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Volumn 289, Issue 23, 2014, Pages 16239-16251

Regulation of TGF-β1-driven differentiation of human Lung fibroblasts: Emerging roles of cathepsin B and cystatin C

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOLOGICAL ORGANS; CELL CULTURE; ENZYME ACTIVITY; PHOSPHORYLATION; PROTEINS; RESPIRATORY SYSTEM;

EID: 84902213879     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.542407     Document Type: Article
Times cited : (62)

References (65)
  • 3
    • 84872304968 scopus 로고    scopus 로고
    • Current and novel drug therapies for idiopathic pulmonary fibrosis
    • Adamali, H. I., and Maher, T. M. (2012) Current and novel drug therapies for idiopathic pulmonary fibrosis. Drug Des. Devel. Ther. 6, 261-271
    • (2012) Drug Des. Devel. Ther. , vol.6 , pp. 261-271
    • Adamali, H.I.1    Maher, T.M.2
  • 4
    • 0028109801 scopus 로고
    • Transforming growth factor beta in tissue fibrosis
    • Border, W. A., and Noble, N. A. (1994) Transforming growth factor beta in tissue fibrosis. N. Engl. J. Med. 331, 1286-1292
    • (1994) N. Engl. J. Med. , vol.331 , pp. 1286-1292
    • Border, W.A.1    Noble, N.A.2
  • 5
    • 0035181092 scopus 로고    scopus 로고
    • Regulation of the effects of TGF-β1 by activation of latent TGF-β1 and differential expression of TGF-β receptors (TβR-I and TβR-II) in idiopathic pulmonary fibrosis
    • Khalil, N., Parekh, T., O'Connor, R., Antman, N., Kepron, W., Yehaulaeshet, T., Xu, Y., and Gold, L. (2001) Regulation of the effects of TGF-β1 by activation of latent TGF-β1 and differential expression of TGF-β receptors (TβR-I and TβR-II) in idiopathic pulmonary fibrosis. Thorax 56, 907-915
    • (2001) Thorax , vol.56 , pp. 907-915
    • Khalil, N.1    Parekh, T.2    O'Connor, R.3    Antman, N.4    Kepron, W.5    Yehaulaeshet, T.6    Xu, Y.7    Gold, L.8
  • 7
    • 0027212686 scopus 로고
    • Transforming growth factor-beta 1 induces alpha-smooth muscle actin expression in granulation tissue myofibroblasts and in quiescent and growing cultured fibroblasts
    • Desmouliere, A., Geinoz, A., Gabbiani, F., and Gabbiani, G. (1993) Transforming growth factor-beta 1 induces alpha-smooth muscle actin expression in granulation tissue myofibroblasts and in quiescent and growing cultured fibroblasts. J. Cell Biol. 122, 103-111
    • (1993) J. Cell Biol. , vol.122 , pp. 103-111
    • Desmouliere, A.1    Geinoz, A.2    Gabbiani, F.3    Gabbiani, G.4
  • 9
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papainlike cysteine proteases: Their role in physiology and pathology and recent developments in inhibitor design
    • Lecaille, F., Kaleta, J., and Bromme, D. (2002) Human and parasitic papainlike cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev. 102, 4459-4488
    • (2002) Chem. Rev. , vol.102 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Bromme, D.3
  • 10
    • 84881539601 scopus 로고    scopus 로고
    • Cathepsin K: A unique collagenolytic cysteine peptidase
    • Novinec, M., and Lenarcic, B. (2013) Cathepsin K: a unique collagenolytic cysteine peptidase. Biol. Chem. 394, 1163-1179
    • (2013) Biol. Chem. , vol.394 , pp. 1163-1179
    • Novinec, M.1    Lenarcic, B.2
  • 11
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings, N. D., Barrett, A. J., and Bateman, A. (2012) MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 40, D343-D350
    • (2012) Nucleic Acids Res. , vol.40
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 13
    • 38649111363 scopus 로고    scopus 로고
    • Cysteine cathepsins: Cellular roadmap to different functions
    • Brix, K., Dunkhorst, A., Mayer, K., and Jordans, S. (2008) Cysteine cathepsins: cellular roadmap to different functions. Biochimie (Paris) 90, 194-207
    • (2008) Biochimie (Paris) , vol.90 , pp. 194-207
    • Brix, K.1    Dunkhorst, A.2    Mayer, K.3    Jordans, S.4
  • 14
    • 77957855881 scopus 로고    scopus 로고
    • Specialized roles for cysteine cathepsins in health and disease
    • Reiser, J., Adair, B., and Reinheckel, T. (2010) Specialized roles for cysteine cathepsins in health and disease. J. Clin. Invest. 120, 3421-3431
