메뉴 건너뛰기




Volumn 164, Issue 6, 2004, Pages 2203-2216

Pivotal role of cathepsin K in lung fibrosis

Author keywords

[No Author keywords available]

Indexed keywords

BLEOMYCIN; CATHEPSIN K; COLLAGEN;

EID: 2442694270     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)63777-7     Document Type: Article
Times cited : (171)

References (54)
  • 1
    • 0031965748 scopus 로고    scopus 로고
    • Idiopathic pulmonary fibrosis: Clinical relevance of pathologic classification
    • Katzenstein AL, Myers JL: Idiopathic pulmonary fibrosis: clinical relevance of pathologic classification. Am J Respir Crit Care Med 1998, 157:1301-1315
    • (1998) Am J Respir Crit Care Med , vol.157 , pp. 1301-1315
    • Katzenstein, A.L.1    Myers, J.L.2
  • 5
    • 0031225747 scopus 로고    scopus 로고
    • Incidence and recognition of interstitial pulmonary fibrosis in developing countries
    • Jindal SK, Gupta D: Incidence and recognition of interstitial pulmonary fibrosis in developing countries. Curr Opin Pulm Med 1997, 3:378-383
    • (1997) Curr Opin Pulm Med , vol.3 , pp. 378-383
    • Jindal, S.K.1    Gupta, D.2
  • 6
    • 0036250298 scopus 로고    scopus 로고
    • Pathology and pathophysiology of chronic obstructive pulmonary disease
    • Nagai A: Pathology and pathophysiology of chronic obstructive pulmonary disease. Intern Med 2002, 41:265-269
    • (2002) Intern Med , vol.41 , pp. 265-269
    • Nagai, A.1
  • 9
    • 2442703702 scopus 로고    scopus 로고
    • Edited by RG Crystal, JB West, ER Weibel, PJ Barnes. Philadelphia, Lippencott-Raven
    • Chambers RC, Laurent JL: Collagens. The Lung. Edited by RG Crystal, JB West, ER Weibel, PJ Barnes. Philadelphia, Lippencott-Raven, 2003, pp 709-727
    • (2003) Collagens. The Lung , pp. 709-727
    • Chambers, R.C.1    Laurent, J.L.2
  • 10
    • 0029837675 scopus 로고    scopus 로고
    • Cytokines and pulmonary fibrosis
    • Zhang K, Phan SH: Cytokines and pulmonary fibrosis. Biol Signals 1996, 5:232-239
    • (1996) Biol Signals , vol.5 , pp. 232-239
    • Zhang, K.1    Phan, S.H.2
  • 12
    • 0036211999 scopus 로고    scopus 로고
    • Involvement of gelatinases (MMP-2 and MMP-9) in the development of airway inflammation and pulmonary fibrosis
    • Corbel M, Belleguic C, Boichot E, Lagante V: Involvement of gelatinases (MMP-2 and MMP-9) in the development of airway inflammation and pulmonary fibrosis. Cell Biol Toxicol 2002, 18:51-61
    • (2002) Cell Biol Toxicol , vol.18 , pp. 51-61
    • Corbel, M.1    Belleguic, C.2    Boichot, E.3    Lagante, V.4
  • 13
    • 0029840755 scopus 로고    scopus 로고
    • Immunohistochemical study of metalloproteinases and their tissue inhibitors in the lungs of patients with diffuse alveolar damage and idiopathic pulmonary fibrosis
    • Hayashi T, Stetler-Stevenson WG, Fleming MV, Fishback N, Koss MN, Liotta LA, Ferrans VJ, Travis WD: Immunohistochemical study of metalloproteinases and their tissue inhibitors in the lungs of patients with diffuse alveolar damage and idiopathic pulmonary fibrosis. Am J Pathol 1996, 149:1241-1256
    • (1996) Am J Pathol , vol.149 , pp. 1241-1256
    • Hayashi, T.1    Stetler-Stevenson, W.G.2    Fleming, M.V.3    Fishback, N.4    Koss, M.N.5    Liotta, L.A.6    Ferrans, V.J.7    Travis, W.D.8
  • 14
    • 0031780581 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinases-1, -2, and -9 and tissue inhibitor of metal loproteinase-2 in interstitial lung diseases
    • Fukuda Y, Ishizaki M, Kudoh S, Kitaichi M, Yamanaka N: Localization of matrix metalloproteinases-1, -2, and -9 and tissue inhibitor of metal loproteinase-2 in interstitial lung diseases. Lab Invest 1998, 78:687-698
    • (1998) Lab Invest , vol.78 , pp. 687-698
    • Fukuda, Y.1    Ishizaki, M.2    Kudoh, S.3    Kitaichi, M.4    Yamanaka, N.5
  • 15
    • 0033830350 scopus 로고    scopus 로고
    • TIMP-1, -2, -3, and -4 in idiopathic pulmonary fibrosis. A prevailing nondegradative lung microenvironment?
    • Selman M, Ruiz V, Cabrera S, Segura L, Ramirez R, Barrios R, Pardo A: TIMP-1, -2, -3, and -4 in idiopathic pulmonary fibrosis. A prevailing nondegradative lung microenvironment? Am J Physiol 2000, 279: L562-L574
    • (2000) Am J Physiol , vol.279
    • Selman, M.1    Ruiz, V.2    Cabrera, S.3    Segura, L.4    Ramirez, R.5    Barrios, R.6    Pardo, A.7
  • 16
