메뉴 건너뛰기




Volumn 15, Issue , 2012, Pages 84-98

Antimicrobial peptides in periodontal innate defense

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; BACTERIAL TOXIN; BIOLOGICAL MARKER; BPIFA2 PROTEIN, HUMAN; LEUKOCYTE ELASTASE INHIBITOR; SALIVA PROTEIN;

EID: 84855522617     PISSN: 14202433     EISSN: 16623770     Source Type: Book Series    
DOI: 10.1159/000329673     Document Type: Article
Times cited : (76)

References (101)
  • 1
    • 0035949276 scopus 로고    scopus 로고
    • The oral cleanliness and periodontal health of UK adults in 1998
    • Morris AJ, Steele J, White DA: The oral cleanliness and periodontal health of UK adults in 1998. Br Dent J 2001;191:186-192. (Pubitemid 33755285)
    • (2001) British Dental Journal , vol.191 , Issue.4 , pp. 186-192
    • Morris, A.J.1
  • 2
    • 77951760725 scopus 로고    scopus 로고
    • Periodontal health in Europe: Future trends based on treatment needs and the provision of periodontal services -Position paper 1
    • Kig J, Holtfreter B, Kocher T: Periodontal health in Europe: future trends based on treatment needs and the provision of periodontal services -position paper 1. Eur J Dent Educ 2010;14:4-24.
    • (2010) Eur J Dent Educ , vol.14 , pp. 4-24
    • Kig, J.1    Holtfreter, B.2    Kocher, T.3
  • 3
    • 33747853795 scopus 로고    scopus 로고
    • The breadth of bacterial diversity in the human periodontal pocket and other oral sites
    • Paster BJ, Olsen I, Aas JA, Dewhirst FE: The breadth of bacterial diversity in the human periodontal pocket and other oral sites. Periodontol 2000 2006; 42:80-87.
    • (2000) Periodontol , vol.2006 , Issue.42 , pp. 80-87
    • Paster, B.J.1    Olsen, I.2    Aas, J.A.3    Dewhirst, F.E.4
  • 4
    • 0030280520 scopus 로고    scopus 로고
    • Periodontics WWoC Consensus report Periodontal diseases: Pathogenesis and microbial factors
    • Periodontics WWoC: Consensus report. Periodontal diseases: pathogenesis and microbial factors. Ann Periodontol 1996;1:926-932.
    • (1996) Ann Periodontol , vol.1 , pp. 926-932
  • 6
    • 33747835523 scopus 로고    scopus 로고
    • Microbiological goals of periodontal therapy
    • Teles RP, Haffajee AD, Socransky SS: Microbiological goals of periodontal therapy. Periodontol 2000 2006; 42:180-218.
    • (2000) Periodontol , vol.2006 , Issue.42 , pp. 180-218
    • Teles, R.P.1    Haffajee, A.D.2    Socransky, S.S.3
  • 7
    • 2442643113 scopus 로고    scopus 로고
    • Dental Plaque revisited: Bacteria associated with Periodontal Disease
    • Lovegrove JM: Dental plaque revisited: Bacteria associated with periodontal disease. J N Z Soc Periodontol 2004:7-21. (Pubitemid 38707464)
    • (2004) Journal- New Zealand Society Of Periodontology , Issue.87 , pp. 7-21
    • Lovegrove, J.M.1
  • 8
    • 34548555687 scopus 로고    scopus 로고
    • Control of inflammation and periodontitis
    • Van Dyke TE: Control of inflammation and periodontitis. Periodontology 2000 2007;45:158-166.
    • (2000) Periodontology , vol.2007 , Issue.45 , pp. 158-166
    • Van Dyke, T.E.1
  • 10
    • 69149102398 scopus 로고    scopus 로고
    • Antimicrobial peptides of the oral cavity
    • Gorr S-U: Antimicrobial peptides of the oral cavity. Periodontol 2000 2009;51:152-180.
    • (2000) Periodontol , vol.2009 , Issue.51 , pp. 152-180
    • Gorr, S.-U.1
  • 11
    • 0037068959 scopus 로고    scopus 로고
    • Deficiency of antibacterial peptides in patients with morbus Kostmann: An observation study
    • DOI 10.1016/S0140-6736(02)11201-3
    • Putsep K, Carlsson G, Boman HG, Andersson M: Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study. Lancet 2002;360:1144-1149. (Pubitemid 35246490)
    • (2002) Lancet , vol.360 , Issue.9340 , pp. 1144-1149
    • Putsep, K.1    Carlsson, G.2    Boman, H.G.3    Andersson, M.4
  • 12
    • 33748042966 scopus 로고    scopus 로고
    • Role of polymorphonuclear leukocyte-derived serine proteinases in defense against Actinobacillus actinomycetemcomitans
    • DOI 10.1128/IAI.02016-05
    • de Haar SF, Hiemstra PS, van Steenbergen MTJM, Everts V, Beertsen W: Role of polymorphonuclear leukocyte-derived serine proteinases in defense against actinobacillus actinomycetemcomitans. Infect Immun 2006;74:5284-5291. (Pubitemid 44300447)
    • (2006) Infection and Immunity , vol.74 , Issue.9 , pp. 5284-5291
    • De Haar, S.F.1    Hiemstra, P.S.2    Van Steenbergen, M.T.J.M.3    Everts, V.4    Beertsen, W.5
  • 16
    • 79951917226 scopus 로고    scopus 로고
    • Antimicrobial peptides and periodontal disease
    • Gorr SU, Abdolhosseini M: Antimicrobial peptides and periodontal disease. J Clin Periodontol 2011;38: 126-141.
