메뉴 건너뛰기




Volumn 388, Issue 11, 2007, Pages 1131-1140

Cysteine cathepsin non-inhibitory binding partners: Modulating intracellular trafficking and function

Author keywords

Cancer; Cathepsin B; Cysteine cathepsin; Glycosaminoglycan

Indexed keywords

BINDING PROTEIN; CATHEPSIN; CYSTEINE; GLYCOSAMINOGLYCAN;

EID: 35848947186     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2007.150     Document Type: Conference Paper
Times cited : (18)

References (127)
  • 4
    • 0034256042 scopus 로고    scopus 로고
    • Regulated secretion of conventional lysosomes
    • Andrews, N.W. (2000). Regulated secretion of conventional lysosomes. Trends Cell Biol. 10, 316-321.
    • (2000) Trends Cell Biol , vol.10 , pp. 316-321
    • Andrews, N.W.1
  • 5
    • 0033202958 scopus 로고    scopus 로고
    • The lectin ERGIC-53 is a cargo transport receptor for glycoproteins
    • Appenzeller, C., Andersson, H., Kappeler, F., and Hauri, H.P. (1999). The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. Nat. Cell Biol. 1, 330-334.
    • (1999) Nat. Cell Biol , vol.1 , pp. 330-334
    • Appenzeller, C.1    Andersson, H.2    Kappeler, F.3    Hauri, H.P.4
  • 6
    • 1842529346 scopus 로고    scopus 로고
    • pH-induced conversion of the transport lectin ERGIC-53 triggers glycoprotein release
    • Appenzeller-Herzog, C., Roche, A.C., Nufer, O., and Hauri, H.P. (2004). pH-induced conversion of the transport lectin ERGIC-53 triggers glycoprotein release. J. Biol. Chem. 279, 12943-12950.
    • (2004) J. Biol. Chem , vol.279 , pp. 12943-12950
    • Appenzeller-Herzog, C.1    Roche, A.C.2    Nufer, O.3    Hauri, H.P.4
  • 9
    • 0031983123 scopus 로고    scopus 로고
    • Intact vitronectin induces matrix metalloproteinase-2 and tissue inhibitor of metalloproteinases-2 expression and enhanced cellular invasion by melanoma cells
    • Bafetti, L.M., Young, T.N., Itoh, Y., and Stack, M.S. (1998). Intact vitronectin induces matrix metalloproteinase-2 and tissue inhibitor of metalloproteinases-2 expression and enhanced cellular invasion by melanoma cells. J. Biol. Chem. 273, 143-149.
    • (1998) J. Biol. Chem , vol.273 , pp. 143-149
    • Bafetti, L.M.1    Young, T.N.2    Itoh, Y.3    Stack, M.S.4
  • 10
    • 0032417878 scopus 로고    scopus 로고
    • Galanin causes Cl- secretion in the human colon. Potential significance of inflammation-associated NF-κB activation on galanin-1 receptor expression and function
    • Benya, R.V., Matkowskyj, K.A., Danilkovich, A., and Hecht, G. (1998). Galanin causes Cl- secretion in the human colon. Potential significance of inflammation-associated NF-κB activation on galanin-1 receptor expression and function. Ann. NY Acad. Sci. 863, 64-77.
    • (1998) Ann. NY Acad. Sci , vol.863 , pp. 64-77
    • Benya, R.V.1    Matkowskyj, K.A.2    Danilkovich, A.3    Hecht, G.4
  • 13
    • 0034527909 scopus 로고    scopus 로고
    • SETA is a multifunctional adapter protein with three SH3 domains that binds Grb2, Cbl, and the novel SB1 proteins
    • Borinstein, S.C., Hyatt, M.A., Sykes, V.W., Straub, R.E., Lipkowitz, S., Boulter, J., and Bogler, O. (2000). SETA is a multifunctional adapter protein with three SH3 domains that binds Grb2, Cbl, and the novel SB1 proteins. Cell. Signal. 12, 769-779.
