , pp. 1146-1155
    • Nauseef, W.M.1
  • 182
    • 30544444120 scopus 로고    scopus 로고
    • Myeloperoxidase-mediated oxidation of high-density lipoproteins: Fingerprints of newly recognized potential proatherogenic lipoproteins
    • Malle E, Marsche G, Panzenboeck U, et al. Myeloperoxidase-mediated oxidation of high-density lipoproteins: fingerprints of newly recognized potential proatherogenic lipoproteins. Arch Biochem Biophys 2006; 445: 245-255.
    • (2006) Arch Biochem Biophys , vol.445 , pp. 245-255
    • Malle, E.1    Marsche, G.2    Panzenboeck, U.3
  • 183
    • 0029932445 scopus 로고    scopus 로고
    • Presence of hypochlorite-modified proteins in human atherosclerotic lesions
    • Hazell LJ, Arnold L, Flowers D, et al. Presence of hypochlorite-modified proteins in human atherosclerotic lesions. J Clin Invest 1996; 97: 1535-1544.
    • (1996) J Clin Invest , vol.97 , pp. 1535-1544
    • Hazell, L.J.1    Arnold, L.2    Flowers, D.3
  • 184
    • 0035798684 scopus 로고    scopus 로고
    • Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase
    • Fu X, Kassim SY, Parks WC, et al. Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J Biol Chem 2001; 276: 41279-41287.
    • (2001) J Biol Chem , vol.276 , pp. 41279-41287
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3
  • 185
    • 0011489860 scopus 로고
    • Activation of the endogenous metalloproteinase, gelatinase, by triggered human neutrophils
    • Peppin GJ, Weiss SJ,. Activation of the endogenous metalloproteinase, gelatinase, by triggered human neutrophils. Proc Natl Acad Sci U S A 1986; 83: 4322-4326.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4322-4326
    • Peppin, G.J.1    Weiss, S.J.2
  • 186
    • 0021961153 scopus 로고
    • Oxidative autoactivation of latent collagenase by human neutrophils
    • Weiss SJ, Peppin G, Ortiz X, et al. Oxidative autoactivation of latent collagenase by human neutrophils. Science 1985; 227: 747-749.
    • (1985) Science , vol.227 , pp. 747-749
    • Weiss, S.J.1    Peppin, G.2    Ortiz, X.3
  • 187
    • 0026500717 scopus 로고
    • Different effects of hypochlorous acid on human neutrophil metalloproteinases: Activation of collagenase and inactivation of collagenase and gelatinase
    • Michaelis J, Vissers MC, Winterbourn CC,. Different effects of hypochlorous acid on human neutrophil metalloproteinases: activation of collagenase and inactivation of collagenase and gelatinase. Arch Biochem Biophys 1992; 292: 555-562.
    • (1992) Arch Biochem Biophys , vol.292 , pp. 555-562
    • Michaelis, J.1    Vissers, M.C.2    Winterbourn, C.C.3
  • 188
    • 0042093741 scopus 로고    scopus 로고
    • Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): An oxidative mechanism for restraining proteolytic activity during inflammation
    • Fu X, Kassim SY, Parks WC, et al. Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): an oxidative mechanism for restraining proteolytic activity during inflammation. J Biol Chem 2003; 278: 28403-28409.
    • (2003) J Biol Chem , vol.278 , pp. 28403-28409
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3
  • 189
    • 0031837825 scopus 로고    scopus 로고
    • The oxidative inactivation of tissue inhibitor of metalloproteinase-1 (TIMP-1) by hypochlorous acid (HOCI) is suppressed by anti-rheumatic drugs
    • Shabani F, McNeil J, Tippett L,. The oxidative inactivation of tissue inhibitor of metalloproteinase-1 (TIMP-1) by hypochlorous acid (HOCI) is suppressed by anti-rheumatic drugs. Free Radic Res 1998; 28: 115-123.
    • (1998) Free Radic Res , vol.28 , pp. 115-123
    • Shabani, F.1    McNeil, J.2    Tippett, L.3
  • 190
    • 36148941000 scopus 로고    scopus 로고
    • Myeloperoxidase inactivates TIMP-1 by oxidizing its N-terminal cysteine residue: An oxidative mechanism for regulating proteolysis during inflammation
    • Wang Y, Rosen H, Madtes DK, et al. Myeloperoxidase inactivates TIMP-1 by oxidizing its N-terminal cysteine residue: an oxidative mechanism for regulating proteolysis during inflammation. J Biol Chem 2007; 282: 31826-31834.
    • (2007) J Biol Chem , vol.282 , pp. 31826-31834
    • Wang, Y.1    Rosen, H.2    Madtes, D.K.3
  • 191
    • 0036802844 scopus 로고    scopus 로고
    • Amplified crevicular leukocyte activity in aggressive periodontal disease
    • Buchmann R, Hasilik A, Van Dyke TE, et al. Amplified crevicular leukocyte activity in aggressive periodontal disease. J Dent Res 2002; 81: 716-721.
