메뉴 건너뛰기




Volumn 14, Issue 1, 1997, Pages 144-157

Mechanisms of connective tissue matrix destruction in periodontitis

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; CYTOKINE; METALLOPROTEINASE; PROTEINASE INHIBITOR; SCLEROPROTEIN;

EID: 0031152007     PISSN: 09066713     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-0757.1997.tb00195.x     Document Type: Article
Times cited : (142)

References (99)
  • 1
    • 0028309211 scopus 로고
    • The role of cytokines in the pathogenesis of periodontal disease
    • Alexander MB, Damoulis PD. The role of cytokines in the pathogenesis of periodontal disease. Curr Opin Periodontol 1994: 39-53.
    • (1994) Curr Opin Periodontol , pp. 39-53
    • Alexander, M.B.1    Damoulis, P.D.2
  • 2
    • 0029671458 scopus 로고    scopus 로고
    • 2 stimulates osteoclast formation via endogenous IL-1β expressed through protein kinase A
    • 2 stimulates osteoclast formation via endogenous IL-1β expressed through protein kinase A. J Immunol 1996: 156: 1931-1936.
    • (1996) J Immunol , vol.156 , pp. 1931-1936
    • Amano, S.1    Naganuma, K.2    Kawata, Y.3
  • 4
    • 0029019867 scopus 로고
    • The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family
    • Apte SS, Olsen BR, Murphy G. The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family. J Biol Chem 1995: 270: 14313-14318.
    • (1995) J Biol Chem , vol.270 , pp. 14313-14318
    • Apte, S.S.1    Olsen, B.R.2    Murphy, G.3
  • 5
    • 0029843761 scopus 로고    scopus 로고
    • Isothiazolones interfere with normal matrix metalloproteinase activation and inhibit cartilage proteoglycan degradation
    • Arner EC, Pratta MA, Freimark B, Lischwe M, Trzaskos JM, Magolda RL, Wright SW. Isothiazolones interfere with normal matrix metalloproteinase activation and inhibit cartilage proteoglycan degradation. Biochem J 1996: 318: 417-424.
    • (1996) Biochem J , vol.318 , pp. 417-424
    • Arner, E.C.1    Pratta, M.A.2    Freimark, B.3    Lischwe, M.4    Trzaskos, J.M.5    Magolda, R.L.6    Wright, S.W.7
  • 7
    • 0030271595 scopus 로고    scopus 로고
    • Focalized proteolysis: Spatial and temporal regulation of extracellular matrix degradation at the cell surface
    • Basbaum CB, Werb Z. Focalized proteolysis: spatial and temporal regulation of extracellular matrix degradation at the cell surface. Curr Opin Cell Biol 1996: 8: 731-738.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 731-738
    • Basbaum, C.B.1    Werb, Z.2
  • 9
    • 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
  • 10
    • 0029150795 scopus 로고
    • Proteolytic remodeling of extracellular matrix
    • Birkedal-Hansen H. Proteolytic remodeling of extracellular matrix. Curr Opin Cell Biol 1995: 7: 728-735.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 728-735
    • Birkedal-Hansen, H.1
  • 12
    • 0028354573 scopus 로고
    • Regional and temporal changes in the synthesis of matrix metalloproteinases and TIMP-1 during development of the rabbit mandibular condyle
    • Breckon JJW, Hembry RM, Reynolds JJ, Meikle MC. Regional and temporal changes in the synthesis of matrix metalloproteinases and TIMP-1 during development of the rabbit mandibular condyle. J Anat 1994: 184: 99-110.
    • (1994) J Anat , vol.184 , pp. 99-110
    • Breckon, J.J.W.1    Hembry, R.M.2    Reynolds, J.J.3    Meikle, M.C.4
  • 14
    • 0024397516 scopus 로고
    • Immunolocalization of metalloproteinases and their inhibitor in the rabbit growth plate
    • Brown CC, Hembry RM, Reynolds JJ. Immunolocalization of metalloproteinases and their inhibitor in the rabbit growth plate. J Bone Joint Surg (Am) 1989: 71A: 580-593.
    • (1989) J Bone Joint Surg (Am) , vol.71 A , pp. 580-593
    • Brown, C.C.1    Hembry, R.M.2    Reynolds, J.J.3
  • 15
    • 0029026517 scopus 로고    scopus 로고
    • Matrilysin expression by human mononuclear phagocytes and its regulation by cytokines and hormones
    • Busiek DF, Baragi V, Nehring LC, Parks WC, Welgus HG. Matrilysin expression by human mononuclear phagocytes and its regulation by cytokines and hormones. J Immunol 1996: 154: 6484-6491.
    • (1996) J Immunol , vol.154 , pp. 6484-6491
    • Busiek, D.F.1    Baragi, V.2    Nehring, L.C.3    Parks, W.C.4    Welgus, H.G.5
  • 16
    • 0028924956 scopus 로고
    • The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation
    • Cao J, Sato H, Takino T, Seiki M. The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation. J Biol Chem 1995: 270: 801-805.