    • (2000) Cell. Signal , vol.12 , pp. 769-779
    • Borinstein, S.C.1    Hyatt, M.A.2    Sykes, V.W.3    Straub, R.E.4    Lipkowitz, S.5    Boulter, J.6    Bogler, O.7
  • 14
    • 0029996240 scopus 로고    scopus 로고
    • Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells
    • Brix, K., Lemansky, P., and Herzog, V. (1996). Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells. Endocrinology 137, 1963-1974.
    • (1996) Endocrinology , vol.137 , pp. 1963-1974
    • Brix, K.1    Lemansky, P.2    Herzog, V.3
  • 15
    • 0037468859 scopus 로고    scopus 로고
    • TSRC1, a widely expressed gene containing seven thrombospondin type I repeats
    • Buchner, D.A. and Meisler, M.H. (2003). TSRC1, a widely expressed gene containing seven thrombospondin type I repeats. Gene 307, 23-30.
    • (2003) Gene , vol.307 , pp. 23-30
    • Buchner, D.A.1    Meisler, M.H.2
  • 17
    • 0028145293 scopus 로고
    • Cathepsin B expression in colorectal carcinomas correlates with tumor progression and shortened patient survival
    • Campo, E., Munoz, J., Miquel, R., Palacin, A., Cardesa, A., Sloane, B.F., and Emmert-Buck, M.R. (1994). Cathepsin B expression in colorectal carcinomas correlates with tumor progression and shortened patient survival. Am. J. Pathol. 145, 301-309.
    • (1994) Am. J. Pathol , vol.145 , pp. 301-309
    • Campo, E.1    Munoz, J.2    Miquel, R.3    Palacin, A.4    Cardesa, A.5    Sloane, B.F.6    Emmert-Buck, M.R.7
  • 19
    • 0036034837 scopus 로고    scopus 로고
    • New developments in the genetics and activation of mast cell proteases
    • Caughey, G.H. (2002). New developments in the genetics and activation of mast cell proteases. Mol. Immunol. 38, 1353-1357.
    • (2002) Mol. Immunol , vol.38 , pp. 1353-1357
    • Caughey, G.H.1
  • 20
    • 0642339104 scopus 로고    scopus 로고
    • Cell-surface cathepsin B: Understanding its functional significance
    • Cavallo-Medved, D. and Sloane, B.F. (2003). Cell-surface cathepsin B: understanding its functional significance. Curr. Top. Dev. Biol. 54, 313-341.
    • (2003) Curr. Top. Dev. Biol , vol.54 , pp. 313-341
    • Cavallo-Medved, D.1    Sloane, B.F.2
  • 21
    • 0347683401 scopus 로고    scopus 로고
    • Mutant K-ras regulates cathepsin B localization on the surface of human colorectal carcinoma cells
    • Cavallo-Medved, D., Dosescu, J., Linebaugh, B.E., Sameni, M., Rudy, D., and Sloane, B.F. (2003). Mutant K-ras regulates cathepsin B localization on the surface of human colorectal carcinoma cells. Neoplasia 5, 507-519.
    • (2003) Neoplasia , vol.5 , pp. 507-519
    • Cavallo-Medved, D.1    Dosescu, J.2    Linebaugh, B.E.3    Sameni, M.4    Rudy, D.5    Sloane, B.F.6
  • 22
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman, H.A., Riese, R.J., and Shi, G.P. (1997). Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol. 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
    • 0030949251 scopus 로고    scopus 로고
    • Differentiation-induced changes in the content, secretion, and subcellular distribution of lysosomal cathepsins in the human colon cancer HT-29 cell line
    • De Stefanis, D., Demoz, M., Dragonetti, A., Houri, J.J., Ogier-Denis, E., Codogno, P., Baccino, F.M., and Isidoro, C. (1997). Differentiation-induced changes in the content, secretion, and subcellular distribution of lysosomal cathepsins in the human colon cancer HT-29 cell line. Cell Tissue Res. 289, 109-117.