    • (2002) J Dent Res , vol.81 , pp. 716-721
    • Buchmann, R.1    Hasilik, A.2    Van Dyke, T.E.3
  • 192
    • 84941181704 scopus 로고    scopus 로고
    • Evaluation of local and systemic levels of interleukin-17, interleukin-23, and myeloperoxidase in response to periodontal therapy in patients with generalized aggressive periodontitis
    • Cifcibasi E, Koyuncuoglu C, Ciblak M, et al. Evaluation of local and systemic levels of interleukin-17, interleukin-23, and myeloperoxidase in response to periodontal therapy in patients with generalized aggressive periodontitis. Inflammation 2015; 38: 1959-1968.
    • (2015) Inflammation , vol.38 , pp. 1959-1968
    • Cifcibasi, E.1    Koyuncuoglu, C.2    Ciblak, M.3
  • 193
    • 84949671979 scopus 로고    scopus 로고
    • Myeloperoxidase level around dental implants as an indicator of an inflammatory process
    • Durrani F, Singh R,. Myeloperoxidase level around dental implants as an indicator of an inflammatory process. Indian J Dent 2015; 6: 2-6.
    • (2015) Indian J Dent , vol.6 , pp. 2-6
    • Durrani, F.1    Singh, R.2
  • 194
    • 0027829413 scopus 로고
    • Myeloperoxidase activity in peripheral blood, neutrophil crevicular fluid and whole saliva of patients with periodontal disease
    • Over C, Yamalik N, Yavuzyilmaz E, et al. Myeloperoxidase activity in peripheral blood, neutrophil crevicular fluid and whole saliva of patients with periodontal disease. J Nihon Univ Sch Dent 1993; 35: 235-240.
    • (1993) J Nihon Univ Sch Dent , vol.35 , pp. 235-240
    • Over, C.1    Yamalik, N.2    Yavuzyilmaz, E.3
  • 195
    • 33644785995 scopus 로고    scopus 로고
    • Gingival crevicular fluid levels of calprotectin and myeloperoxidase during therapy for generalized aggressive periodontitis
    • Kaner D, Bernimoulin JP, Kleber BM, et al. Gingival crevicular fluid levels of calprotectin and myeloperoxidase during therapy for generalized aggressive periodontitis. J Periodontal Res 2006; 41: 132-139.
    • (2006) J Periodontal Res , vol.41 , pp. 132-139
    • Kaner, D.1    Bernimoulin, J.P.2    Kleber, B.M.3
  • 196
    • 84897607689 scopus 로고    scopus 로고
    • Matrix metalloproteinases and myeloperoxidase in gingival crevicular fluid provide site-specific diagnostic value for chronic periodontitis
    • Leppilahti JM, Hernandez-Rios PA, Gamonal JA, et al. Matrix metalloproteinases and myeloperoxidase in gingival crevicular fluid provide site-specific diagnostic value for chronic periodontitis. J Clin Periodontol 2014; 41: 348-356.
    • (2014) J Clin Periodontol , vol.41 , pp. 348-356
    • Leppilahti, J.M.1    Hernandez-Rios, P.A.2    Gamonal, J.A.3
  • 197
    • 0022598285 scopus 로고
    • Gingival crevicular fluid myeloperoxidase at periodontitis sites
    • Smith QT, Hinrichs JE, Melnyk RS,. Gingival crevicular fluid myeloperoxidase at periodontitis sites. J Periodontal Res 1986; 21: 45-55.
    • (1986) J Periodontal Res , vol.21 , pp. 45-55
    • Smith, Q.T.1    Hinrichs, J.E.2    Melnyk, R.S.3
  • 198
    • 4644226061 scopus 로고    scopus 로고
    • The investigation of glutathione peroxidase, lactoferrin, myeloperoxidase and interleukin-1beta in gingival crevicular fluid: Implications for oxidative stress in human periodontal diseases
    • Wei PF, Ho KY, Ho YP, et al. The investigation of glutathione peroxidase, lactoferrin, myeloperoxidase and interleukin-1beta in gingival crevicular fluid: implications for oxidative stress in human periodontal diseases. J Periodontal Res 2004; 39: 287-293.
    • (2004) J Periodontal Res , vol.39 , pp. 287-293
    • Wei, P.F.1    Ho, K.Y.2    Ho, Y.P.3
  • 199
    • 0034153976 scopus 로고    scopus 로고
    • The importance of data presentation regarding gingival crevicular fluid myeloperoxidase and elastase-like activity in periodontal disease and health status
    • Yamalik N, Caglayan F, Kilinc K, et al. The importance of data presentation regarding gingival crevicular fluid myeloperoxidase and elastase-like activity in periodontal disease and health status. J Periodontol 2000; 71: 460-467.
    • (2000) J Periodontol , vol.71 , pp. 460-467
    • Yamalik, N.1    Caglayan, F.2    Kilinc, K.3
  • 200
    • 78149436457 scopus 로고    scopus 로고
    • Myeloperoxidase activity is increased in gingival crevicular fluid and whole saliva after fixed orthodontic appliance activation
    • Marcaccini AM, Amato PA, Leao FV, et al. Myeloperoxidase activity is increased in gingival crevicular fluid and whole saliva after fixed orthodontic appliance activation. Am J Orthod Dentofacial Orthop 2010; 138: 613-616.