    • (1995) J Biol Chem , vol.270 , pp. 801-805
    • Cao, J.1    Sato, H.2    Takino, T.3    Seiki, M.4
  • 17
    • 0030033710 scopus 로고    scopus 로고
    • Chondrocyte matrix metalloproteinase-8: Up-regulation of neutrophil collagenase by interleukin-1β in human cartilage from knee and ankle joints
    • Chubinskaya S, Huch K, Mikecz K, CS-Szabo G, Hasty KA, Kuettner KE, Cole AA. Chondrocyte matrix metalloproteinase-8: up-regulation of neutrophil collagenase by interleukin-1β in human cartilage from knee and ankle joints. Lab Invest 1996: 74: 232-240.
    • (1996) Lab Invest , vol.74 , pp. 232-240
    • Chubinskaya, S.1    Huch, K.2    Mikecz, K.3    Cs-Szabo, G.4    Hasty, K.A.5    Kuettner, K.E.6    Cole, A.A.7
  • 19
    • 0030138722 scopus 로고    scopus 로고
    • The "cyclic" regimen of low-dose doxycycline for adult periodontitis: A preliminary study
    • Crout RJ, Lee HM, Schroeder K. The "cyclic" regimen of low-dose doxycycline for adult periodontitis: a preliminary study. J Periodontol 1996: 67: 506-514.
    • (1996) J Periodontol , vol.67 , pp. 506-514
    • Crout, R.J.1    Lee, H.M.2    Schroeder, K.3
  • 20
    • 0024712236 scopus 로고
    • Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage
    • Dean DD, Martel-Pelletier J, Pelletier J-P, Howell DS, Woessner JF. Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage. J Clin Invest 1989: 84: 678-685.
    • (1989) J Clin Invest , vol.84 , pp. 678-685
    • Dean, D.D.1    Martel-Pelletier, J.2    Pelletier, J.-P.3    Howell, D.S.4    Woessner, J.F.5
  • 21
    • 0028598887 scopus 로고
    • Protease inhibitors: Role and potential therapeutic use in human cancer
    • DeClerck YA, Imren S. Protease inhibitors: role and potential therapeutic use in human cancer. Eur J Cancer 1994: 30A: 2170-2180.
    • (1994) Eur J Cancer , vol.30 A , pp. 2170-2180
    • DeClerck, Y.A.1    Imren, S.2
  • 22
    • 0002801861 scopus 로고
    • Mechanism of mineral solubilization and matrix degradation in osteoclastic bone resorption
    • Rifkin BR, Gay CV, ed. Boca Raton, FL: CRC Press
    • Delaisse J-M, Vaes G. Mechanism of mineral solubilization and matrix degradation in osteoclastic bone resorption. In: Rifkin BR, Gay CV, ed. Biology and physiology of the osteoclast. Boca Raton, FL: CRC Press, 1992: 289-314.
    • (1992) Biology and Physiology of the Osteoclast , pp. 289-314
    • Delaisse, J.-M.1    Vaes, G.2
  • 23
    • 0027731213 scopus 로고
    • (Pro) collagenase (matrix metalloproteinase-1) is present in rodent osteoclasts and in the underlying bone-resorbing compartment
    • Delaisse JM, Eeckhout Y, Neff L, François-Gillet C, Henriet P, Su Y, Vaes G, Baron R. (Pro) collagenase (matrix metalloproteinase-1) is present in rodent osteoclasts and in the underlying bone-resorbing compartment. J Cell Sci 1993: 106: 1071-1082.
    • (1993) J Cell Sci , vol.106 , pp. 1071-1082
    • Delaisse, J.M.1    Eeckhout, Y.2    Neff, L.3    François-Gillet, C.4    Henriet, P.5    Su, Y.6    Vaes, G.7    Baron, R.8
  • 25
    • 0026721062 scopus 로고
    • The matrix metalloproteinases and their natural inhibitors: Prospects for treating degenerative tissue diseases
    • Docherty AJP, O'Connell J, Crabbe T, Angal S, Murphy G. The matrix metalloproteinases and their natural inhibitors: prospects for treating degenerative tissue diseases. Trends Biotechnol 1992: 10: 200-207.
    • (1992) Trends Biotechnol , vol.10 , pp. 200-207
    • Docherty, A.J.P.1    O'Connell, J.2    Crabbe, T.3    Angal, S.4    Murphy, G.5
  • 27
    • 0026544215 scopus 로고
    • Degradation of collagen in the bone-resorbing compartment underlying the osteoclast involves both cysteine-proteinases and matrix metalloproteinases
    • Everts V, Delaisse J-M, Korper W, Niehof A, Vaes G, Beertsen W. Degradation of collagen in the bone-resorbing compartment underlying the osteoclast involves both cysteine-proteinases and matrix metalloproteinases. J Cell Physiol 1992: 150: 221-231.
    • (1992) J Cell Physiol , vol.150 , pp. 221-231
    • Everts, V.1    Delaisse, J.-M.2    Korper, W.3    Niehof, A.4    Vaes, G.5    Beertsen, W.6
  • 28
    • 8944249294 scopus 로고    scopus 로고
    • Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling
    • Everts V, Van der Zee E, Creemers L, Beertsen W. Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling. Histochem J 1996: 28: 229-245.