    • (1997) Cell Tissue Res , vol.289 , pp. 109-117
    • De Stefanis, D.1    Demoz, M.2    Dragonetti, A.3    Houri, J.J.4    Ogier-Denis, E.5    Codogno, P.6    Baccino, F.M.7    Isidoro, C.8
  • 24
    • 0032932834 scopus 로고    scopus 로고
    • Evidence for protein splicing in the endoplasmic reticulum-Golgi intermediate compartment
    • Demirov, D., Sarafian, V., Kremensky, I., and Ganev, V. (1999). Evidence for protein splicing in the endoplasmic reticulum-Golgi intermediate compartment. Biochim. Biophys. Acta 1448, 507-511.
    • (1999) Biochim. Biophys. Acta , vol.1448 , pp. 507-511
    • Demirov, D.1    Sarafian, V.2    Kremensky, I.3    Ganev, V.4
  • 28
    • 11144277680 scopus 로고    scopus 로고
    • Effects of triple therapy with octreotide, galanin and serotonin on liver metastasis of human colon cancer in xenografts
    • El-Salhy, M. and Dennerqvist, V. (2004). Effects of triple therapy with octreotide, galanin and serotonin on liver metastasis of human colon cancer in xenografts. Oncol. Rep. 11, 1177-1182.
    • (2004) Oncol. Rep , vol.11 , pp. 1177-1182
    • El-Salhy, M.1    Dennerqvist, V.2
  • 31
    • 0022504458 scopus 로고
    • Isolation of a cDNA clone for the human lysosomal proteinase cathepsin B
    • Fong, D., Calhoun, D.H., Hsieh, W.T., Lee, B., and Wells, R.D. (1986). Isolation of a cDNA clone for the human lysosomal proteinase cathepsin B. Proc. Natl. Acad. Sci. USA 83, 2909-2913.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2909-2913
    • Fong, D.1    Calhoun, D.H.2    Hsieh, W.T.3    Lee, B.4    Wells, R.D.5
  • 32
    • 0026518253 scopus 로고
    • Confirmation of the human cathepsin B gene (CTSB) assignment to chromosome 8
    • Fong, D., Chan, M.M., Hsieh, W.T., Menninger, J.C., and Ward, D.C. (1992). Confirmation of the human cathepsin B gene (CTSB) assignment to chromosome 8. Hum. Genet. 89, 10-12.
    • (1992) Hum. Genet , vol.89 , pp. 10-12
    • Fong, D.1    Chan, M.M.2    Hsieh, W.T.3    Menninger, J.C.4    Ward, D.C.5
  • 33
    • 0033987191 scopus 로고    scopus 로고
    • Bikunin - not just a plasma proteinase inhibitor
    • Fries, E. and Blom, A.M. (2000). Bikunin - not just a plasma proteinase inhibitor. Int. J. Biochem. Cell. Biol. 32, 125-137.
    • (2000) Int. J. Biochem. Cell. Biol , vol.32 , pp. 125-137
    • Fries, E.1    Blom, A.M.2
  • 34
    • 33746888208 scopus 로고    scopus 로고
    • Inhibitors of cathepsin B
    • Frlan, R. and Gobec, S. (2006). Inhibitors of cathepsin B. Curr. Med. Chem. 13, 2309-2327.
    • (2006) Curr. Med. Chem , vol.13 , pp. 2309-2327
    • Frlan, R.1    Gobec, S.2
  • 36
    • 14844282775 scopus 로고    scopus 로고
    • Structural and biochemical characterization of CIB1 delineates a new family of EF-hand-containing proteins
    • Gentry, H.R., Singer, A.U., Betts, L., Yang, C., Ferrara, J.D., Sondek, J., and Parise, L.V. (2005). Structural and biochemical characterization of CIB1 delineates a new family of EF-hand-containing proteins. J. Biol. Chem. 280, 8407-8415.