    • (2010) Am J Orthod Dentofacial Orthop , vol.138 , pp. 613-616
    • Marcaccini, A.M.1    Amato, P.A.2    Leao, F.V.3
  • 201
    • 84876724827 scopus 로고    scopus 로고
    • Salivary MMPs, TIMPs, and MPO levels in periodontal disease patients and controls
    • Meschiari CA, Marcaccini AM, Santos Moura BC, et al. Salivary MMPs, TIMPs, and MPO levels in periodontal disease patients and controls. Clin Chim Acta 2013; 421: 140-146.
    • (2013) Clin Chim Acta , vol.421 , pp. 140-146
    • Meschiari, C.A.1    Marcaccini, A.M.2    Santos Moura, B.C.3
  • 202
    • 84918832511 scopus 로고    scopus 로고
    • Serum and salivary matrix metalloproteinases, neutrophil elastase, myeloperoxidase in patients with chronic or aggressive periodontitis
    • Nizam N, Gumus P, Pitkanen J, et al. Serum and salivary matrix metalloproteinases, neutrophil elastase, myeloperoxidase in patients with chronic or aggressive periodontitis. Inflammation 2014; 37: 1771-1778.
    • (2014) Inflammation , vol.37 , pp. 1771-1778
    • Nizam, N.1    Gumus, P.2    Pitkanen, J.3
  • 203
    • 84879409147 scopus 로고    scopus 로고
    • Evaluation of gelatinases, tissue inhibitor of matrix metalloproteinase-2, and myeloperoxidase protein in healthy and inflamed human dental pulp tissue
    • Accorsi-Mendonca T, Silva EJ, Marcaccini AM, et al. Evaluation of gelatinases, tissue inhibitor of matrix metalloproteinase-2, and myeloperoxidase protein in healthy and inflamed human dental pulp tissue. J Endod 2013; 39: 879-882.
    • (2013) J Endod , vol.39 , pp. 879-882
    • Accorsi-Mendonca, T.1    Silva, E.J.2    Marcaccini, A.M.3
  • 204
    • 0031077878 scopus 로고    scopus 로고
    • Myeloperoxidase isoform activities released by human neutrophils in response to dental and periodontal bacteria
    • Miyasaki KT, Nemirovskiy E,. Myeloperoxidase isoform activities released by human neutrophils in response to dental and periodontal bacteria. Oral Microbiol Immunol 1997; 12: 27-32.
    • (1997) Oral Microbiol Immunol , vol.12 , pp. 27-32
    • Miyasaki, K.T.1    Nemirovskiy, E.2
  • 205
    • 33846243283 scopus 로고    scopus 로고
    • Characterization of the antioxidant profile of human saliva in peri-implant health and disease
    • Liskmann S, Vihalemm T, Salum O, et al. Characterization of the antioxidant profile of human saliva in peri-implant health and disease. Clin Oral Implants Res 2007; 18: 27-33.
    • (2007) Clin Oral Implants Res , vol.18 , pp. 27-33
    • Liskmann, S.1    Vihalemm, T.2    Salum, O.3
  • 206
    • 84989223423 scopus 로고    scopus 로고
    • Salivary concentration of oxidative stress biomarkers in a group of patients with peri-implantitis: A transversal study
    • Epub ahead of print 31 Jul 2015. DOI: 10.1111/cid.12367
    • Sanchez-Siles M, Lucas-Azorin J, Salazar-Sanchez N, et al. Salivary concentration of oxidative stress biomarkers in a group of patients with peri-implantitis: a transversal study. Clin Implant Dent Relat Res. Epub ahead of print 31 Jul 2015. DOI: 10.1111/cid.12367.
    • Clin Implant Dent Relat Res
    • Sanchez-Siles, M.1    Lucas-Azorin, J.2    Salazar-Sanchez, N.3
  • 207
    • 7944224086 scopus 로고    scopus 로고
    • Correlation of peri-implant health and myeloperoxidase levels: A cross-sectional clinical study
    • Liskmann S, Zilmer M, Vihalemm T, et al. Correlation of peri-implant health and myeloperoxidase levels: a cross-sectional clinical study. Clin Oral Implants Res 2004; 15: 546-552.
    • (2004) Clin Oral Implants Res , vol.15 , pp. 546-552
    • Liskmann, S.1    Zilmer, M.2    Vihalemm, T.3
  • 208
    • 84938575143 scopus 로고    scopus 로고
    • Levels of myeloperoxidase and alkaline phosphatase in periimplant sulcus fluid in health and disease and after nonsurgical therapy
    • Malik N, Naik D, Uppoor A,. Levels of myeloperoxidase and alkaline phosphatase in periimplant sulcus fluid in health and disease and after nonsurgical therapy. Implant Dent 2015; 24: 434-440.
    • (2015) Implant Dent , vol.24 , pp. 434-440
    • Malik, N.1    Naik, D.2    Uppoor, A.3
  • 209
    • 84873293442 scopus 로고    scopus 로고
    • Myeloperoxidase: A front-line defender against phagocytosed microorganisms
    • Klebanoff SJ, Kettle AJ, Rosen H, et al. Myeloperoxidase: a front-line defender against phagocytosed microorganisms. J Leukoc Biol 2013; 93: 185-198.