    • (2010) J. Clin. Invest. , vol.120 , pp. 3421-3431
    • Reiser, J.1    Adair, B.2    Reinheckel, T.3
  • 15
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: Successes, failures and future prospects
    • Turk, B. (2006) Targeting proteases: successes, failures and future prospects. Nat. Rev. Drug Discov. 5, 785-799
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 785-799
    • Turk, B.1
  • 16
    • 33846164404 scopus 로고    scopus 로고
    • Emerging roles of cysteine cathepsins in disease and their potential as drug targets
    • Vasiljeva, O., Reinheckel, T., Peters, C., Turk, D., Turk, V., and Turk, B. (2007) Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr. Pharm. Des. 13, 387-403
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 387-403
    • Vasiljeva, O.1    Reinheckel, T.2    Peters, C.3    Turk, D.4    Turk, V.5    Turk, B.6
  • 18
    • 52049096824 scopus 로고    scopus 로고
    • Cystatins: Biochemical and structural properties, and medical relevance
    • Turk, V., Stoka, V., and Turk, D. (2008) Cystatins: biochemical and structural properties, and medical relevance. Front. Biosci. 13, 5406-5420
    • (2008) Front. Biosci. , vol.13 , pp. 5406-5420
    • Turk, V.1    Stoka, V.2    Turk, D.3
  • 20
    • 65449128051 scopus 로고    scopus 로고
    • Cathepsins B and D drive hepatic stellate cell proliferation and promote their fibrogenic potential
    • Moles, A., Tarrats, N., Fernandez-Checa, J. C., and Mari, M. (2009) Cathepsins B and D drive hepatic stellate cell proliferation and promote their fibrogenic potential. Hepatology 49, 1297-1307
    • (2009) Hepatology , vol.49 , pp. 1297-1307
    • Moles, A.1    Tarrats, N.2    Fernandez-Checa, J.C.3    Mari, M.4
  • 23
    • 77953398632 scopus 로고    scopus 로고
    • Antiproteases as therapeutics to target inflammation in cystic fibrosis
    • Quinn, D. J., Weldon, S., and Taggart, C. C. (2010) Antiproteases as therapeutics to target inflammation in cystic fibrosis. Open Respir. Med. J. 4, 20-31
    • (2010) Open Respir. Med. J. , vol.4 , pp. 20-31
    • Quinn, D.J.1    Weldon, S.2    Taggart, C.C.3
  • 25
    • 79957650183 scopus 로고    scopus 로고
    • The effect of cathepsin K deficiency on airway development and TGF-β1 degradation
    • Zhang, D., Leung, N., Weber, E., Saftig, P., and Bromme, D. (2011) The effect of cathepsin K deficiency on airway development and TGF-β1 degradation. Respir. Res. 12, 72
    • (2011) Respir. Res. , vol.12 , pp. 72
    • Zhang, D.1    Leung, N.2    Weber, E.3    Saftig, P.4    Bromme, D.5
  • 26
    • 82255182433 scopus 로고    scopus 로고
    • Antifibrotic effects of curcumin are associated with overexpression of cathepsins K and L in bleomycin treated mice and human fibroblasts
    • Zhang, D., Huang, C., Yang, C., Liu, R. J., Wang, J., Niu, J., and Bromme, D. (2011) Antifibrotic effects of curcumin are associated with overexpression of cathepsins K and L in bleomycin treated mice and human fibroblasts. Respir. Res. 12, 154
    • (2011) Respir. Res. , vol.12 , pp. 154
    • Zhang, D.1    Huang, C.2    Yang, C.3    Liu, R.J.4    Wang, J.5    Niu, J.6    Bromme, D.7
  • 27
    • 26244460586 scopus 로고    scopus 로고
    • Overexpression of cathepsin K during silica-induced lung fibrosis and control by TGF-beta
    • Van den Brule, S., Misson, P., Buhling, F., Lison, D., and Huaux, F. (2005) Overexpression of cathepsin K during silica-induced lung fibrosis and control by TGF-beta. Respir. Res. 6, 84
    • (2005) Respir. Res. , vol.6 , pp. 84
    • Van Den Brule, S.1    Misson, P.2    Buhling, F.3    Lison, D.4    Huaux, F.5
  • 28
    • 0035132101 scopus 로고    scopus 로고
    • Interleukin-6 and transforming growth factor-beta 1 control expression of cathepsins B and L in human lung epithelial cells
    • Gerber, A., Wille, A., Welte, T., Ansorge, S., and Buhling, F. (2001) Interleukin-6 and transforming growth factor-beta 1 control expression of cathepsins B and L in human lung epithelial cells. J. Interf. Cytokine Res. 21, 11-19.