    • (2005) J. Biol. Chem , vol.280 , pp. 8407-8415
    • Gentry, H.R.1    Singer, A.U.2    Betts, L.3    Yang, C.4    Ferrara, J.D.5    Sondek, J.6    Parise, L.V.7
  • 38
    • 33846643454 scopus 로고    scopus 로고
    • Cysteine cathepsins and the cutting edge of cancer invasion
    • Gocheva, V. and Joyce, J.A. (2007). Cysteine cathepsins and the cutting edge of cancer invasion. Cell Cycle 6, 60-64.
    • (2007) Cell Cycle , vol.6 , pp. 60-64
    • Gocheva, V.1    Joyce, J.A.2
  • 40
    • 9144231998 scopus 로고    scopus 로고
    • RNAi-mediated inhibition of cathepsin B and uPAR leads to decreased cell invasion, angiogenesis and tumor growth in gliomas
    • Gondi, C.S., Lakka, S.S., Dinh, D.H., Olivero, W.C., Gujrati, M., and Rao, J.S. (2004a). RNAi-mediated inhibition of cathepsin B and uPAR leads to decreased cell invasion, angiogenesis and tumor growth in gliomas. Oncogene 23, 8486-8496.
    • (2004) Oncogene , vol.23 , pp. 8486-8496
    • Gondi, C.S.1    Lakka, S.S.2    Dinh, D.H.3    Olivero, W.C.4    Gujrati, M.5    Rao, J.S.6
  • 41
    • 3042551389 scopus 로고    scopus 로고
    • Adenovirus-mediated expression of antisense urokinase plasminogen activator receptor and antisense cathepsin B inhibits tumor growth, invasion, and angiogenesis in gliomas
    • Gondi, C.S., Lakka, S.S., Yanamandra, N., Olivero, W.C., Dinh, D.H., Gujrati, M., Tung, C.H., Weissleder, R., and Rao, J.S. (2004b). Adenovirus-mediated expression of antisense urokinase plasminogen activator receptor and antisense cathepsin B inhibits tumor growth, invasion, and angiogenesis in gliomas. Cancer Res. 64, 4069-4077.
    • (2004) Cancer Res , vol.64 , pp. 4069-4077
    • Gondi, C.S.1    Lakka, S.S.2    Yanamandra, N.3    Olivero, W.C.4    Dinh, D.H.5    Gujrati, M.6    Tung, C.H.7    Weissleder, R.8    Rao, J.S.9
  • 43
    • 0035180207 scopus 로고    scopus 로고
    • Cathepsin B knockout mice are resistant to tumor necrosis factor-α- mediated hepatocyte apoptosis and liver injury: Implications for therapeutic applications
    • Guicciardi, M.E., Miyoshi, H., Bronk, S.F., and Gores, G.J. (2001). Cathepsin B knockout mice are resistant to tumor necrosis factor-α- mediated hepatocyte apoptosis and liver injury: implications for therapeutic applications. Am. J. Pathol. 159, 2045-2054.
    • (2001) Am. J. Pathol , vol.159 , pp. 2045-2054
    • Guicciardi, M.E.1    Miyoshi, H.2    Bronk, S.F.3    Gores, G.J.4
  • 44
    • 0027931667 scopus 로고
    • A lipoxygenase metabolite, 12-(S)-HETE, stimulates protein kinase C-mediated release of cathepsin B from malignant cells
    • Honn, K.V., Timar, J., Rozhin, J., Bazaz, R., Sameni, M., Ziegler, G., and Sloane, B.F. (1994). A lipoxygenase metabolite, 12-(S)-HETE, stimulates protein kinase C-mediated release of cathepsin B from malignant cells. Exp. Cell Res. 214, 120-130.
    • (1994) Exp. Cell Res , vol.214 , pp. 120-130
    • Honn, K.V.1    Timar, J.2    Rozhin, J.3    Bazaz, R.4    Sameni, M.5    Ziegler, G.6    Sloane, B.F.7
  • 45
    • 0022376534 scopus 로고
    • Different immunolocalizations of cathepsins B, H, and L in the liver
    • Ii, K., Hizawa, K., Kominami, E., Bando, Y., and Katunuma, N. (1985). Different immunolocalizations of cathepsins B, H, and L in the liver. J. Histochem. Cytochem. 33, 1173-1175.