    • (2013) J Leukoc Biol , vol.93 , pp. 185-198
    • Klebanoff, S.J.1    Kettle, A.J.2    Rosen, H.3
  • 210
    • 84866175158 scopus 로고    scopus 로고
    • Neutrophil extracellular traps: Double-edged swords of innate immunity
    • Kaplan MJ, Radic M,. Neutrophil extracellular traps: double-edged swords of innate immunity. J Immunol 2012; 189: 2689-2695.
    • (2012) J Immunol , vol.189 , pp. 2689-2695
    • Kaplan, M.J.1    Radic, M.2
  • 211
    • 84881509539 scopus 로고    scopus 로고
    • Neutrophil extracellular traps as a new paradigm in innate immunity: Friend or foe?
    • Cooper PR, Palmer LJ, Chapple IL,. Neutrophil extracellular traps as a new paradigm in innate immunity: friend or foe? Periodontol 2000 2013; 63: 165-197.
    • (2013) Periodontol 2000 , vol.63 , pp. 165-197
    • Cooper, P.R.1    Palmer, L.J.2    Chapple, I.L.3
  • 212
    • 84983190360 scopus 로고    scopus 로고
    • Neutrophil extracellular trap formation in supragingival biofilms
    • Hirschfeld J, Dommisch H, Skora P, et al. Neutrophil extracellular trap formation in supragingival biofilms. Int J Med Microbiol 2015; 305: 453-463.
    • (2015) Int J Med Microbiol , vol.305 , pp. 453-463
    • Hirschfeld, J.1    Dommisch, H.2    Skora, P.3
  • 213
    • 84945959235 scopus 로고    scopus 로고
    • A novel mechanism for NETosis provides antimicrobial defense at the oral mucosa
    • Mohanty T, Sjögren J, Kahn F, et al. A novel mechanism for NETosis provides antimicrobial defense at the oral mucosa. Blood 2015; 126: 2128-2137.
    • (2015) Blood , vol.126 , pp. 2128-2137
    • Mohanty, T.1    Sjögren, J.2    Kahn, F.3
  • 214
    • 84881025794 scopus 로고    scopus 로고
    • Elevated levels of circulating DNA and chromatin are independently associated with severe coronary atherosclerosis and a prothrombotic state
    • Borissoff JI, Joosen IA, Versteylen MO, et al. Elevated levels of circulating DNA and chromatin are independently associated with severe coronary atherosclerosis and a prothrombotic state. Arterioscler Thromb Vasc Biol 2013; 33: 2032-2040.
    • (2013) Arterioscler Thromb Vasc Biol , vol.33 , pp. 2032-2040
    • Borissoff, J.I.1    Joosen, I.A.2    Versteylen, M.O.3
  • 215
    • 84907086753 scopus 로고    scopus 로고
    • Periodontal bacteria in human carotid atherothrombosis as a potential trigger for neutrophil activation
    • Range H, Labreuche J, Louedec L, et al. Periodontal bacteria in human carotid atherothrombosis as a potential trigger for neutrophil activation. Atherosclerosis 2014; 236: 448-455.
    • (2014) Atherosclerosis , vol.236 , pp. 448-455
    • Range, H.1    Labreuche, J.2    Louedec, L.3
  • 216
    • 0037189377 scopus 로고    scopus 로고
    • Myeloperoxidase, a leukocyte-derived vascular NO oxidase
    • Eiserich JP, Baldus S, Brennan ML, et al. Myeloperoxidase, a leukocyte-derived vascular NO oxidase. Science 2002; 296: 2391-2394.
    • (2002) Science , vol.296 , pp. 2391-2394
    • Eiserich, J.P.1    Baldus, S.2    Brennan, M.L.3
  • 217
    • 3042756855 scopus 로고    scopus 로고
    • Serum myeloperoxidase levels independently predict endothelial dysfunction in humans
    • Vita JA, Brennan ML, Gokce N, et al. Serum myeloperoxidase levels independently predict endothelial dysfunction in humans. Circulation 2004; 110: 1134-1139.
    • (2004) Circulation , vol.110 , pp. 1134-1139
    • Vita, J.A.1    Brennan, M.L.2    Gokce, N.3
  • 218
    • 84929317722 scopus 로고    scopus 로고
    • Aggressive periodontitis: An appraisal of systemic effects on its etiology-genetic aspect
    • Debabrata K, Prasanta B, Vineet N, et al. Aggressive periodontitis: an appraisal of systemic effects on its etiology-genetic aspect. J Indian Soc Periodontol 2015; 19: 169-173.
    • (2015) J Indian Soc Periodontol , vol.19 , pp. 169-173
    • Debabrata, K.1    Prasanta, B.2    Vineet, N.3
  • 219
    • 77954045412 scopus 로고    scopus 로고
    • Genetic variation of myeloperoxidase gene contributes to aggressive periodontitis: A preliminary association study in Turkish population
    • Erciyas K, Pehlivan S, Sever T, et al. Genetic variation of myeloperoxidase gene contributes to aggressive periodontitis: a preliminary association study in Turkish population. Dis Markers 2010; 28: 95-99.
    • (2010) Dis Markers , vol.28 , pp. 95-99
    • Erciyas, K.1    Pehlivan, S.2    Sever, T.3
  • 220
    • 0036547366 scopus 로고    scopus 로고
    • Gender and smoking-related risk reduction of periodontal disease with variant myeloperoxidase alleles
    • Meisel P, Krause T, Cascorbi I, et al. Gender and smoking-related risk reduction of periodontal disease with variant myeloperoxidase alleles. Genes Immun 2002; 3: 102-106.