    • J Clin Periodontol , vol.2011 , Issue.38 , pp. 126-141
    • Gorr, S.U.1    Abdolhosseini, M.2
  • 18
    • 69249096200 scopus 로고    scopus 로고
    • The roles of antimicrobial peptides in innate host defense
    • Diamond G, Beckloff N, Weinberg A, Kisich KO: The roles of antimicrobial peptides in innate host defense. Curr Pharm Des 2009;15:2377-2392.
    • (2009) Curr Pharm des , vol.15 , pp. 2377-2392
    • Diamond, G.1    Beckloff, N.2    Weinberg, A.3    Kisich, K.O.4
  • 19
    • 67651101168 scopus 로고    scopus 로고
    • Alarmins and antimicrobial immunity
    • Yang D, Oppenheim JJ: Alarmins and antimicrobial immunity. Med Mycol 2009;47:S146-S153.
    • (2009) Med Mycol , vol.47
    • Yang, D.1    Oppenheim, J.J.2
  • 20
    • 70949104973 scopus 로고    scopus 로고
    • Direct and alternative antimicrobial mechanisms of neutrophil-derived granule proteins
    • Soehnlein O: Direct and alternative antimicrobial mechanisms of neutrophil-derived granule proteins. J Mol Med 2009;87:1157-1164.
    • (2009) J Mol Med , vol.87 , pp. 1157-1164
    • Soehnlein, O.1
  • 21
    • 42649142893 scopus 로고    scopus 로고
    • The role of the multifunctional peptide LL-37 in host defense
    • DOI 10.2741/2964
    • Kai-Larsen Y, Agerberth B: The role of the multifunctional peptide ll-37 in host defense. Front Biosci 2008;13:3760-3767. (Pubitemid 351594656)
    • (2008) Frontiers in Bioscience , vol.13 , Issue.10 , pp. 3760-3767
    • Kai-Larsen, Y.1    Agerberth, B.2
  • 24
    • 45149091570 scopus 로고    scopus 로고
    • Analysis of neutrophil-derived antimicrobial peptides in gingival crevicular fluid suggests importance of cathelicidin LL-37 in the innate immune response against periodontogenic bacteria
    • DOI 10.1111/j.1399-302X.2008.00433.x
    • Puklo M, Guentsch A, Hiemstra PS, Eick S, Potempa J: Analysis of neutrophil-derived antimicrobial peptides in gingival crevicular fluid suggests importance of cathelicidin ll-37 in the innate immune response against periodontogenic bacteria. Oral Microbiol Immunol 2008;23:328-335. (Pubitemid 351832179)
    • (2008) Oral Microbiology and Immunology , vol.23 , Issue.4 , pp. 328-335
    • Puklo, M.1    Guentsch, A.2    Hiemstra, P.S.3    Eick, S.4    Potempa, J.5
  • 25
    • 67649964706 scopus 로고    scopus 로고
    • Gingival crevicular fluid levels of cathelicidin ll-37 and interleukin-18 in patients with chronic periodontitis
    • Turkoglu O, Emingil G, Kutukculer N, Atilla G: Gingival crevicular fluid levels of cathelicidin ll-37 and interleukin-18 in patients with chronic periodontitis. J Periodontol 2009;80:969-976.
    • (2009) J Periodontol , vol.80 , pp. 969-976
    • Turkoglu, O.1    Emingil, G.2    Kutukculer, N.3    Atilla, G.4
  • 27
    • 0033926971 scopus 로고    scopus 로고
    • Sensitivity of Actinobacillus actinomycetemcomitans and Capnocytophaga spp. to the bactericidal action of LL-37: A cathelicidin found in human leukocytes and epithelium
    • Tanaka D, Miyasaki KT, Lehrer RI: Sensitivity of Actinobacillus actinomycetemcomitans and Capnocytophaga spp. to the bactericidal action of LL-37: a cathelicidin found in human leukocytes and epithelium. Oral Microbiol Immunol 2000;15: 226-231. (Pubitemid 30466488)
    • (2000) Oral Microbiology and Immunology , vol.15 , Issue.4 , pp. 226-231
    • Tanaka, D.1    Miyasaki, K.T.2    Lehrer, R.I.3
  • 28
    • 30744475282 scopus 로고    scopus 로고
    • The mammalian ionic environment dictates microbial susceptibility to antimicrobial defense peptides
    • DOI 10.1096/fj.05-4406com
    • Dorschner RA, Lopez-Garcia B, Peschel A, Kraus D, Morikawa K, Nizet V, Gallo RL: The mammalian ionic environment dictates microbial susceptibility to antimicrobial defense peptides. FASEB J 2006;20: 35-42. (Pubitemid 43100473)
    • (2006) FASEB Journal , vol.20 , Issue.1 , pp. 35-42
    • Dorschner, R.A.1    Lopez-Garcia, B.2    Peschel, A.3    Kraus, D.4    Morikawa, K.5    Nizet, V.6    Gallo, R.L.7
  • 29
    • 34548230420 scopus 로고    scopus 로고
    • Susceptibility of various oral bacteria to antimicrobial peptides and to phagocytosis by neutrophils
    • Ji S, Hyun J, Park E, Lee BL, Kim KK, Choi Y: Susceptibility of various oral bacteria to antimicrobial peptides and to phagocytosis by neutrophils. J Periodontal Res 2007;42:410-419.