    • (1996) Histochem J , vol.28 , pp. 229-245
    • Everts, V.1    Van Der Zee, E.2    Creemers, L.3    Beertsen, W.4
  • 30
    • 0028322352 scopus 로고
    • Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas
    • Freije JMP, Diez-Itza I, Balbin M, Sanchez LM, Blasco R, Tolivia J, Lopez-Otin C. Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas. J Biol Chem 1994: 269: 16766-16773.
    • (1994) J Biol Chem , vol.269 , pp. 16766-16773
    • Freije, J.M.P.1    Diez-Itza, I.2    Balbin, M.3    Sanchez, L.M.4    Blasco, R.5    Tolivia, J.6    Lopez-Otin, C.7
  • 31
    • 0028509288 scopus 로고
    • Collagenase activity and tissue inhibitor of metalloproteinases-1 (TIMP-1) content in human whole saliva from clinically healthy and periodontally diseased subjects
    • Hayakawa H, Yamashita K, Ohwaki K, Sawa M, Noguchi T, Iwata K, Hayakawa T. Collagenase activity and tissue inhibitor of metalloproteinases-1 (TIMP-1) content in human whole saliva from clinically healthy and periodontally diseased subjects. J Periodont Res 1994: 29: 305-308.
    • (1994) J Periodont Res , vol.29 , pp. 305-308
    • Hayakawa, H.1    Yamashita, K.2    Ohwaki, K.3    Sawa, M.4    Noguchi, T.5    Iwata, K.6    Hayakawa, T.7
  • 33
    • 0028854885 scopus 로고
    • Immunolocalisation studies on six matrix metalloproteinases and their inhibitors, TIMP-1 and TIMP-2, in synovia from patients with osteo- and rheumatoid arthritis
    • Hembry RM, Bagga MR, Reynolds JJ, Hamblen DL. Immunolocalisation studies on six matrix metalloproteinases and their inhibitors, TIMP-1 and TIMP-2, in synovia from patients with osteo- and rheumatoid arthritis. Ann Rheum Dis 1995: 54: 25-32.
    • (1995) Ann Rheum Dis , vol.54 , pp. 25-32
    • Hembry, R.M.1    Bagga, M.R.2    Reynolds, J.J.3    Hamblen, D.L.4
  • 34
    • 0026722877 scopus 로고
    • Cloning and sequencing of mouse collagenase cDNA. Divergence of mouse and rat collagenases from the other mammalian collagenases
    • Henriet P, Rousseau GG, Eeckhout Y. Cloning and sequencing of mouse collagenase cDNA. Divergence of mouse and rat collagenases from the other mammalian collagenases. FEBS Lett 1992: 310: 175-178.
    • (1992) FEBS Lett , vol.310 , pp. 175-178
    • Henriet, P.1    Rousseau, G.G.2    Eeckhout, Y.3
  • 36
    • 0027960243 scopus 로고
    • The effects of selective inhibitors of matrix metalloproteinases (MMPs) on bone resorption and the identification of MMPs and TIMP-1 in isolated osteoclasts
    • Hill PA, Murphy G, Docherty AJP, Hembry RM, Millican TA, Reynolds JJ, Meikle MC. The effects of selective inhibitors of matrix metalloproteinases (MMPs) on bone resorption and the identification of MMPs and TIMP-1 in isolated osteoclasts. J Cell Sci 1994: 107: 3055-3064.
    • (1994) J Cell Sci , vol.107 , pp. 3055-3064
    • Hill, P.A.1    Murphy, G.2    Docherty, A.J.P.3    Hembry, R.M.4    Millican, T.A.5    Reynolds, J.J.6    Meikle, M.C.7
  • 38
    • 0028987190 scopus 로고
    • Cooperative signaling by α5β1 and α4β1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin
    • Huhtala P, Humphries MJ, McCarthy JB, Tremble PM, Werb Z, Damsky CH. Cooperative signaling by α5β1 and α4β1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin. J Cell Biol 1995: 129: 867-879.
    • (1995) J Cell Biol , vol.129 , pp. 867-879
    • Huhtala, P.1    Humphries, M.J.2    McCarthy, J.B.3    Tremble, P.M.4    Werb, Z.5    Damsky, C.H.6
  • 39
    • 0030245742 scopus 로고    scopus 로고
    • Fibronectin and fibronectin fragments modulate the expression of proteinases and proteinase inhibitors in human periodontal ligament cells
    • Kapila YL, Kapila S, Johnson PW. Fibronectin and fibronectin fragments modulate the expression of proteinases and proteinase inhibitors in human periodontal ligament cells. Matrix Biol 1996: 15: 251-261.
    • (1996) Matrix Biol , vol.15 , pp. 251-261
    • Kapila, Y.L.1    Kapila, S.2    Johnson, P.W.3
  • 40
    • 0030037395 scopus 로고    scopus 로고
    • Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase A (MMP-2) are able to generate active enzyme
    • Knauper V, Will H, Lopez-Otin C, Smith B, Atkinson SJ, Stanton H, Hembry RM, Murphy G. Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase A (MMP-2) are able to generate active enzyme. J Biol Chem 1996: 271: 17124-17131.