    • (2002) Genes Immun , vol.3 , pp. 102-106
    • Meisel, P.1    Krause, T.2    Cascorbi, I.3
  • 221
    • 0037016059 scopus 로고    scopus 로고
    • Neutrophil infiltration of culprit lesions in acute coronary syndromes
    • Naruko T, Ueda M, Haze K, et al. Neutrophil infiltration of culprit lesions in acute coronary syndromes. Circulation 2002; 106: 2894-2900.
    • (2002) Circulation , vol.106 , pp. 2894-2900
    • Naruko, T.1    Ueda, M.2    Haze, K.3
  • 222
    • 77955984271 scopus 로고    scopus 로고
    • High neutrophil numbers in human carotid atherosclerotic plaques are associated with characteristics of rupture-prone lesions
    • Ionita MG, van den Borne P, Catanzariti LM, et al. High neutrophil numbers in human carotid atherosclerotic plaques are associated with characteristics of rupture-prone lesions. Arterioscler Thromb Vasc Biol 2010; 30: 1842-1848.
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , pp. 1842-1848
    • Ionita, M.G.1    Van Den Borne, P.2    Catanzariti, L.M.3
  • 223
    • 84907495558 scopus 로고    scopus 로고
    • Acute myocardial infarct size is related to periodontitis extent and severity
    • Marfil-Alvarez R, Mesa F, Arrebola-Moreno A, et al. Acute myocardial infarct size is related to periodontitis extent and severity. J Dent Res 2014; 93: 993-998.
    • (2014) J Dent Res , vol.93 , pp. 993-998
    • Marfil-Alvarez, R.1    Mesa, F.2    Arrebola-Moreno, A.3
  • 225
    • 33644863710 scopus 로고    scopus 로고
    • Periodontal tissues in health and disease: Introduction
    • Bartold PM,. Periodontal tissues in health and disease: introduction. Periodontol 2000 2006; 40: 7-10.
    • (2006) Periodontol 2000 , vol.40 , pp. 7-10
    • Bartold, P.M.1
  • 226
    • 33644851481 scopus 로고    scopus 로고
    • Structure of periodontal tissues in health and disease
    • Nanci A, Bosshardt DD,. Structure of periodontal tissues in health and disease. Periodontol 2000 2006; 40: 11-28.
    • (2006) Periodontol 2000 , vol.40 , pp. 11-28
    • Nanci, A.1    Bosshardt, D.D.2
  • 227
    • 0034648768 scopus 로고    scopus 로고
    • Atherosclerosis
    • Lusis AJ,. Atherosclerosis. Nature 2000; 407: 233-241.
    • (2000) Nature , vol.407 , pp. 233-241
    • Lusis, A.J.1
  • 228
    • 1642390201 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A review of their structure and role in acute coronary syndrome
    • Jones CB, Sane DC, Herrington DM,. Matrix metalloproteinases: a review of their structure and role in acute coronary syndrome. Cardiovasc Res 2003; 59: 812-823.
    • (2003) Cardiovasc Res , vol.59 , pp. 812-823
    • Jones, C.B.1    Sane, D.C.2    Herrington, D.M.3
  • 229
    • 0028139999 scopus 로고
    • Reduction of matrix metalloproteinase 8-neutrophil collagenase levels during long-term doxycycline treatment of reactive arthritis
    • Lauhio A, Konttinen YT, Tschesche H, et al. Reduction of matrix metalloproteinase 8-neutrophil collagenase levels during long-term doxycycline treatment of reactive arthritis. Antimicrob Agents Chemother 1994; 38: 400-402.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 400-402
    • Lauhio, A.1    Konttinen, Y.T.2    Tschesche, H.3
  • 230
    • 0027942457 scopus 로고
    • In vivo inhibition of human neutrophil collagenase (MMP-8) activity during long-term combination therapy of doxycycline and non-steroidal anti-inflammatory drugs (NSAID) in acute reactive arthritis
    • Lauhio A, Salo T, Ding Y, et al. In vivo inhibition of human neutrophil collagenase (MMP-8) activity during long-term combination therapy of doxycycline and non-steroidal anti-inflammatory drugs (NSAID) in acute reactive arthritis. Clin Exp Immunol 1994; 98: 21-28.
    • (1994) Clin Exp Immunol , vol.98 , pp. 21-28
    • Lauhio, A.1    Salo, T.2    Ding, Y.3
  • 231
    • 84879219355 scopus 로고    scopus 로고
    • Subantimicrobial-dose doxycycline treatment increases serum cholesterol efflux capacity from macrophages
    • Salminen A, Pussinen PJ, Payne JB, et al. Subantimicrobial-dose doxycycline treatment increases serum cholesterol efflux capacity from macrophages. Inflamm Res 2013; 62: 711-720.
    • (2013) Inflamm Res , vol.62 , pp. 711-720
    • Salminen, A.1    Pussinen, P.J.2    Payne, J.B.3
  • 232
    • 0032200444 scopus 로고    scopus 로고
    • Tetracyclines inhibit connective tissue breakdown by multiple non-antimicrobial mechanisms
    • Golub LM, Lee HM, Ryan ME, et al. Tetracyclines inhibit connective tissue breakdown by multiple non-antimicrobial mechanisms. Adv Dent Res 1998; 12: 12-26.