    • (2007) J Periodontal Res , vol.42 , pp. 410-419
    • Ji, S.1    Hyun, J.2    Park, E.3    Lee, B.L.4    Kim, K.K.5    Choi, Y.6
  • 30
    • 72449155528 scopus 로고    scopus 로고
    • Saliva enables the antimicrobial activity of LL-37 in the presence of proteases of porphyromonas gingivalis
    • Gutner M, Chaushu S, Balter D, Bachrach G: Saliva enables the antimicrobial activity of LL-37 in the presence of proteases of porphyromonas gingivalis. Infect Immun 2009;77:5558-5563.
    • (2009) Infect Immun , vol.77 , pp. 5558-5563
    • Gutner, M.1    Chaushu, S.2    Balter, D.3    Bachrach, G.4
  • 31
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule-and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • Yang D, Chen Q, Schmidt AP, Anderson GM, Wang JM, Wooters J, Oppenheim JJ, Chertov O: LL-37, the neutrophil granule-and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J Exp Med 2000;192:1069-1074.
    • (2000) J Exp Med , vol.192 , pp. 1069-1074
    • Yang, D.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.6    Oppenheim, J.J.7    Chertov, O.8
  • 35
    • 46449087690 scopus 로고    scopus 로고
    • Cathelicidin stimulates colonic mucus synthesis by up-regulating MUC1 and MUC2 expression through a mitogen-activated protein kinase pathway
    • Tai EKK, Wong HPS, Lam EKY, Wu WKK, Yu L, Koo MWL, Cho CH: Cathelicidin stimulates colonic mucus synthesis by up-regulating MUC1 and MUC2 expression through a mitogen-activated protein kinase pathway. J Cell Biochem 2008; 104: 251-258.
    • (2008) J Cell Biochem , vol.104 , pp. 251-258
    • Ekk, T.1    Hps, W.2    Eky, L.3    Wkk, W.4    Yu, L.5    Mwl, K.6    Cho, C.H.7
  • 36
    • 47249162101 scopus 로고    scopus 로고
    • Salivary mucins inhibit antibacterial activity of the cathelicidin-derived LL-37 peptide but not the cationic steroid CSA-13
    • Bucki R, Namiot DB, Namiot Z, Savage PB, Janmey PA: Salivary mucins inhibit antibacterial activity of the cathelicidin-derived LL-37 peptide but not the cationic steroid CSA-13. J Antimicrob Chemother 2008;62:329-225.
    • (2008) J Antimicrob Chemother , vol.62 , pp. 329-225
    • Bucki, R.1    Namiot, D.B.2    Namiot, Z.3    Savage, P.B.4    Janmey, P.A.5
  • 38
    • 78649605533 scopus 로고    scopus 로고
    • Suppressive effect of the antimicrobial peptide LL-37 on expression of IL-6, IL-8 and CXCL10 induced by Porphyromonas gingivalis cells and extracts in human gingival fibroblasts
    • Inomata M, Into T, Murakami Y: Suppressive effect of the antimicrobial peptide LL-37 on expression of IL-6, IL-8 and CXCL10 induced by Porphyromonas gingivalis cells and extracts in human gingival fibroblasts. Eur J Oral Sci 2010;118:574-581.