    • (2001) J. Interf. Cytokine Res. , vol.21 , pp. 11-19
    • Gerber, A.1    Wille, A.2    Welte, T.3    Ansorge, S.4    Buhling, F.5
  • 29
    • 0029816035 scopus 로고    scopus 로고
    • Biotin-labelled peptidyl diazomethane inhibitors derived from the substrate-like sequence of cystatin: Targeting of the active site of cruzipain, the major cysteine proteinase of Trypanosoma cruzi
    • Lalmanach, G., Mayer, R., Serveau, C., Scharfstein, J., and Gauthier, F. (1996) Biotin-labelled peptidyl diazomethane inhibitors derived from the substrate-like sequence of cystatin: targeting of the active site of cruzipain, the major cysteine proteinase of Trypanosoma cruzi. Biochem. J. 318, 395-399
    • (1996) Biochem. J. , vol.318 , pp. 395-399
    • Lalmanach, G.1    Mayer, R.2    Serveau, C.3    Scharfstein, J.4    Gauthier, F.5
  • 30
    • 0026847819 scopus 로고
    • Human lung fibroblast subpopulations with different C1q binding and functional properties
    • Akamine, A., Raghu, G., and Narayanan, A. S. (1992) Human lung fibroblast subpopulations with different C1q binding and functional properties. Am. J. Respir. Cell Mol. Biol. 6, 382-389
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.6 , pp. 382-389
    • Akamine, A.1    Raghu, G.2    Narayanan, A.S.3
  • 31
    • 79957536131 scopus 로고    scopus 로고
    • Quantitative analysis of transient and sustained transforming growth factor-β signaling dynamics
    • Zi, Z., Feng, Z., Chapnick, D. A., Dahl, M., Deng, D., Klipp, E., Moustakas, A., and Liu, X. (2011) Quantitative analysis of transient and sustained transforming growth factor-β signaling dynamics. Mol. Syst. Biol. 7, 492
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 492
    • Zi, Z.1    Feng, Z.2    Chapnick, D.A.3    Dahl, M.4    Deng, D.5    Klipp, E.6    Moustakas, A.7    Liu, X.8
  • 34
    • 25144497589 scopus 로고    scopus 로고
    • Labelling of four distinct trophozoite falcipains of Plasmodium falciparum by a cystatin-derived probe
    • Florent, I., Lecaille, F., Montagne, J.-J., Gauthier, F., Schrével, J., and Lalmanach, G. (2005) Labelling of four distinct trophozoite falcipains of Plasmodium falciparum by a cystatin-derived probe. Biol. Chem. 386, 401-406
    • (2005) Biol. Chem. , vol.386 , pp. 401-406
    • Florent, I.1    Lecaille, F.2    Montagne, J.-J.3    Gauthier, F.4    Schrével, J.5    Lalmanach, G.6
  • 35
    • 52649142110 scopus 로고    scopus 로고
    • Overexpression of cathepsin K in mice decreases collagen deposition and lung resistance in response to bleomycin-induced pulmonary fibrosis
    • Srivastava, M., Steinwede, K., Kiviranta, R., Morko, J., Hoymann, H.-G., Länger, F., Buhling, F., Welte, T., and Maus, U. A. (2008) Overexpression of cathepsin K in mice decreases collagen deposition and lung resistance in response to bleomycin-induced pulmonary fibrosis. Respir. Res. 9, 54
    • (2008) Respir. Res. , vol.9 , pp. 54
    • Srivastava, M.1    Steinwede, K.2    Kiviranta, R.3    Morko, J.4    Hoymann, H.-G.5    Länger, F.6    Buhling, F.7    Welte, T.8    Maus, U.A.9
  • 36
    • 84855503594 scopus 로고    scopus 로고
    • Cathepsin B overexpression due to acid sphingomyelinase ablation promotes liver fibrosis in Niemann-Pick disease