    • (1998) Adv Dent Res , vol.12 , pp. 12-26
    • Golub, L.M.1    Lee, H.M.2    Ryan, M.E.3
  • 233
    • 4744366846 scopus 로고    scopus 로고
    • TIMP-1 stimulates proliferation of human aortic smooth muscle cells and Ras effector pathways
    • Akahane T, Akahane M, Shah A, et al. TIMP-1 stimulates proliferation of human aortic smooth muscle cells and Ras effector pathways. Biochem Biophys Res Commun 2004; 324: 440-445.
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 440-445
    • Akahane, T.1    Akahane, M.2    Shah, A.3
  • 234
    • 84899650162 scopus 로고    scopus 로고
    • The effect of prolonged systemic doxycycline therapy on serum tissue degrading proteinases in coronary bypass patients: A randomized, double-masked, placebo-controlled clinical trial
    • Kormi I, Alfakry H, Tervahartiala T, et al. The effect of prolonged systemic doxycycline therapy on serum tissue degrading proteinases in coronary bypass patients: a randomized, double-masked, placebo-controlled clinical trial. Inflamm Res 2014; 63: 329-334.
    • (2014) Inflamm Res , vol.63 , pp. 329-334
    • Kormi, I.1    Alfakry, H.2    Tervahartiala, T.3
  • 235
    • 80054091646 scopus 로고    scopus 로고
    • Serum MMP-8, -9 and TIMP-1 in sepsis: High serum levels of MMP-8 and TIMP-1 are associated with fatal outcome in a multicentre, prospective cohort study. Hypothetical impact of tetracyclines
    • Lauhio A, Hästbacka J, Pettila V, et al. Serum MMP-8, -9 and TIMP-1 in sepsis: high serum levels of MMP-8 and TIMP-1 are associated with fatal outcome in a multicentre, prospective cohort study. Hypothetical impact of tetracyclines. Pharmacol Res 2011; 64: 590-594.
    • (2011) Pharmacol Res , vol.64 , pp. 590-594
    • Lauhio, A.1    Hästbacka, J.2    Pettila, V.3
  • 236
    • 77649228649 scopus 로고    scopus 로고
    • Association of gingival crevicular fluid biomarkers during periodontal maintenance with subsequent progressive periodontitis
    • Reinhardt RA, Stoner JA, Golub LM, et al. Association of gingival crevicular fluid biomarkers during periodontal maintenance with subsequent progressive periodontitis. J Periodontol 2010; 81: 251-259.
    • (2010) J Periodontol , vol.81 , pp. 251-259
    • Reinhardt, R.A.1    Stoner, J.A.2    Golub, L.M.3
  • 237
    • 84866789438 scopus 로고    scopus 로고
    • Proof of concept: Matrix metalloproteinase inhibitor decreases inflammation and improves muscle insulin sensitivity in people with type 2 diabetes
    • Frankwich K, Tibble C, Torres-Gonzalez M, et al. Proof of concept: matrix metalloproteinase inhibitor decreases inflammation and improves muscle insulin sensitivity in people with type 2 diabetes. J Inflamm (Lond) 2012; 9: 35-35.
    • (2012) J Inflamm (Lond) , vol.9 , pp. 35-35
    • Frankwich, K.1    Tibble, C.2    Torres-Gonzalez, M.3
  • 238
    • 49849083714 scopus 로고    scopus 로고
    • Proteinase activity and receptor cleavage: Mechanism for insulin resistance in the spontaneously hypertensive rat
    • DeLano FA, Schmid-Schonbein GW,. Proteinase activity and receptor cleavage: mechanism for insulin resistance in the spontaneously hypertensive rat. Hypertension 2008; 52: 415-423.
    • (2008) Hypertension , vol.52 , pp. 415-423
    • DeLano, F.A.1    Schmid-Schonbein, G.W.2
  • 239
    • 27744585664 scopus 로고    scopus 로고
    • Safety of doxycycline and minocycline: A systematic review
    • Smith K, Leyden JJ,. Safety of doxycycline and minocycline: a systematic review. Clin Ther 2005; 27: 1329-1342.
    • (2005) Clin Ther , vol.27 , pp. 1329-1342
    • Smith, K.1    Leyden, J.J.2
  • 240
    • 84877125152 scopus 로고    scopus 로고
    • Therapeutic effects of alpha lipoic acid and Vitamin C on alveolar bone resorption after experimental periodontitis in rats: A biochemical, histochemical, and stereologic study
    • Akman S, Canakci V, Kara A, et al. Therapeutic effects of alpha lipoic acid and vitamin C on alveolar bone resorption after experimental periodontitis in rats: a biochemical, histochemical, and stereologic study. J Periodontol 2013; 84: 666-674.
    • (2013) J Periodontol , vol.84 , pp. 666-674
    • Akman, S.1    Canakci, V.2    Kara, A.3
  • 241
    • 65549118885 scopus 로고    scopus 로고
    • Myeloperoxidase as inflammatory marker of periodontal disease: Experimental study in rats
    • Gomes DA, Pires JR, Zuza EP, et al. Myeloperoxidase as inflammatory marker of periodontal disease: experimental study in rats. Immunol Invest 2009; 38: 117-122.