    • 0035069059 scopus 로고    scopus 로고
    • Inhibition of bleomycin-induced pulmonary fibrosis in mice by the matrix metalloproteinase inhibitor batimastat
    • Corbel M, Caulet-Maugendre S, Germain N, Molet S, Lagente V, Boichot E: Inhibition of bleomycin-induced pulmonary fibrosis in mice by the matrix metalloproteinase inhibitor batimastat. J Pathol 2001, 193:538-545
    • (2001) J Pathol , vol.193 , pp. 538-545
    • Corbel, M.1    Caulet-Maugendre, S.2    Germain, N.3    Molet, S.4    Lagente, V.5    Boichot, E.6
  • 18
    • 0035984567 scopus 로고    scopus 로고
    • Differences in the fibrogenic response after transfer of active transforming growth factor-beta1 gene to lungs of "fibrosis-prone" and "fibrosis-resistant" mouse strains
    • Kolb M, Bonniaud P, Galt T, Sime PJ, Kelly MM, Margetts PJ, Gauldie J: Differences in the fibrogenic response after transfer of active transforming growth factor-beta1 gene to lungs of "fibrosis-prone" and "fibrosis-resistant" mouse strains. Am J Respir Cell Mol Biol 2002, 27:141-150
    • (2002) Am J Respir Cell Mol Biol , vol.27 , pp. 141-150
    • Kolb, M.1    Bonniaud, P.2    Galt, T.3    Sime, P.J.4    Kelly, M.M.5    Margetts, P.J.6    Gauldie, J.7
  • 19
    • 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
  • 20
    • 0029064989 scopus 로고
    • Control of collagen deposition in mammalian lung
    • Bienkowski RS, Gotkin MG: Control of collagen deposition in mammalian lung. Proc Soc Exp Biol Med 1995, 209:118-140
    • (1995) Proc Soc Exp Biol Med , vol.209 , pp. 118-140
    • Bienkowski, R.S.1    Gotkin, M.G.2
  • 21
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman HA, Riese RJ, Shi GP: Emerging roles for cysteine proteases in human biology. Annu Rev Physiol 1997, 59:63-88
    • (1997) Annu Rev Physiol , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 23
    • 0029809357 scopus 로고    scopus 로고
    • Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
    • Gelb BD, Shi GP, Chapman HA, Desnick RJ: Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science 1996, 273:1236-1238
    • (1996) Science , vol.273 , pp. 1236-1238
    • Gelb, B.D.1    Shi, G.P.2    Chapman, H.A.3    Desnick, R.J.4
  • 25
    • 0033802292 scopus 로고    scopus 로고
    • Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages
    • Punturieri A, Filippov S, Allen E, Caras I, Murray R, Reddy V, Weiss SJ: Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages. J Exp Med 2000, 192:789-800
    • (2000) J Exp Med , vol.192 , pp. 789-800
    • Punturieri, A.1    Filippov, S.2    Allen, E.3    Caras, I.4    Murray, R.5    Reddy, V.6    Weiss, S.J.7
  • 26
    • 0032145836 scopus 로고    scopus 로고
    • Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells
    • Sukhova GK, Shi GP, Simon DI, Chapman HA, Libby P: Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. J Clin Invest 1998, 102:576-583
    • (1998) J Clin Invest , vol.102 , pp. 576-583
    • Sukhova, G.K.1    Shi, G.P.2    Simon, D.I.3    Chapman, H.A.4    Libby, P.5
  • 30
    • 0034252159 scopus 로고    scopus 로고
    • Expression of the proteinase specialized in bone resorption, cathepsin K, in granulomatous inflammation
    • Diaz A, Willis AC, Sim RB: Expression of the proteinase specialized in bone resorption, cathepsin K, in granulomatous inflammation. Mol Med 2000, 6:648-659
    • (2000) Mol Med , vol.6 , pp. 648-659
    • Diaz, A.1    Willis, A.C.2    Sim, R.B.3
  • 32
    • 0033872052 scopus 로고    scopus 로고
    • The development of bleomycin-induced pulmonary fibrosis in mice deficient for components of the fibrinolytic system
    • Swaisgood CM, French EL, Noga C, Simon RH, Ploplis VA: The development of bleomycin-induced pulmonary fibrosis in mice deficient for components of the fibrinolytic system. Am J Pathol 2000, 157:177-187
    • (2000) Am J Pathol , vol.157 , pp. 177-187
    • Swaisgood, C.M.1    French, E.L.2    Noga, C.3    Simon, R.H.4    Ploplis, V.A.5
  • 35
    • 0030897953 scopus 로고    scopus 로고
    • Monoclonal antibodies against cathepsin L and procathepsin L of different species
    • Weber E, Bahn H, Günther D: Monoclonal antibodies against cathepsin L and procathepsin L of different species. Hybridoma 1997, 16:159-166
    • (1997) Hybridoma , vol.16 , pp. 159-166
    • Weber, E.1    Bahn, H.2    Günther, D.3
  • 36