    • Eur J Oral Sci , vol.2010 , Issue.118 , pp. 574-581
    • Inomata, M.1    Into, T.2    Murakami, Y.3
  • 39
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • DOI 10.1038/nri1180
    • Ganz T: Defensins: antimicrobial peptides of innate immunity. Nat Rev Immunol 2003;3:710-720. (Pubitemid 41070812)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 40
    • 34548222649 scopus 로고    scopus 로고
    • Antimicrobial activity of truncated α-defensin (human neutrophil peptide (HNP)-1) analogues without disulphide bridges
    • DOI 10.1016/j.molimm.2007.04.018, PII S0161589007001769
    • Lundy FT, Nelson J, Lockhart D, Greer B, Harriott P, Marley JJ: Antimicrobial activity of truncated [alpha]-defensin (human neutrophil peptide (HNP)-1) analogues without disulphide bridges. Mol Immunol 2008;45:190-193. (Pubitemid 47331643)
    • (2008) Molecular Immunology , vol.45 , Issue.1 , pp. 190-193
    • Lundy, F.T.1    Nelson, J.2    Lockhart, D.3    Greer, B.4    Harriott, P.5    Marley, J.J.6
  • 41
    • 0034194257 scopus 로고    scopus 로고
    • Large-scale synthesis and functional elements for the antimicrobial activity of defensins
    • DOI 10.1042/0264-6021:3470633
    • Raj PA, Antonyraj KJ, Karunakaran T: Large-scale synthesis and functional elements for the antimicrobial activity of defensins. Biochem J 2000;347(part 3):633-641. (Pubitemid 30260951)
    • (2000) Biochemical Journal , vol.347 , Issue.3 , pp. 633-641
    • Raj, P.A.1    Antonyraj, K.J.2    Karunakaran, T.3
  • 42
    • 0025690257 scopus 로고
    • In vitro sensitivity of oral, gram-negative, facultative bacteria to the bactericidal activity of human neutrophil defensins
    • Miyasaki KT, Bodeau AL, Ganz T, Selsted ME, Lehrer RI: In vitro sensitivity of oral, gram-negative, facultative bacteria to the bactericidal activity of human neutrophil defensins. Infect Immun 1990;58: 3934-3940.
    • (1990) Infect Immun , vol.58 , pp. 3934-3940
    • Miyasaki, K.T.1    Bodeau, A.L.2    Ganz, T.3    Selsted, M.E.4    Lehrer, R.I.5
  • 43
    • 0036208192 scopus 로고    scopus 로고
    • Epithelial cell-derived human β-defensin-2 acts as a chemotaxin for mast cells through a pertussis toxin-sensitive and phospholipase C-dependent pathway
    • Niyonsaba F, Iwabuchi K, Matsuda H, Ogawa H, Nagaoka I: Epithelial cell-derived human β-defensin-2 acts as a chemotaxin for mast cells through a pertussis toxin-sensitive and phospholipase c-dependent pathway. Int Immunol 2002;14: 421-426. (Pubitemid 34257769)
    • (2002) International Immunology , vol.14 , Issue.4 , pp. 421-426
    • Niyonsaba, F.1    Iwabuchi, K.2    Matsuda, H.3    Ogawa, H.4    Nagaoka, I.5
  • 44
    • 72449156168 scopus 로고    scopus 로고
    • Antibacterial and lipopolysaccharide (LPS)-neutralising activity of human cationic antimicrobial peptides against periodontopathogens
    • Lee SH, Jun HK, Lee HR, Chung CP, Choi BK: Antibacterial and lipopolysaccharide (LPS)-neutralising activity of human cationic antimicrobial peptides against periodontopathogens. Int J Antimicrob Agents 2010;35:138-145.
    • Int J Antimicrob Agents , vol.2010 , Issue.35 , pp. 138-145
    • Lee, S.H.1    Jun, H.K.2    Lee, H.R.3    Chung, C.P.4    Choi, B.K.5
  • 45
    • 24344438507 scopus 로고    scopus 로고
    • Differential induction of human beta-defensin expression by periodontal commensals and pathogens in periodontal pocket epithelial cells
    • DOI 10.1902/jop.2005.76.8.1293
    • Vankeerberghen A, Nuytten H, Dierickx K, Quirynen M, Cassiman JJ, Cuppens H: Differential induction of human beta-defensin expression by periodontal commensals and pathogens in periodontal pocket epithelial cells. J Periodontol 2005; 76:1293-1303. (Pubitemid 41245773)
    • (2005) Journal of Periodontology , vol.76 , Issue.8 , pp. 1293-1303
    • Vankeerberghen, A.1    Nuytten, H.2    Dierickx, K.3    Quirynen, M.4    Cassiman, J.-J.5    Cuppens, H.6
  • 49
    • 0018962398 scopus 로고
    • Inheritance of a parotid secretory protein in mice and its use in determining salivary amylase quantitative variants
    • Owerbach D, Hjorth JP: Inheritance of a parotid secretory protein in mice and its use in determining salivary amylase quantitative variants. Genetics 1980;95:129-141. (Pubitemid 10012092)
    • (1980) Genetics , vol.95 , Issue.1 , pp. 129-141
    • Owerbach, D.1    Hjorth, J.P.2
  • 50
    • 0024505788 scopus 로고
    • Physical and genetic characterization of a 75-kilobase deletion associated with a(l), a recessive lethal allele at the mouse agouti locus
    • Barsh GS, Epstein CJ: Physical and geneticcharacterization of a 75-kilobase deletion associated with al, a recessive lethal allele at the mouse agouti locus. Genetics 1989;121:811-818. (Pubitemid 19105490)
    • (1989) Genetics , vol.121 , Issue.4 , pp. 811-818
    • Barsh, G.S.1    Epstein, C.J.2
  • 51
    • 0012030796 scopus 로고
    • Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase
    • DOI 10.1073/pnas.83.18.6692
    • Thompson RC, Ohlsson K: Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proc Natl Acad Sci U S A 1986; 83:6692-6696. (Pubitemid 16002300)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.18 , pp. 6692-6696
    • Thompson, R.C.1    Ohlsson, K.2
  • 52
    • 15544374581 scopus 로고    scopus 로고
    • Anti-inflammatory and antimicrobial roles of secretory leukocyte protease inhibitor
    • DOI 10.1128/IAI.73.3.1271-1274.2005
    • Doumas S, Kolokotronis A, Stefanopoulos P: Antiinflammatory and antimicrobial roles of secretory leukocyte protease inhibitor. Infect Immun 2005;73: 1271-1274. (Pubitemid 40470711)
    • (2005) Infection and Immunity , vol.73 , Issue.3 , pp. 1271-1274
    • Doumas, S.1    Kolokotronis, A.2    Stefanopoulos, P.3
  • 53
    • 0036193824 scopus 로고    scopus 로고
    • The presence of elafin, SLPI, IL1-RA and STNFα RI in head and neck squamous cell carcinomas and their relation to the degree of tumour differentiation
    • DOI 10.1080/09629350210304
    • Westin U, Nystrom M, Ljungcrantz I, Eriksson B, Ohlsson K: The presence of elafin, SLPI, IL1-RA and STNFalpha RI in head and neck squamous cell carcinomas and their relation to the degree of tumour differentiation. Mediators Inflamm 2002; 11:7-12. (Pubitemid 34252541)
    • (2002) Mediators of Inflammation , vol.11 , Issue.1 , pp. 7-12
    • Westin, U.1    Nystrom, M.2    Ljungcrantz, I.3    Eriksson, B.4    Ohlsson, K.5
  • 54
    • 0029115952 scopus 로고
    • Secretory leukocyte protease inhibitor: A human saliva protein exhibiting anti-human immunodeficiency virus 1 activity in vitro
    • McNeely TB, Dealy M, Dripps DJ, Orenstein JM, Eisenberg SP, Wahl SM: Secretory leukocyte protease inhibitor: a human saliva protein exhibiting anti-human immunodeficiency virus 1 activity in vitro. J Clin Invest 1995;96:456-464.
    • (1995) J Clin Invest , vol.96 , pp. 456-464
    • McNeely, T.B.1    Dealy, M.2    Dripps, D.J.3    Orenstein, J.M.4    Eisenberg, S.P.5    Wahl, S.M.6
  • 56
    • 0034907705 scopus 로고    scopus 로고
    • Salivary concentration of secretory leukocyte protease inhibitor, an antimicrobial protein, is decreased with advanced age
    • DOI 10.1159/000052808
    • Shugars DC, Watkins CA, Cowen HJ: Salivary concentration of secretory leukocyte protease inhibitor, an antimicrobial protein, is decreased with advanced age. Gerontology 2001;47:246-253. (Pubitemid 32725028)
    • (2001) Gerontology , vol.47 , Issue.5 , pp. 246-253
    • Shugars, D.C.1    Watkins, C.A.2    Cowen, H.J.3
  • 57
    • 3343007202 scopus 로고    scopus 로고
    • Salivary secretory leukocyte protease inhibitor increases in HIV infection
    • DOI 10.1111/j.1600-0714.2004.00218.x
    • Lin AL, Johnson DA, Stephan KT, Yeh C-K: Salivary secretory leukocyte protease inhibitor increases in HIV infection. J Oral Pathol Med 2004;33:410-416. (Pubitemid 38988196)
    • (2004) Journal of Oral Pathology and Medicine , vol.33 , Issue.7 , pp. 410-416
    • Lin, A.L.1    Johnson, D.A.2    Stephan, K.T.3    Yeh, C.-K.4
  • 58
    • 0042866218 scopus 로고    scopus 로고
    • Changes of αI-protease inhibitor and secretory leukocyte protease inhibitor levels in gingival crevicular fluid before and after non-surgical periodontal treatment
    • DOI 10.1034/j.1601-0825.2003.02884.x
    • Nakamura-Minami M, Furuichi Y, Ishikawa K, Mitsuzono-Tofuku Y, Izumi Y: Changes of alpha1-protease inhibitor and secretory leukocyte protease inhibitor levels in gingival crevicular fluid before and after non-surgical periodontal treatment. Oral Dis 2003;9:249-254. (Pubitemid 37047633)
    • (2003) Oral Diseases , vol.9 , Issue.5 , pp. 249-254
    • Nakamura-Minami, M.1    Furuichi, Y.2    Ishikawa, K.3    Mitsuzono-Tofuku, Y.4    Izumi, Y.5
  • 60
    • 0042847135 scopus 로고    scopus 로고
    • Murine macrophages produce secretory leukocyte protease inhibitor during clearance of apoptotic cells: Implications for resolution of the inflammatory response
    • Odaka C, Mizuochi T, Yang J, Ding A: Murine macrophages produce secretory leukocyte protease inhibitor during clearance of apoptotic cells: implications for resolution of the inflammatory response. J Immunol 2003;171:1507-1514. (Pubitemid 36900086)
    • (2003) Journal of Immunology , vol.171 , Issue.3 , pp. 1507-1514
    • Odaka, C.1    Mizuochi, T.2    Yang, J.3    Ding, A.4
  • 61
  • 62
    • 0026802037 scopus 로고
    • Neonatal rat submandibulargland protein SMG-A and parotid secretory protein are alternatively regulated members of a salivary protein multigene family
    • Mirels L, Ball WD: Neonatal rat submandibulargland protein SMG-A and parotid secretory protein are alternatively regulated members of a salivary protein multigene family. J Biol Chem 1992;267: 2679-2687.