    • (2009) Immunol Invest , vol.38 , pp. 117-122
    • Gomes, D.A.1    Pires, J.R.2    Zuza, E.P.3
  • 242
    • 84914150614 scopus 로고    scopus 로고
    • Influence of parstatin on experimental periodontal disease and repair in rats
    • Spolidorio LC, Lucas PD, Steffens JP, et al. Influence of parstatin on experimental periodontal disease and repair in rats. J Periodontol 2014; 85: 1266-1274.
    • (2014) J Periodontol , vol.85 , pp. 1266-1274
    • Spolidorio, L.C.1    Lucas, P.D.2    Steffens, J.P.3
  • 243
    • 84884676199 scopus 로고    scopus 로고
    • Olmesartan decreases IL-1beta and TNF-alpha levels; Downregulates MMP-2, MMP-9, COX-2, and RANKL; And upregulates OPG in experimental periodontitis
    • Araujo AA, Lopes de Souza G, Souza TO, et al. Olmesartan decreases IL-1beta and TNF-alpha levels; downregulates MMP-2, MMP-9, COX-2, and RANKL; and upregulates OPG in experimental periodontitis. Naunyn Schmiedebergs Arch Pharmacol 2013; 386: 875-884.
    • (2013) Naunyn Schmiedebergs Arch Pharmacol , vol.386 , pp. 875-884
    • Araujo, A.A.1    Lopes De Souza, G.2    Souza, T.O.3
  • 244
    • 84901274544 scopus 로고    scopus 로고
    • Azilsartan increases levels of IL-10, down-regulates MMP-2, MMP-9, RANKL/RANK, Cathepsin K and up-regulates OPG in an experimental periodontitis model
    • Araujo AA, Varela H, Brito GA, et al. Azilsartan increases levels of IL-10, down-regulates MMP-2, MMP-9, RANKL/RANK, Cathepsin K and up-regulates OPG in an experimental periodontitis model. PLoS One 2014; 9: e96750-e96750.
    • (2014) PLoS One , vol.9 , pp. e96750-e96750
    • Araujo, A.A.1    Varela, H.2    Brito, G.A.3
  • 245
    • 84879772484 scopus 로고    scopus 로고
    • Carvedilol decrease IL-1beta and TNF-alpha, inhibits MMP-2, MMP-9, COX-2, and RANKL expression, and up-regulates OPG in a rat model of periodontitis
    • de Araujo Junior RF, Souza TO, de Medeiros CA, et al. Carvedilol decrease IL-1beta and TNF-alpha, inhibits MMP-2, MMP-9, COX-2, and RANKL expression, and up-regulates OPG in a rat model of periodontitis. PLoS One 2013; 8: e66391-e66391.
    • (2013) PLoS One , vol.8 , pp. e66391-e66391
    • De Araujo Junior, R.F.1    Souza, T.O.2    De Medeiros, C.A.3
  • 246
    • 84885395127 scopus 로고    scopus 로고
    • Atorvastatin decreases bone loss, inflammation and oxidative stress in experimental periodontitis
    • de Araujo Junior RF, Souza TO, de Moura LM, et al. Atorvastatin decreases bone loss, inflammation and oxidative stress in experimental periodontitis. PLoS One 2013; 8: e75322-e75322.
    • (2013) PLoS One , vol.8 , pp. e75322-e75322
    • De Araujo Junior, R.F.1    Souza, T.O.2    De Moura, L.M.3
  • 247
    • 81055147533 scopus 로고    scopus 로고
    • Nafamostat mesilate, a potent tryptase inhibitor, modulates periodontitis in rats
    • Holzhausen M, Balejo RD, Lara GM, et al. Nafamostat mesilate, a potent tryptase inhibitor, modulates periodontitis in rats. Clin Oral Investig 2011; 15: 967-973.
    • (2011) Clin Oral Investig , vol.15 , pp. 967-973
    • Holzhausen, M.1    Balejo, R.D.2    Lara, G.M.3
  • 248
    • 84891827222 scopus 로고    scopus 로고
    • Low-dose combination of alendronate and atorvastatin reduces ligature-induced alveolar bone loss in rats
    • Goes P, Melo IM, Silva LM, et al. Low-dose combination of alendronate and atorvastatin reduces ligature-induced alveolar bone loss in rats. J Periodontal Res 2014; 49: 45-54.
    • (2014) J Periodontal Res , vol.49 , pp. 45-54
    • Goes, P.1    Melo, I.M.2    Silva, L.M.3
  • 249
    • 18044395737 scopus 로고    scopus 로고
    • Statins downregulate myeloperoxidase gene expression in macrophages
    • Kumar AP, Reynolds WF,. Statins downregulate myeloperoxidase gene expression in macrophages. Biochem Biophys Res Commun 2005; 331: 442-451.
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 442-451
    • Kumar, A.P.1    Reynolds, W.F.2
  • 250
    • 84882288944 scopus 로고    scopus 로고
    • Protective mechanisms of simvastatin in experimental periodontal disease
    • Dalcico R, de Menezes AM, Deocleciano OB, et al. Protective mechanisms of simvastatin in experimental periodontal disease. J Periodontol 2013; 84: 1145-1157.