    • 0030026637 scopus 로고    scopus 로고
    • Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme
    • Bromme D, Okamoto K, Wang BB, Biroc S: Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme. J Biol Chem 1996, 271:2126-2132
    • (1996) J Biol Chem , vol.271 , pp. 2126-2132
    • Bromme, D.1    Okamoto, K.2    Wang, B.B.3    Biroc, S.4
  • 39
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • Barrett AJ, Kirschke H: Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol 1981, 80:535-561
    • (1981) Methods Enzymol , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 41
    • 0001931264 scopus 로고    scopus 로고
    • Studying lung ultrastructure
    • Edited by S Uhling, AE Tayllor. Basel, Birkhäuser
    • Fehrenbach H, Ochs M: Studying lung ultrastructure. Methods in Pulmonary Research. Edited by S Uhling, AE Tayllor. Basel, Birkhäuser, 1998, pp 429-454
    • (1998) Methods in Pulmonary Research , pp. 429-454
    • Fehrenbach, H.1    Ochs, M.2
  • 42
    • 0015228599 scopus 로고
    • Use of a mixture of proteinase-free collagenases for the specific assay of radioactive collagen in the presence of other proteins
    • Peterkofsky B, Diegelmann R: Use of a mixture of proteinase-free collagenases for the specific assay of radioactive collagen in the presence of other proteins. Biochemistry 1971, 10:988-994
    • (1971) Biochemistry , vol.10 , pp. 988-994
    • Peterkofsky, B.1    Diegelmann, R.2
  • 43
    • 0024236123 scopus 로고
    • Collagen production by fibroblasts
    • Agelli M, Wahl SM: Collagen production by fibroblasts. Methods Enzymol 1988, 52:642-656
    • (1988) Methods Enzymol , vol.52 , pp. 642-656
    • Agelli, M.1    Wahl, S.M.2
  • 44
    • 0031750927 scopus 로고    scopus 로고
    • Cysteine proteinase cathepsin K mRNA is expressed in synovium of patients with rheumatoid arthritis and is detected at sites of synovial bone destruction
    • Hummel KM, Petrow PK, Franz JK, Müller-Ladner U, Aicher WK, Gay RE, Brömme D, Gay S: Cysteine proteinase cathepsin K mRNA is expressed in synovium of patients with rheumatoid arthritis and is detected at sites of synovial bone destruction. J Rheumatol 1998, 25:1887-1894
    • (1998) J Rheumatol , vol.25 , pp. 1887-1894
    • Hummel, K.M.1    Petrow, P.K.2    Franz, J.K.3    Müller-Ladner, U.4    Aicher, W.K.5    Gay, R.E.6    Brömme, D.7    Gay, S.8
  • 48
    • 0035126575 scopus 로고    scopus 로고
    • Treatment of idiopathic pulmonary fibrosis: The rise and fall of corticosteroids
    • Collard HR, King Jr TE: Treatment of idiopathic pulmonary fibrosis: the rise and fall of corticosteroids. Am J Med 2001, 110:326-328
    • (2001) Am J Med , vol.110 , pp. 326-328
    • Collard, H.R.1    King Jr., T.E.2
  • 50
    • 0019050844 scopus 로고
    • Regulation of the production of secretory proteins: Intracellular degradation of newly synthesized "defective" collagen
    • Berg RA, Schwartz ML, Crystal RG: Regulation of the production of secretory proteins: intracellular degradation of newly synthesized "defective" collagen. Proc Natl Acad Sci USA 1980, 77:4746-4750
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 4746-4750
    • Berg, R.A.1    Schwartz, M.L.2    Crystal, R.G.3
  • 51
    • 0029763527 scopus 로고    scopus 로고
    • Role of integrins in regulation of collagen phagocytosis by human fibroblasts
    • Lee W, Sodek J, McCulloch CA: Role of integrins in regulation of collagen phagocytosis by human fibroblasts. J Cell Physiol 1996, 168:695-704
    • (1996) J Cell Physiol , vol.168 , pp. 695-704
    • Lee, W.1    Sodek, J.2    McCulloch, C.A.3
  • 53
    • 0034041529 scopus 로고    scopus 로고
    • Cathepsin K and the design of inhibitors of cathepsin K
    • Yamashita DS, Dodds RA: Cathepsin K and the design of inhibitors of cathepsin K. Curr Pharm Des 2000, 6:1-24
    • (2000) Curr Pharm Des , vol.6 , pp. 1-24
    • Yamashita, D.S.1    Dodds, R.A.2
  • 54
    • 0037047275 scopus 로고    scopus 로고
    • Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate
    • Li Z, Hou WS, Escalante-Torres CR, Gelb BD, Bromme D: Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate. J Biol Chem 2002, 277:28669-28676
    • (2002) J Biol Chem , vol.277 , pp. 28669-28676
    • Li, Z.1    Hou, W.S.2    Escalante-Torres, C.R.3    Gelb, B.D.4    Bromme, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.