    • (1996) J Biol Chem , vol.271 , pp. 17124-17131
    • Knauper, V.1    Will, H.2    Lopez-Otin, C.3    Smith, B.4    Atkinson, S.J.5    Stanton, H.6    Hembry, R.M.7    Murphy, G.8
  • 41
    • 0030103118 scopus 로고    scopus 로고
    • Expression of mRNA for matrix metalloproteinases and tissue inhibitors of metalloproteinases in periodontitis-affected human gingival tissue
    • Kubota T, Nomura T, Takahashi T, Hara K. Expression of mRNA for matrix metalloproteinases and tissue inhibitors of metalloproteinases in periodontitis-affected human gingival tissue. Arch Oral Biol 1996: 41: 253-262.
    • (1996) Arch Oral Biol , vol.41 , pp. 253-262
    • Kubota, T.1    Nomura, T.2    Takahashi, T.3    Hara, K.4
  • 42
    • 0028855894 scopus 로고
    • IL-10 inhibits metalloproteinase and stimulates TIMP-1 production in human mononuclear phagocytes
    • Lacraz S, Nicod LP, Chicheportiche R, Welgus HG, Dayer J-M. IL-10 inhibits metalloproteinase and stimulates TIMP-1 production in human mononuclear phagocytes. J Clin Invest 1995: 96: 2304-2310.
    • (1995) J Clin Invest , vol.96 , pp. 2304-2310
    • Lacraz, S.1    Nicod, L.P.2    Chicheportiche, R.3    Welgus, H.G.4    Dayer, J.-M.5
  • 43
    • 0022969814 scopus 로고
    • Collagenase and collagenase inhibitor activities in crevicular fluid of patients receiving treatment for localized juvenile periodontitis
    • Larivee J, Sodek J, Ferrier JM. Collagenase and collagenase inhibitor activities in crevicular fluid of patients receiving treatment for localized juvenile periodontitis. J Periodont Res 1986: 21: 702-715.
    • (1986) J Periodont Res , vol.21 , pp. 702-715
    • Larivee, J.1    Sodek, J.2    Ferrier, J.M.3
  • 44
    • 0028244447 scopus 로고
    • Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues
    • Leco KJ, Khokha R, Pavloff N, Hawkes SP, Edwards DR. Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues. J Biol Chem 1994: 269: 9352-9360.
    • (1994) J Biol Chem , vol.269 , pp. 9352-9360
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3    Hawkes, S.P.4    Edwards, D.R.5
  • 45
    • 0029141399 scopus 로고
    • Evidence of a direct relationship between neutrophil collagenase activity and periodontal tissue destruction in vivo: Role of active enzyme in human periodontitis
    • Lee W, Aitken S, Sodek J, McCulloch CAG. Evidence of a direct relationship between neutrophil collagenase activity and periodontal tissue destruction in vivo: role of active enzyme in human periodontitis. J Periodont Res 1995: 30: 23-33.
    • (1995) J Periodont Res , vol.30 , pp. 23-33
    • Lee, W.1    Aitken, S.2    Sodek, J.3    McCulloch, C.A.G.4
  • 47
    • 0030055680 scopus 로고    scopus 로고
    • Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristat 13-acetate
    • Lohi J, Lehti K, Westermarck J, Kahari VM, Keski-Oja J. Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristat 13-acetate. Eur J Biochem 1996: 239: 239-247.
    • (1996) Eur J Biochem , vol.239 , pp. 239-247
    • Lohi, J.1    Lehti, K.2    Westermarck, J.3    Kahari, V.M.4    Keski-Oja, J.5
  • 48
    • 0028488241 scopus 로고
    • Matrix metalloproteinases (MMP-2 and MMP-9) of the oral cavity: Cellular origin and relationship to periodontal status
    • Makela M, Salo T, Uitto V-J, Larjava H. Matrix metalloproteinases (MMP-2 and MMP-9) of the oral cavity: cellular origin and relationship to periodontal status. J Dent Res 1994: 73: 1397-1406.
    • (1994) J Dent Res , vol.73 , pp. 1397-1406
    • Makela, M.1    Salo, T.2    Uitto, V.-J.3    Larjava, H.4
  • 49
    • 0028921766 scopus 로고
    • Cytokine regulation of gelatinase production by head and neck squamous cell carcinoma: The role of tumor necrosis factor-alpha
    • Mann EA, Hibbs MS, Spiro JD, Bowik C, Wang XZ, Clawson M, Chen LL. Cytokine regulation of gelatinase production by head and neck squamous cell carcinoma: the role of tumor necrosis factor-alpha. Ann Otol Rhinol Laryngol 1995: 104: 203-209.
    • (1995) Ann Otol Rhinol Laryngol , vol.104 , pp. 203-209
    • Mann, E.A.1    Hibbs, M.S.2    Spiro, J.D.3    Bowik, C.4    Wang, X.Z.5    Clawson, M.6    Chen, L.L.7
  • 50
    • 0028247201 scopus 로고
    • Excess of metalloproteases over tissue inhibitor of metalloprotease may contribute to cartilage degradation in osteoarthritis and rheumatoid arthritis
    • Martel-Pelletier J, McCollum R, Fujimoto N, Obata K-I, Cloutier J-M, Pelletier J-P. Excess of metalloproteases over tissue inhibitor of metalloprotease may contribute to cartilage degradation in osteoarthritis and rheumatoid arthritis. Lab Invest 1994: 70: 807-815.