    • (2013) J Periodontol , vol.84 , pp. 1145-1157
    • Dalcico, R.1    De Menezes, A.M.2    Deocleciano, O.B.3
  • 251
    • 84893127676 scopus 로고    scopus 로고
    • The impact of type 2 diabetes and atorvastatin treatment on serum levels of MMP-7 and MMP-8
    • Kadoglou NP, Sailer N, Fotiadis G, et al. The impact of type 2 diabetes and atorvastatin treatment on serum levels of MMP-7 and MMP-8. Exp Clin Endocrinol Diabetes 2014; 122: 44-49.
    • (2014) Exp Clin Endocrinol Diabetes , vol.122 , pp. 44-49
    • Kadoglou, N.P.1    Sailer, N.2    Fotiadis, G.3
  • 252
    • 36048970075 scopus 로고    scopus 로고
    • Myeloperoxidase: A target for new drug development?
    • Malle E, Furtmuller PG, Sattler W, et al. Myeloperoxidase: a target for new drug development? Br J Pharmacol 2007; 152: 838-854.
    • (2007) Br J Pharmacol , vol.152 , pp. 838-854
    • Malle, E.1    Furtmuller, P.G.2    Sattler, W.3
  • 253
    • 3342943466 scopus 로고    scopus 로고
    • Supplementary taurine may stabilize atheromatous plaque by antagonizing the activation of metalloproteinases by hypochlorous acid
    • McCarty MF,. Supplementary taurine may stabilize atheromatous plaque by antagonizing the activation of metalloproteinases by hypochlorous acid. Med Hypotheses 2004; 63: 414-418.
    • (2004) Med Hypotheses , vol.63 , pp. 414-418
    • McCarty, M.F.1
  • 254
    • 84940391482 scopus 로고    scopus 로고
    • Salivary matrix metalloproteinase-8 and -9 and myeloperoxidase in relation to coronary heart and periodontal diseases: A subgroup report from the PAROKRANK study (periodontitis and its relation to coronary artery disease)
    • Rathnayake N, Gustafsson A, Norhammar A, et al. Salivary matrix metalloproteinase-8 and -9 and myeloperoxidase in relation to coronary heart and periodontal diseases: a subgroup report from the PAROKRANK study (periodontitis and its relation to coronary artery disease). PLoS One 2015; 10: e0126370-e0126370.
    • (2015) PLoS One , vol.10 , pp. e0126370-e0126370
    • Rathnayake, N.1    Gustafsson, A.2    Norhammar, A.3
  • 255
    • 0037133346 scopus 로고    scopus 로고
    • Porphyromonas gingivalis infection accelerates the progression of atherosclerosis in a heterozygous apolipoprotein E-deficient murine model
    • Li L, Messas E, Batista EL Jr, et al. Porphyromonas gingivalis infection accelerates the progression of atherosclerosis in a heterozygous apolipoprotein E-deficient murine model. Circulation 2002; 105: 861-867.
    • (2002) Circulation , vol.105 , pp. 861-867
    • Li, L.1    Messas, E.2    Batista, E.L.J.3
  • 256
    • 84861585150 scopus 로고    scopus 로고
    • Elevated serum myeloperoxidase activities are significantly associated with the prevalence of ACS and High LDL-C levels in CHD patients
    • Liu C, Xie G, Huang W, et al. Elevated serum myeloperoxidase activities are significantly associated with the prevalence of ACS and High LDL-C levels in CHD patients. J Atheroscler Thromb 2012; 19: 435-443.
    • (2012) J Atheroscler Thromb , vol.19 , pp. 435-443
    • Liu, C.1    Xie, G.2    Huang, W.3
  • 257
    • 43949112974 scopus 로고    scopus 로고
    • Postprandial serum induces apoptosis in endothelial cells: Role of polymorphonuclear-derived myeloperoxidase and metalloproteinase-9 activity
    • Spallarossa P, Garibaldi S, Barisione C, et al. Postprandial serum induces apoptosis in endothelial cells: Role of polymorphonuclear-derived myeloperoxidase and metalloproteinase-9 activity. Atherosclerosis 2008; 198: 458-467.
    • (2008) Atherosclerosis , vol.198 , pp. 458-467
    • Spallarossa, P.1    Garibaldi, S.2    Barisione, C.3
  • 258
    • 84864325532 scopus 로고    scopus 로고
    • The association of serum neutrophil markers and acute coronary syndrome
    • Alfakry H, Sinisalo J, Paju S, et al. The association of serum neutrophil markers and acute coronary syndrome. Scand J Immunol 2012; 76: 181-187.
    • (2012) Scand J Immunol , vol.76 , pp. 181-187
    • Alfakry, H.1    Sinisalo, J.2    Paju, S.3
  • 259
    • 77958538075 scopus 로고    scopus 로고
    • Oxidative stress, systemic inflammation, and severe periodontitis
    • D'Aiuto F, Nibali L, Parkar M, et al. Oxidative stress, systemic inflammation, and severe periodontitis. J Dent Res 2010; 89: 1241-1246.
    • (2010) J Dent Res , vol.89 , pp. 1241-1246
    • D'Aiuto, F.1    Nibali, L.2    Parkar, M.3


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