    • (1992) J Biol Chem , vol.267 , pp. 2679-2687
    • Mirels, L.1    Ball, W.D.2
  • 63
    • 0041566732 scopus 로고    scopus 로고
    • Expression and anti-bacterial activity of human parotid secretory protein (PSP)
    • DOI 10.1042/BST0310815
    • Geetha C, Venkatesh SG, Fasciotto Dunn BH, Gorr S-U: Expression and anti-bacterial activity of human parotid secretory protein (PSP). Biochem Soc Trans 2003;31:815-818. (Pubitemid 36981134)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.4 , pp. 815-818
    • Geetha, C.1    Venkatesh, S.G.2    Dunn, B.H.3    Gorr, S.-U.4
  • 64
    • 15544376642 scopus 로고    scopus 로고
    • Design and validation of anti-inflammatory peptides from human parotid secretory protein
    • DOI 10.1177/154405910508400208
    • Geetha C, Venkatesh SG, Bingle L, Bingle CD, Gorr SU: Design and validation of anti-inflammatory peptides from human parotid secretory protein. J Dent Res 2005;84:149-153. (Pubitemid 43822047)
    • (2005) Journal of Dental Research , vol.84 , Issue.2 , pp. 149-153
    • Geetha, C.1    Venkatesh, S.G.2    Bingle, L.3    Bingle, C.D.4    Gorr, S.-U.5
  • 67
    • 69249142900 scopus 로고    scopus 로고
    • Initial comparison of proteomic profiles of whole unstimulated saliva obtained from generalized aggressive periodontitis patients and healthy control subjects
    • Wu Y, Shu R, Luo LJ, Ge LH, Xie YF: Initial comparison of proteomic profiles of whole unstimulated saliva obtained from generalized aggressive periodontitis patients and healthy control subjects. J Periodontal Res 2009;44:636-644.
    • (2009) J Periodontal Res , vol.44 , pp. 636-644
    • Wu, Y.1    Shu, R.2    Luo, L.J.3    Ge, L.H.4    Xie, Y.F.5
  • 68
    • 0037091061 scopus 로고    scopus 로고
    • PLUNC: A novel family of candidate host defence proteins expressed in the upper airways and nasopharynx
    • Bingle CD, Craven CJ: PLUNC: a novel family of candidate host defence proteins expressed in the upper airways and nasopharynx. Hum Mol Genet 2002;11:937-943. (Pubitemid 34449781)
    • (2002) Human Molecular Genetics , vol.11 , Issue.8 , pp. 937-943
    • Bingle, C.D.1    Craven, C.J.2
  • 69
    • 4143135448 scopus 로고    scopus 로고
    • Host defense in oral and airway epithelia: Chromosome 20 contributes a new protein family
    • DOI 10.1016/j.biocel.2004.05.002, PII S1357272504001864
    • Bingle CD, Gorr S-U: Host defense in oral and airway epithelia: chromosome 20 contributes a new protein family. Int J Biochem Cell Biol 2004;36:2144-2152. (Pubitemid 39094438)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.11 , pp. 2144-2152
    • Bingle, C.D.1    Gorr, S.-U.2
  • 71
    • 55949094578 scopus 로고    scopus 로고
    • Design of bacteria-agglutinating peptides derived from parotid secretory protein, a member of the bactericidal/permeability increasing-like protein family
    • DOI 10.1016/j.peptides.2008.09.019, PII S0196978108004026
    • Gorr S-U, Sotsky JB, Shelar AP, Demuth DR: Design of bacteria- agglutinating peptides derived from parotid secretory protein, a member of the bactericidal/ permeability increasing-like protein family. Peptides 2008;29:2118-2127. (Pubitemid 50326971)
    • (2008) Peptides , vol.29 , Issue.12 , pp. 2118-2127
    • Gorr, S.-U.1    Sotsky, J.B.2    Shelar, A.P.3    Demuth, D.R.4
  • 73
    • 38949114256 scopus 로고    scopus 로고
    • The bovine salivary proteins BSP30a and BSP30b are independently expressed BPI-like proteins with anti-Pseudomonas activity
    • DOI 10.1016/j.molimm.2007.10.032, PII S0161589007008346
    • Haigh B, Hood K, Broadhurst M, Medele S, Callaghan M, Smolenski G, Dines M, Wheeler T: The bovine salivary proteins BSP30a and BSP30b are independently expressed BPI-like proteins with anti-Pseudomonas activity. Mol Immunol 2007;45: 1944-1951. (Pubitemid 351226276)
    • (2008) Molecular Immunology , vol.45 , Issue.7 , pp. 1944-1951
    • Haigh, B.1    Hood, K.2    Broadhurst, M.3    Medele, S.4    Callaghan, M.5    Smolenski, G.6    Dines, M.7    Wheeler, T.8
  • 75
    • 83555173386 scopus 로고    scopus 로고
    • Human parotid secretory protein is a lipopolysaccharide-binding protein: Identification of an anti-inflammatory peptide domain
    • DOI 10.1007/s11010-011-0991-0992
    • Abdolhosseini M, Sotsky JB, Shelar AP, Joyce PB, Gorr SU: Human parotid secretory protein is a lipopolysaccharide-binding protein: identification of an anti-inflammatory peptide domain. Mol Cell Biochem 2011;DOI 10.1007/s11010-011- 0991-2.