    • (1994) Lab Invest , vol.70 , pp. 807-815
    • Martel-Pelletier, J.1    McCollum, R.2    Fujimoto, N.3    Obata, K.-I.4    Cloutier, J.-M.5    Pelletier, J.-P.6
  • 51
    • 0026896029 scopus 로고
    • The matrix-degrading metalloproteinases
    • Matrisian LM. The matrix-degrading metalloproteinases. BioEssays 1992: 14: 455-463.
    • (1992) BioEssays , vol.14 , pp. 455-463
    • Matrisian, L.M.1
  • 52
    • 0022712672 scopus 로고
    • Advances in understanding cell interactions in tissue resorption. Relevance to the pathogenesis of periodontal diseases and a new hypothesis
    • Meikle MC, Heath JK, Reynolds JJ. Advances in understanding cell interactions in tissue resorption. Relevance to the pathogenesis of periodontal diseases and a new hypothesis. J Oral Pathol 1986: 15: 239-250.
    • (1986) J Oral Pathol , vol.15 , pp. 239-250
    • Meikle, M.C.1    Heath, J.K.2    Reynolds, J.J.3
  • 53
    • 5244270080 scopus 로고
    • Interleukin-1 production by peripheral blood mononuclear cells from patients with severe periodontitis
    • Lehner T, Cimasoni G, ed. Geneva: Editions Medecine et Hygiene
    • Meikle MC, McAlpine CG, Heath JK, Newman HN, Reynolds JJ. Interleukin-1 production by peripheral blood mononuclear cells from patients with severe periodontitis. In: Lehner T, Cimasoni G, ed. The borderland between caries and periodontal disease. Geneva: Editions Medecine et Hygiene, 1986: 283-290.
    • (1986) The Borderland between Caries and Periodontal Disease , pp. 283-290
    • Meikle, M.C.1    McAlpine, C.G.2    Heath, J.K.3    Newman, H.N.4    Reynolds, J.J.5
  • 54
    • 0024661765 scopus 로고
    • Gingival fibroblasts degrade type I collagen films when stimulated with tumor necrosis factor and interleukin 1: Evidence that breakdown is mediated by metalloproteinases
    • Meikle MC, Atkinson SJ, Ward RV, Murphy G, Reynolds JJ. Gingival fibroblasts degrade type I collagen films when stimulated with tumor necrosis factor and interleukin 1: evidence that breakdown is mediated by metalloproteinases. J Periodont Res 1989: 24: 207-213.
    • (1989) J Periodont Res , vol.24 , pp. 207-213
    • Meikle, M.C.1    Atkinson, S.J.2    Ward, R.V.3    Murphy, G.4    Reynolds, J.J.5
  • 56
    • 0028391312 scopus 로고
    • Immunolocalization of matrix metalloproteinases and TIMP-1 (tissue inhibitor of metalloproteinases) in human gingival tissues from periodontitis patients
    • Meikle MC, Hembry RM, Holley J, Horton C, McFarlane CG, Reynolds JJ. Immunolocalization of matrix metalloproteinases and TIMP-1 (tissue inhibitor of metalloproteinases) in human gingival tissues from periodontitis patients. J Periodont Res 1994: 29: 118-126.
    • (1994) J Periodont Res , vol.29 , pp. 118-126
    • Meikle, M.C.1    Hembry, R.M.2    Holley, J.3    Horton, C.4    McFarlane, C.G.5    Reynolds, J.J.6
  • 57
    • 0021400277 scopus 로고
    • Thymocyte activating factor(s) in human gingival fluids
    • Mergenhagen SE. Thymocyte activating factor(s) in human gingival fluids. J Dent Res 1984: 63: 461-464.
    • (1984) J Dent Res , vol.63 , pp. 461-464
    • Mergenhagen, S.E.1
  • 58
    • 0002230624 scopus 로고
    • Extracellular matrix degradation
    • Royce PM, Steinmann B, ed. New York: Wiley-Liss
    • Murphy G, Reynolds JJ. Extracellular matrix degradation. In: Royce PM, Steinmann B, ed. Connective tissue and its heritable disorders. New York: Wiley-Liss, 1993: 287-316.
    • (1993) Connective Tissue and Its Heritable Disorders , pp. 287-316
    • Murphy, G.1    Reynolds, J.J.2
  • 59
    • 0025799478 scopus 로고
    • The origin of matrix metalloproteinases and their familial relationships
    • Murphy GJP, Murphy G, Reynolds JJ. The origin of matrix metalloproteinases and their familial relationships. FEBS Lett 1991: 289: 4-7.
    • (1991) FEBS Lett , vol.289 , pp. 4-7
    • Murphy, G.J.P.1    Murphy, G.2    Reynolds, J.J.3
  • 60
    • 0027057950 scopus 로고
    • The role of plasminogen activators in the regulation of connective tissue metalloproteinases
    • Murphy G, Atkinson S, Ward R, Gavrilovic J, Reynolds JJ. The role of plasminogen activators in the regulation of connective tissue metalloproteinases. Ann N Y Acad Sci 1992: 667: 1-12.