    • (1985) J. Histochem. Cytochem , vol.33 , pp. 1173-1175
    • Ii, K.1    Hizawa, K.2    Kominami, E.3    Bando, Y.4    Katunuma, N.5
  • 46
    • 0029038786 scopus 로고
    • Chemoprevention by galanin against colon carcinogenesis induced by azoxymethane in Wistar rats
    • Iishi, H., Tatsuta, M., Baba, M., Uehara, H., Yano, H., and Nakaizumi, A. (1995). Chemoprevention by galanin against colon carcinogenesis induced by azoxymethane in Wistar rats. Int. J. Cancer 61, 861-863.
    • (1995) Int. J. Cancer , vol.61 , pp. 861-863
    • Iishi, H.1    Tatsuta, M.2    Baba, M.3    Uehara, H.4    Yano, H.5    Nakaizumi, A.6
  • 47
    • 0029876344 scopus 로고    scopus 로고
    • ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins
    • Itin, C., Roche, A.C., Monsigny, M., and Hauri, H.P. (1996). ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins. Mol. Biol. Cell 7, 483-493.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 483-493
    • Itin, C.1    Roche, A.C.2    Monsigny, M.3    Hauri, H.P.4
  • 49
    • 10044296973 scopus 로고    scopus 로고
    • Cysteine cathepsins in human cancer
    • Jedeszko, C. and Sloane, B.F. (2004). Cysteine cathepsins in human cancer. Biol. Chem. 385, 1017-1027.
    • (2004) Biol. Chem , vol.385 , pp. 1017-1027
    • Jedeszko, C.1    Sloane, B.F.2
  • 50
    • 0031450221 scopus 로고    scopus 로고
    • The recycling of ERGIC-53 in the early secretory pathway. ERGIC-53 carries a cytosolic endoplasmic reticulum-exit determinant interacting with COPII
    • Kappeler, F., Klopfenstein, D.R., Foguet, M., Paccaud, J.P., and Hauri, H.P. (1997). The recycling of ERGIC-53 in the early secretory pathway. ERGIC-53 carries a cytosolic endoplasmic reticulum-exit determinant interacting with COPII. J. Biol. Chem. 272, 31801-31808.
    • (1997) J. Biol. Chem , vol.272 , pp. 31801-31808
    • Kappeler, F.1    Klopfenstein, D.R.2    Foguet, M.3    Paccaud, J.P.4    Hauri, H.P.5
  • 51
  • 52
    • 0242613912 scopus 로고    scopus 로고
    • Role of laminin in matrix induction of macrophage urokinase-type plasminogen activator and 92-kDa metalloproteinase expression
    • Khan, K.M. and Falcone, D.J. (1997). Role of laminin in matrix induction of macrophage urokinase-type plasminogen activator and 92-kDa metalloproteinase expression. J. Biol. Chem. 272, 8270-8275.
    • (1997) J. Biol. Chem , vol.272 , pp. 8270-8275
    • Khan, K.M.1    Falcone, D.J.2
  • 53
    • 0033850811 scopus 로고    scopus 로고
    • Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase
    • Klemencic, I., Carmona, A.K., Cezari, M.H., Juliano, M.A., Juliano, L., Guncar, G., Turk, D., Krizaj, I., Turk, V., and Turk, B. (2000). Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase. Eur. J. Biochem. 267, 5404-5412.
    • (2000) Eur. J. Biochem , vol.267 , pp. 5404-5412
    • Klemencic, I.1    Carmona, A.K.2    Cezari, M.H.3    Juliano, M.A.4    Juliano, L.5    Guncar, G.6    Turk, D.7    Krizaj, I.8    Turk, V.9    Turk, B.10
  • 54
    • 33646366421 scopus 로고    scopus 로고
    • Contact of high-invasive, but not low-invasive, melanoma cells to native collagen I induces the release of mature cathepsin B
    • Klose, A., Wilbrand-Hennes, A., Zigrino, P., Weber, E., Krieg, T., Mauch, C., and Hunzelmann, N. (2006). Contact of high-invasive, but not low-invasive, melanoma cells to native collagen I induces the release of mature cathepsin B. Int. J. Cancer 118, 2735-2743.