    • (2011) Mol Cell Biochem
    • Abdolhosseini, M.1    Sotsky, J.B.2    Shelar, A.P.3    Joyce, P.B.4    Gorr, S.U.5
  • 78
    • 70449379016 scopus 로고    scopus 로고
    • Saliva: An emerging biofluid for early detection of diseases
    • Lee YH, Wong DT: Saliva: an emerging biofluid for early detection of diseases. Am J Dent 2009;22:241-248.
    • (2009) Am J Dent , vol.22 , pp. 241-248
    • Lee, Y.H.1    Wong, D.T.2
  • 79
    • 78649404957 scopus 로고    scopus 로고
    • Saliva as a diagnostic fluid
    • Malamud D: Saliva as a diagnostic fluid. Dental Clin N Am 2011;55:159-178.
    • Dental Clin N Am , vol.2011 , Issue.55 , pp. 159-178
    • Malamud, D.1
  • 84
    • 33644785995 scopus 로고    scopus 로고
    • Gingival crevicular fluid levels of calprotectin and myeloperoxidase during therapy for generalized aggressive periodontitis
    • DOI 10.1111/j.1600-0765.2005.00849.x
    • Kaner D, Bernimoulin J, Kleber B, Heizmann W, Friedmann A: Gingival crevicular fluid levels of calprotectin and myeloperoxidase during therapy for generalized aggressive periodontitis. J Periodontal Res 2006;41:132-139. (Pubitemid 43341286)
    • (2006) Journal of Periodontal Research , vol.41 , Issue.2 , pp. 132-139
    • Kaner, D.1    Bernimoulin, J.-P.2    Kleber, B.-M.3    Heizmann, W.R.4    Friedmann, A.5
  • 85
    • 0025200926 scopus 로고
    • Antimicrobial polypeptides of human neutrophils
    • Lehrer RI, Ganz T: Antimicrobial polypeptides of human neutrophils. Blood 1990;76:2169-2181.
    • (1990) Blood , vol.76 , pp. 2169-2181
    • Lehrer, R.I.1    Ganz, T.2
  • 87
    • 33644839351 scopus 로고    scopus 로고
    • Radioimmunoassay quantification of adrenomedullin in human gingival crevicular fluid
    • DOI 10.1016/j.archoralbio.2005.08.006, PII S0003996905002177
    • Lundy FT, O'Hare MMT, McKibben BM, Fulton CR, Briggs JE, Linden GJ: Radioimmunoassay quantification of adrenomedullin in human gingival crevicular fluid. Arch Oral Biol 2006;51:334-338. (Pubitemid 43363509)
    • (2006) Archives of Oral Biology , vol.51 , Issue.4 , pp. 334-338
    • Lundy, F.T.1    O'Hare, M.M.T.2    McKibben, B.M.3    Fulton, C.R.4    Briggs, J.E.5    Linden, G.J.6
  • 88
    • 0033152740 scopus 로고    scopus 로고
    • 2-microglobulin, and transforming growth factor-α in gingival crevicular fluid from human periodontal disease
    • DOI 10.1016/S0003-9969(99)00020-5, PII S0003996999000205
    • Mogi M, Otogoto J, Ota N, Inagaki H, Minami M, Kojima K: Interleukin 1[beta], interleukin 6, [beta]2-microglobulin, and transforming growth factor-[alpha] in gingival crevicular fluid from human periodontal disease. Arch Oral Biol 1999;44: 535-539. (Pubitemid 29264475)
    • (1999) Archives of Oral Biology , vol.44 , Issue.6 , pp. 535-539
    • Mogi, M.1    Otogoto, J.2    Ota, N.3    Inagaki, H.4    Minami, M.5    Kojima, K.6
  • 89
    • 34548210843 scopus 로고    scopus 로고
    • Human β-Defensin-1 and -2 expression in the gingiva of patients with specific periodontal diseases
    • Vardar-Sengul S, Demirci T, Sen BH, Erkizan V, Kurulgan E, Baylas H: Human β-defensin-1 and -2 expression in the gingiva of patients with specific periodontal diseases. J Periodontal Res 2007;42:429-437.