    • Moles, A., Tarrats, N., Fernández-Checa, J. C., and Marí, M. (2012) Cathepsin B overexpression due to acid sphingomyelinase ablation promotes liver fibrosis in Niemann-Pick disease. J. Biol. Chem. 287, 1178-1188
    • (2012) J. Biol. Chem. , vol.287 , pp. 1178-1188
    • Moles, A.1    Tarrats, N.2    Fernández-Checa, J.C.3    Marí, M.4
  • 39
    • 0031760367 scopus 로고    scopus 로고
    • Cysteine proteinases and cystatin C in bronchoalveolar lavage fluid from subjects with subclinical emphysema
    • Takeyabu, K., Betsuyaku, T., Nishimura, M., Yoshioka, A., Tanino, M., Miyamoto, K., and Kawakami, Y. (1998) Cysteine proteinases and cystatin C in bronchoalveolar lavage fluid from subjects with subclinical emphysema. Eur. Respir. J. 12, 1033-1039
    • (1998) Eur. Respir. J. , vol.12 , pp. 1033-1039
    • Takeyabu, K.1    Betsuyaku, T.2    Nishimura, M.3    Yoshioka, A.4    Tanino, M.5    Miyamoto, K.6    Kawakami, Y.7
  • 40
    • 32344440534 scopus 로고    scopus 로고
    • Cathepsin B localizes to plasma membrane caveolae of differentiating myoblasts and is secreted in an active form at physiological pH
    • Jane, D. T., Morvay, L., Dasilva, L., Cavallo-Medved, D., Sloane, B. F., and Dufresne, M. J. (2006) Cathepsin B localizes to plasma membrane caveolae of differentiating myoblasts and is secreted in an active form at physiological pH. Biol. Chem. 387, 223-234
    • (2006) Biol. Chem. , vol.387 , pp. 223-234
    • Jane, D.T.1    Morvay, L.2    Dasilva, L.3    Cavallo-Medved, D.4    Sloane, B.F.5    Dufresne, M.J.6
  • 41
  • 42
    • 43049146157 scopus 로고    scopus 로고
    • The role of proteases in transforming growth factorbeta activation
    • Jenkins, G. (2008) The role of proteases in transforming growth factorbeta activation. Int. J. Biochem. Cell Biol. 40, 1068-1078
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1068-1078
    • Jenkins, G.1
  • 44
    • 40549131272 scopus 로고    scopus 로고
    • Extracellular matrix dynamics in development and regenerative medicine
    • Daley, W. P., Peters, S. B., and Larsen, M. (2008) Extracellular matrix dynamics in development and regenerative medicine. J. Cell Sci. 121, 255-264
    • (2008) J. Cell Sci. , vol.121 , pp. 255-264
    • Daley, W.P.1    Peters, S.B.2    Larsen, M.3
  • 45
    • 0023710423 scopus 로고
    • Identification of mannose 6-phosphate in two asparagine-linked sugar chains of recombinant transforming growth factor-beta 1 precursor
    • Purchio, A. F., Cooper, J. A., Brunner, A. M., Lioubin, M. N., Gentry, L. E., Kovacina, K. S., Roth, R. A., and Marquardt, H. (1988) Identification of mannose 6-phosphate in two asparagine-linked sugar chains of recombinant transforming growth factor-beta 1 precursor. J. Biol. Chem. 263, 14211-14215
    • (1988) J. Biol. Chem. , vol.263 , pp. 14211-14215
    • Purchio, A.F.1    Cooper, J.A.2    Brunner, A.M.3    Lioubin, M.N.4    Gentry, L.E.5    Kovacina, K.S.6    Roth, R.A.7    Marquardt, H.8
  • 46
    • 0037067762 scopus 로고    scopus 로고
    • Functional analysis of cathepsin B-like cysteine proteases from Leishmania donovani complex. Evidence for the activation of latent transforming growth factor beta