    • (1992) Ann N Y Acad Sci , vol.667 , pp. 1-12
    • Murphy, G.1    Atkinson, S.2    Ward, R.3    Gavrilovic, J.4    Reynolds, J.J.5
  • 61
    • 0005866388 scopus 로고
    • Studies on the structure and function of the matrix metalloproteinases and their inhibitors
    • Bond JS, Barrett AJ, ed. Colchester: Portland Press
    • Murphy G, Willenbrock F, Ward R, O'Shea M, Docherty A. Studies on the structure and function of the matrix metalloproteinases and their inhibitors. In: Bond JS, Barrett AJ, ed. Proteolysis and protein turnover. Colchester: Portland Press, 1994: 25-32.
    • (1994) Proteolysis and Protein Turnover , pp. 25-32
    • Murphy, G.1    Willenbrock, F.2    Ward, R.3    O'Shea, M.4    Docherty, A.5
  • 62
    • 0026660964 scopus 로고
    • Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9
    • Ogata Y, Enghild JJ, Nagase H. Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9. J Biol Chem 1992: 267: 3581-3584.
    • (1992) J Biol Chem , vol.267 , pp. 3581-3584
    • Ogata, Y.1    Enghild, J.J.2    Nagase, H.3
  • 63
    • 0028935326 scopus 로고
    • Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas
    • Okada A, Bellocq JP, Rouyer N, Chenard M-P, Rio M-C, Chambon P, Basset P. Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas. Proc Natl Acad Sci U S A 1995: 92: 2730-2734.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 2730-2734
    • Okada, A.1    Bellocq, J.P.2    Rouyer, N.3    Chenard, M.-P.4    Rio, M.-C.5    Chambon, P.6    Basset, P.7
  • 64
    • 0028957812 scopus 로고
    • Localization of matrix metalloproteinase 9 (92-kilodalton gelatinase/type IV collagenase=gelatinase B) in osteoclasts: Implications for bone resorption
    • Okada Y, Naka K, Kawamura K, Matsumoto T, Nakanishi I, Fujimoto N, Sato H, Seiki M. Localization of matrix metalloproteinase 9 (92-kilodalton gelatinase/type IV collagenase=gelatinase B) in osteoclasts: implications for bone resorption. Lab Invest 1995: 72: 311-322.
    • (1995) Lab Invest , vol.72 , pp. 311-322
    • Okada, Y.1    Naka, K.2    Kawamura, K.3    Matsumoto, T.4    Nakanishi, I.5    Fujimoto, N.6    Sato, H.7    Seiki, M.8
  • 65
    • 0030183421 scopus 로고    scopus 로고
    • Interleukin-la produced in human gingival fibroblasts induces several activities related to the progression of periodontitis by direct contact
    • Okamatsu Y, Kobayashi M, Nishihara T, Hasegawa K. Interleukin-la produced in human gingival fibroblasts induces several activities related to the progression of periodontitis by direct contact. J Periodont Res 1996: 31: 355-364.
    • (1996) J Periodont Res , vol.31 , pp. 355-364
    • Okamatsu, Y.1    Kobayashi, M.2    Nishihara, T.3    Hasegawa, K.4
  • 66
    • 0026453778 scopus 로고
    • Sitedirected mutations that alter the inhibitor activity of the tissue inhibitor of metalloproteinases-1: Importance of the N-terminal region between cysteine 3 and cysteine 13
    • O'Shea M, Willenbrock F, Williamson RA, Cockett MI, Freedman RB, Reynolds JJ, Docherty AJP, Murphy G. Sitedirected mutations that alter the inhibitor activity of the tissue inhibitor of metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13. Biochemistry 1992: 31: 10146-10152.
    • (1992) Biochemistry , vol.31 , pp. 10146-10152
    • O'Shea, M.1    Willenbrock, F.2    Williamson, R.A.3    Cockett, M.I.4    Freedman, R.B.5    Reynolds, J.J.6    Docherty, A.J.P.7    Murphy, G.8
  • 67
    • 0023301216 scopus 로고
    • Demonstration of tissue collagenase activity in vivo and its relationship to inflammation severity in human gingiva
    • Overall CM, Wiebkin OW, Thonard JC. Demonstration of tissue collagenase activity in vivo and its relationship to inflammation severity in human gingiva. J Periodont Res 1987: 22: 81-88.
    • (1987) J Periodont Res , vol.22 , pp. 81-88
    • Overall, C.M.1    Wiebkin, O.W.2    Thonard, J.C.3
  • 68
    • 0026794057 scopus 로고
    • A new inhibitor of metalloproteinases from chicken: ChIMP-3. A third member of the TIMP family
    • Pavloff N, Staskus PW, Kishnani NS, Hawkes SP. A new inhibitor of metalloproteinases from chicken: ChIMP-3. A third member of the TIMP family. J Biol Chem 1992: 267: 17321-17326.
    • (1992) J Biol Chem , vol.267 , pp. 17321-17326
    • Pavloff, N.1    Staskus, P.W.2    Kishnani, N.S.3    Hawkes, S.P.4
  • 69
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei D, Weiss SJ. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 1995: 375: 244-247.
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 70
    • 0029811452 scopus 로고    scopus 로고
    • Vascular co-localization of proteolytic enzymes and proteinase inhibitors in advanced periodontitis
    • Pinchback JS, Gibbins JR, Hunter N. Vascular co-localization of proteolytic enzymes and proteinase inhibitors in advanced periodontitis. J Pathol 1996: 179: 326-332.