    • (2007) J Periodontal Res , vol.42 , pp. 429-437
    • Vardar-Sengul, S.1    Demirci, T.2    Sen, B.H.3    Erkizan, V.4    Kurulgan, E.5    Baylas, H.6
  • 90
    • 0035653754 scopus 로고    scopus 로고
    • Quantitative analysis of MRP-8 in gingival crevicular fluid in periodontal health and disease using microbore HPLC
    • Lundy FT, Chalk R, Lamey P-J, Shaw C, Linden GJ: Quantitative analysis of MRP-8 in gingival crevicular fluid in periodontal health and disease using microbore HPLC. J Clin Periodontol 2001;28:1172-1177. (Pubitemid 33755225)
    • (2001) Journal of Clinical Periodontology , vol.28 , Issue.12 , pp. 1172-1177
    • Lundy, F.T.1    Chalk, R.2    Lamey, P.-J.3    Shaw, C.4    Linden, G.J.5
  • 92
    • 0020770759 scopus 로고
    • Lysozyme and lactoferrin quantitation in the crevicular fluid
    • Friedman SA, Mandel ID, Herrera MS: Lysozyme and lactoferrin quantitation in the crevicular fluid. J Periodontol 1983;54:347-350.
    • (1983) J Periodontol , vol.54 , pp. 347-350
    • Friedman, S.A.1    Mandel, I.D.2    Herrera, M.S.3
  • 93
    • 0026810756 scopus 로고
    • The ability of gingival crevicular fluid acute phase proteins to distinguish healthy, gingivitis and periodontitis sites
    • Adonogianaki E, Mooney J, Kinane DF: The ability of gingival crevicular fluid acute phase proteins to distinguish healthy, gingivitis and periodontitis sites. J Clin Periodontol 1992;19:98-102.
    • (1992) J Clin Periodontol , vol.19 , pp. 98-102
    • Adonogianaki, E.1    Mooney, J.2    Kinane, D.F.3
  • 95
    • 0033112626 scopus 로고    scopus 로고
    • Calcitonin gene-related peptide in gingival crevicular fluid in periodontal health and disease
    • Lundy FT, Shaw C, McKinnell J, Lamey PJ, Linden GJ: Calcitonin gene-related peptide in gingival crevicular fluid in periodontal health and disease. J Clin Periodontol 1999;26:212-216.
    • (1999) J Clin Periodontol , vol.26 , pp. 212-216
    • Lundy, F.T.1    Shaw, C.2    McKinnell, J.3    Lamey, P.J.4    Linden, G.J.5
  • 97
    • 0033218035 scopus 로고    scopus 로고
    • Cysteine protease inhibitory activity and levels of salivary cystatins in whole saliva of periodontally diseased patients
    • Baron AC, Gansky SA, Ryder MI, Featherstone DB: Cysteine protease inhibitory activity and levels of salivary cystatins in whole saliva of periodontally diseased patients. J Periodontal Res 1999;34:437-444.
    • (1999) J Periodontal Res , vol.34 , pp. 437-444
    • Baron, A.C.1    Gansky, S.A.2    Ryder, M.I.3    Featherstone, D.B.4
  • 98
    • 0024698422 scopus 로고
    • Concentrations of fibronectin in the sera and crevicular fluid in various stages of periodontal disease
    • Lopatin DE, Caffesse ER, Bye FL, Caffesse RG: Concentrations of fibronectin in the sera and crevicular fluid in various stages of periodontal disease. J Clin Periodontol 1989;16:359-364.
    • (1989) J Clin Periodontol , vol.16 , pp. 359-364
    • Lopatin, D.E.1    Caffesse, E.R.2    Bye, F.L.3    Caffesse, R.G.4
  • 99
    • 0034901202 scopus 로고    scopus 로고
    • Effect of Actinobacillus actinomycetemcomitans protease on the proliferation of gingival epithelial cells
    • DOI 10.1034/j.1601-0825.2001.0070406.x
    • Wang PL, Azuma Y, Shinohara M, Ohura K: Effect of actinobacillus actinomycetemcomitans protease on the proliferation of gingival epithelial cells. Oral Dis 2001;7:233-237. (Pubitemid 32734922)
    • (2001) Oral Diseases , vol.7 , Issue.4 , pp. 233-237
    • Wang, P.L.1    Azuma, Y.2    Shinohara, M.3    Ohura, K.4
  • 101
    • 58849115831 scopus 로고    scopus 로고
    • Neuropeptide y (NPY) and NPY Y1 receptor in periodontal health and disease
    • Lundy FT, El Karim IA, Linden GJ: Neuropeptide Y (NPY) and NPY Y1 receptor in periodontal health and disease. Arch Oral Biol 2009;54:258-262.
    • (2009) Arch Oral Biol , vol.54 , pp. 258-262
    • Lundy, F.T.1    El Karim, I.A.2    Linden, G.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.