    • Somanna, A., Mundodi, V., and Gedamu, L. (2002) Functional analysis of cathepsin B-like cysteine proteases from Leishmania donovani complex. Evidence for the activation of latent transforming growth factor beta. J. Biol. Chem. 277, 25305-25312
    • (2002) J. Biol. Chem. , vol.277 , pp. 25305-25312
    • Somanna, A.1    Mundodi, V.2    Gedamu, L.3
  • 47
    • 84871234236 scopus 로고    scopus 로고
    • UPAR and cathepsin B shRNA impedes TGF-β1-driven proliferation and invasion of meningioma cells in a XIAP-dependent pathway
    • Gogineni, V. R., Gupta, R., Nalla, A. K., Velpula, K. K., and Rao, J. S. (2012) uPAR and cathepsin B shRNA impedes TGF-β1-driven proliferation and invasion of meningioma cells in a XIAP-dependent pathway. Cell Death Dis. 3, e439
    • (2012) Cell Death Dis. , vol.3
    • Gogineni, V.R.1    Gupta, R.2    Nalla, A.K.3    Velpula, K.K.4    Rao, J.S.5
  • 48
    • 0023879547 scopus 로고
    • Recombinant type 1 transforming growth factor beta precursor produced in Chinese hamster ovary cells is glycosylated and phosphorylated
    • Brunner, A. M., Gentry, L. E., Cooper, J. A., and Purchio, A. F. (1988) Recombinant type 1 transforming growth factor beta precursor produced in Chinese hamster ovary cells is glycosylated and phosphorylated. Moll. Cell Biol. 8, 2229-2232
    • (1988) Moll. Cell Biol. , vol.8 , pp. 2229-2232
    • Brunner, A.M.1    Gentry, L.E.2    Cooper, J.A.3    Purchio, A.F.4
  • 50
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-beta signaling from cell membrane to the nucleus
    • Shi, Y., and Massagué, J. (2003) Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell 113, 685-700
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massagué, J.2
  • 51
    • 0029007093 scopus 로고
    • Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages
    • Reddy, V. Y., Zhang, Q. Y., and Weiss, S. J. (1995) Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc. Natl. Acad. Sci. U. S. A. 92, 3849-3853
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3849-3853
    • Reddy, V.Y.1    Zhang, Q.Y.2    Weiss, S.J.3
  • 52
    • 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, G. K., Shi, G. P., Simon, D. I., Chapman, H. A., and Libby, P. (1998) Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. J. Clin. Invest. 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
  • 54
    • 33644882743 scopus 로고    scopus 로고
    • Variable expression of cystatin C in cultured trans-differentiating rat hepatic stellate cells
    • Gressner, A. M., Lahme, B., Meurer, S. K., Gressner, O., and Weiskirchen, R. (2006) Variable expression of cystatin C in cultured trans-differentiating rat hepatic stellate cells. World J. Gastroenterol. 12, 731-738
    • (2006) World J. Gastroenterol. , vol.12 , pp. 731-738
    • Gressner, A.M.1    Lahme, B.2    Meurer, S.K.3    Gressner, O.4    Weiskirchen, R.5
  • 55
    • 34447328697 scopus 로고    scopus 로고
    • The upregulation of cystatin C in oral submucous fibrosis
    • Chung-Hung, T., Shun-Fa, Y., and Yu-Chao, C. (2007) The upregulation of cystatin C in oral submucous fibrosis. Oral Oncol. 43, 680-685
    • (2007) Oral Oncol. , vol.43 , pp. 680-685
    • Chung-Hung, T.1    Shun-Fa, Y.2    Yu-Chao, C.3
  • 57
    • 0037899249 scopus 로고    scopus 로고
    • The myofibroblast in wound healing and fibrocontractive diseases