    • (1996) J Pathol , vol.179 , pp. 326-332
    • Pinchback, J.S.1    Gibbins, J.R.2    Hunter, N.3
  • 71
    • 0029770472 scopus 로고    scopus 로고
    • The effect of subgingival antimicrobial therapy on the levels of stromelysin and tissue inhibitor of metalloproteinases in gingival crevicular fluid
    • Pourtaghi N, Radvar M, Mooney J, Kinane DF. The effect of subgingival antimicrobial therapy on the levels of stromelysin and tissue inhibitor of metalloproteinases in gingival crevicular fluid. J Periodontol 1996: 67: 866-870.
    • (1996) J Periodontol , vol.67 , pp. 866-870
    • Pourtaghi, N.1    Radvar, M.2    Mooney, J.3    Kinane, D.F.4
  • 72
    • 0030022539 scopus 로고    scopus 로고
    • Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma
    • Puente XS, Pendas AM, Llano E, Velasco G, Lopez-Otin C. Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma. Cancer Res 1996: 56: 944-949.
    • (1996) Cancer Res , vol.56 , pp. 944-949
    • Puente, X.S.1    Pendas, A.M.2    Llano, E.3    Velasco, G.4    Lopez-Otin, C.5
  • 73
    • 0029880393 scopus 로고    scopus 로고
    • The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes. A role in osteoarthritis
    • Reboul P, Pelletier J-P, Tardif G, Cloutier J-M, Martel-Pelletier J. The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes. A role in osteoarthritis. J Clin Invest 1996: 97: 2011-2019.
    • (1996) J Clin Invest , vol.97 , pp. 2011-2019
    • Reboul, P.1    Pelletier, J.-P.2    Tardif, G.3    Cloutier, J.-M.4    Martel-Pelletier, J.5
  • 74
    • 0028476829 scopus 로고
    • Connective tissue degradation in health and periodontal disease and the roles of matrix metalloproteinases and their natural inhibitors
    • Reynolds JJ, Hembry RM, Meikle MC. Connective tissue degradation in health and periodontal disease and the roles of matrix metalloproteinases and their natural inhibitors. Adv Dent Res 1994: 8: 312-319.
    • (1994) Adv Dent Res , vol.8 , pp. 312-319
    • Reynolds, J.J.1    Hembry, R.M.2    Meikle, M.C.3
  • 75
    • 0029310597 scopus 로고
    • Cytokine regulation of matrix metalloproteinase activity and its regulatory disfunction in disease
    • Ries C, Petrides PE. Cytokine regulation of matrix metalloproteinase activity and its regulatory disfunction in disease. Biol Chem Hoppe-Seyler 1995: 376: 345-355.
    • (1995) Biol Chem Hoppe-Seyler , vol.376 , pp. 345-355
    • Ries, C.1    Petrides, P.E.2
  • 76
    • 0029688549 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their inhibition in periodontal treatment
    • Ryan ME, Ramamurthy NS, Golub LM. Matrix metalloproteinases and their inhibition in periodontal treatment. Curr Opin Periodontol 1996: 3: 85-96.
    • (1996) Curr Opin Periodontol , vol.3 , pp. 85-96
    • Ryan, M.E.1    Ramamurthy, N.S.2    Golub, L.M.3
  • 77
  • 78
    • 0030577022 scopus 로고    scopus 로고
    • Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2
    • Sato H, Kinoshita T, Takino T, Nakayama K, Seiki M. Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2. FEBS Lett 1996: 393: 101-104.
    • (1996) FEBS Lett , vol.393 , pp. 101-104
    • Sato, H.1    Kinoshita, T.2    Takino, T.3    Nakayama, K.4    Seiki, M.5
  • 79
    • 0026762898 scopus 로고
    • Identification of TIMP-2 in human alveolar macrophages. Regulation of biosynthesis is opposite to that of metalloproteinases and TIMP-1
    • Shapiro SD, Kobayashi DK, Welgus HG. Identification of TIMP-2 in human alveolar macrophages. Regulation of biosynthesis is opposite to that of metalloproteinases and TIMP-1. J Biol Chem 1992: 267: 13890-13894.
    • (1992) J Biol Chem , vol.267 , pp. 13890-13894
    • Shapiro, S.D.1    Kobayashi, D.K.2    Welgus, H.G.3
  • 80
    • 0027515289 scopus 로고
    • Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages
    • Shapiro SD, Kobayashi DK, Ley TJ. Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. J Biol Chem 1993: 268: 23824-23829.
    • (1993) J Biol Chem , vol.268 , pp. 23824-23829
    • Shapiro, S.D.1    Kobayashi, D.K.2    Ley, T.J.3
  • 81
    • 0030022245 scopus 로고    scopus 로고
    • Activation of recombinant human neutrophil procollagenase in the presence of doxycycline results in fragmentation of the enzyme and loss of enzyme activity
    • Smith GN, Brandt KD, Hasty KA. Activation of recombinant human neutrophil procollagenase in the presence of doxycycline results in fragmentation of the enzyme and loss of enzyme activity. Arthritis Rheum 1996: 39: 235-244.