    • Gabbiani, G. (2003) The myofibroblast in wound healing and fibrocontractive diseases. J. Pathol. 200, 500-503
    • (2003) J. Pathol. , vol.200 , pp. 500-503
    • Gabbiani, G.1
  • 58
    • 0027861133 scopus 로고
    • Secretion of a latent, acid activatable cathepsin L precursor by human non-small cell lung cancer cell lines
    • Heidtmann, H. H., Salge, U., Havemann, K., Kirschke, H., and Wiederanders, B. (1993) Secretion of a latent, acid activatable cathepsin L precursor by human non-small cell lung cancer cell lines. Oncol. Res. 5, 441-451
    • (1993) Oncol. Res. , vol.5 , pp. 441-451
    • Heidtmann, H.H.1    Salge, U.2    Havemann, K.3    Kirschke, H.4    Wiederanders, B.5
  • 60
    • 77953178516 scopus 로고    scopus 로고
    • Cathepsin B is the driving force of esophageal cell invasion in a fibroblastdependent manner
    • Andl, C. D., McCowan, K. M., Allison, G. L., and Rustgi, A. K. (2010) Cathepsin B is the driving force of esophageal cell invasion in a fibroblastdependent manner. Neoplasia 12, 485-498
    • (2010) Neoplasia , vol.12 , pp. 485-498
    • Andl, C.D.1    McCowan, K.M.2    Allison, G.L.3    Rustgi, A.K.4
  • 61
    • 84869193514 scopus 로고    scopus 로고
    • TGF-β Signaling, Activated Stromal Fibroblasts, and Cysteine Cathepsins B and L Drive the Invasive Growth of Human Melanoma Cells
    • Yin, M., Soikkeli, J., Jahkola, T., Virolainen, S., Saksela, O., and Hölttä, E. (2012) TGF-β Signaling, Activated Stromal Fibroblasts, and Cysteine Cathepsins B and L Drive the Invasive Growth of Human Melanoma Cells. Am. J. Pathol. 181, 2202-2216
    • (2012) Am. J. Pathol. , vol.181 , pp. 2202-2216
    • Yin, M.1    Soikkeli, J.2    Jahkola, T.3    Virolainen, S.4    Saksela, O.5    Hölttä, E.6
  • 62
    • 0037177886 scopus 로고    scopus 로고
    • Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-betaL a process initiated by the exocytosis of cathepsin B
    • Guo, M., Mathieu, P. A., Linebaugh, B., Sloane, B. F., and Reiners, J. J., Jr (2002) Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-betaL a process initiated by the exocytosis of cathepsin B. J. Biol. Chem. 277, 14829-14837
    • (2002) J. Biol. Chem. , vol.277 , pp. 14829-14837
    • Guo, M.1    Mathieu, P.A.2    Linebaugh, B.3    Sloane, B.F.4    Reiners Jr., J.J.5
  • 63
    • 0036661078 scopus 로고    scopus 로고
    • CA-074, but not its methyl ester CA-074Me, is a selective inhibitor of cathepsin B within living cells
    • Montaser, M., Lalmanach, G., and Mach, L. (2002) CA-074, but not its methyl ester CA-074Me, is a selective inhibitor of cathepsin B within living cells. Biol. Chem. 383, 1305-1308
    • (2002) Biol. Chem. , vol.383 , pp. 1305-1308
    • Montaser, M.1    Lalmanach, G.2    Mach, L.3
  • 64
    • 77955907280 scopus 로고    scopus 로고
    • CystatinCincreases in cardiac injury: A role in extracellular matrix protein modulation
    • Xie, L., Terrand, J., Xu, B., Tsaprailis, G., Boyer, J., and Chen, Q. M. (2010) CystatinCincreases in cardiac injury: a role in extracellular matrix protein modulation. Cardiovasc. Res. 87, 628-635
    • (2010) Cardiovasc. Res. , vol.87 , pp. 628-635
    • Xie, L.1    Terrand, J.2    Xu, B.3    Tsaprailis, G.4    Boyer, J.5    Chen, Q.M.6


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