    • (1996) Arthritis Rheum , vol.39 , pp. 235-244
    • Smith, G.N.1    Brandt, K.D.2    Hasty, K.A.3
  • 82
    • 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, Haapasalo M, Konttinen YT, Lindy O, Saari H, Uitto V-J. 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    Haapasalo, M.4    Konttinen, Y.T.5    Lindy, O.6    Saari, H.7    Uitto, V.-J.8
  • 83
    • 0025033983 scopus 로고
    • Tissue inhibitor of metalloproteinases-2 (TIMP-2) mRNA expression in tumor cell lines and human tumor tissues
    • Stetler-Stevenson WG, Brown PD, Onisto M, Levy AT, Liotta LA. Tissue inhibitor of metalloproteinases-2 (TIMP-2) mRNA expression in tumor cell lines and human tumor tissues. J Biol Chem 1990: 265: 13933-13938.
    • (1990) J Biol Chem , vol.265 , pp. 13933-13938
    • Stetler-Stevenson, W.G.1    Brown, P.D.2    Onisto, M.3    Levy, A.T.4    Liotta, L.A.5
  • 84
    • 0028969678 scopus 로고
    • The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • Stocker W, Grams F, Baumann U, Reinemer P, Gomis-Ruth F-X, McKay DB, Bode W. The metzincins - topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci 1995: 4: 823-840.
    • (1995) Protein Sci , vol.4 , pp. 823-840
    • Stocker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Ruth, F.-X.5    McKay, D.B.6    Bode, W.7
  • 85
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J Biol Chem 1995: 270: 5331-5338.
    • (1995) J Biol Chem , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 87
    • 0029118269 scopus 로고
    • Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family
    • Takino T, Sato H, Shinagawa A, Seiki M. Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family. J Biol Chem 1995: 270: 23013-23020.
    • (1995) J Biol Chem , vol.270 , pp. 23013-23020
    • Takino, T.1    Sato, H.2    Shinagawa, A.3    Seiki, M.4
  • 90
    • 0030254795 scopus 로고    scopus 로고
    • Cytokine-induced endogenous procollagenase stored in the extracellular matrix of soft connective tissue results in a burst of collagen breakdown following its activation
    • Van der Zee E, Everts V, Beertsen W. Cytokine-induced endogenous procollagenase stored in the extracellular matrix of soft connective tissue results in a burst of collagen breakdown following its activation. J Periodont Res 1996: 31: 483-488.
    • (1996) J Periodont Res , vol.31 , pp. 483-488
    • Van Der Zee, E.1    Everts, V.2    Beertsen, W.3
  • 91
    • 0023403456 scopus 로고
    • Collagenolytic activity in crevicular fluid from patients with chronic adult periodontitis, localized juvenile periodontitis and gingivitis, and from healthy control subjects
    • Villela B, Cogen RB, Bartolucci AA, Birkedal-Hansen H. Collagenolytic activity in crevicular fluid from patients with chronic adult periodontitis, localized juvenile periodontitis and gingivitis, and from healthy control subjects. J Periodont Res 1987: 22: 381-389.
    • (1987) J Periodont Res , vol.22 , pp. 381-389
    • Villela, B.1    Cogen, R.B.2    Bartolucci, A.A.3    Birkedal-Hansen, H.4
  • 93
    • 0028077527 scopus 로고
    • Cell surface-mediated activation of progelatinase A: Demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts
    • Ward RV, Atkinson SJ, Reynolds JJ, Murphy G. Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts. Biochem J 1994: 304: 263-269.
    • (1994) Biochem J , vol.304 , pp. 263-269
    • Ward, R.V.1    Atkinson, S.J.2    Reynolds, J.J.3    Murphy, G.4
  • 95
    • 0029122697 scopus 로고
    • Competence for collagenase gene expression by tissue fibroblasts requires activation of an interleukin 1α autocrine loop
    • West-Mays JA, Strissel KJ, Sadow PM, Fini ME. Competence for collagenase gene expression by tissue fibroblasts requires activation of an interleukin 1α autocrine loop. Proc Natl Acad Sci U S A 1995: 92: 6768-6772.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 6768-6772
    • West-Mays, J.A.1    Strissel, K.J.2    Sadow, P.M.3    Fini, M.E.4
  • 96
    • 0029133344 scopus 로고
    • cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment
    • Will H, Hinzmann B. cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. Eur J Biochem 1995: 231: 602-608.
    • (1995) Eur J Biochem , vol.231 , pp. 602-608
    • Will, H.1    Hinzmann, B.2
  • 98
    • 0030207158 scopus 로고    scopus 로고
    • Cytokine-induced components of periodontopathogenic bacteria
    • Wilson M, Reddi K, Henderson B. Cytokine-induced components of periodontopathogenic bacteria. J Periodont Res 1996: 31: 393-407.
    • (1996) J Periodont Res , vol.31 , pp. 393-407
    • Wilson, M.1    Reddi, K.2    Henderson, B.3
  • 99
    • 0019515449 scopus 로고
    • Immunolocalization of collagenase in periodontal disease
    • Woolley DE, Davies RM. Immunolocalization of collagenase in periodontal disease. J Periodont Res 1981: 16: 292-297.
    • (1981) J Periodont Res , vol.16 , pp. 292-297
    • Woolley, D.E.1    Davies, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.