    • (2006) Int. J. Cancer , vol.118 , pp. 2735-2743
    • Klose, A.1    Wilbrand-Hennes, A.2    Zigrino, P.3    Weber, E.4    Krieg, T.5    Mauch, C.6    Hunzelmann, N.7
  • 55
    • 0026734254 scopus 로고
    • Inhibition of in vitro ovarian cancer cell invasion by modulation of urokinase-type plasminogen activator and cathepsin B
    • Kobayashi, H., Ohi, H., Sugimura, M., Shinohara, H., Fujii, T., and Terao, T. (1992). Inhibition of in vitro ovarian cancer cell invasion by modulation of urokinase-type plasminogen activator and cathepsin B. Cancer Res. 52, 3610-3614.
    • (1992) Cancer Res , vol.52 , pp. 3610-3614
    • Kobayashi, H.1    Ohi, H.2    Sugimura, M.3    Shinohara, H.4    Fujii, T.5    Terao, T.6
  • 56
    • 0037200058 scopus 로고    scopus 로고
    • Interaction of human breast fibroblasts with collagen I increases secretion of procathepsin
    • Koblinski, J.E., Dosescu, J., Sameni, M., Moin, K., Clark, K., and Sloane, B.F. (2002). Interaction of human breast fibroblasts with collagen I increases secretion of procathepsin B. J. Biol. Chem. 277, 32220-32227.
    • (2002) B. J. Biol. Chem , vol.277 , pp. 32220-32227
    • Koblinski, J.E.1    Dosescu, J.2    Sameni, M.3    Moin, K.4    Clark, K.5    Sloane, B.F.6
  • 58
    • 0022572229 scopus 로고
    • Trafficking of lysosomal enzymes in normal and disease states
    • Kornfeld, S. (1986). Trafficking of lysosomal enzymes in normal and disease states. J. Clin. Invest. 77, 1-6.
    • (1986) J. Clin. Invest , vol.77 , pp. 1-6
    • Kornfeld, S.1
  • 59
    • 0025365591 scopus 로고
    • Lysosomal enzyme targeting
    • Kornfeld, S. (1990). Lysosomal enzyme targeting. Biochem. Soc. Trans. 18, 367-374.
    • (1990) Biochem. Soc. Trans , vol.18 , pp. 367-374
    • Kornfeld, S.1
  • 60
    • 0033406453 scopus 로고    scopus 로고
    • Inhibitory effects of antisense cathepsin B cDNA transfection on invasion and motility in a human osteosarcoma cell line
    • Krueger, S., Haeckel, C., Buehling, F., and Roessner, A. (1999). Inhibitory effects of antisense cathepsin B cDNA transfection on invasion and motility in a human osteosarcoma cell line. Cancer Res. 59, 6010-6014.
    • (1999) Cancer Res , vol.59 , pp. 6010-6014
    • Krueger, S.1    Haeckel, C.2    Buehling, F.3    Roessner, A.4
  • 61
    • 2942718949 scopus 로고    scopus 로고
    • Inhibition of cathepsin B and MMP-9 gene expression in glioblastoma cell line via RNA interference reduces tumor cell invasion, tumor growth and angiogenesis
    • Lakka, S.S., Gondi, C.S., Yanamandra, N., Olivero, W.C., Dinh, D.H., Gujrati, M., and Rao, J.S. (2004). Inhibition of cathepsin B and MMP-9 gene expression in glioblastoma cell line via RNA interference reduces tumor cell invasion, tumor growth and angiogenesis. Oncogene 23, 4681-4689.
    • (2004) Oncogene , vol.23 , pp. 4681-4689
    • Lakka, S.S.1    Gondi, C.S.2    Yanamandra, N.3    Olivero, W.C.4    Dinh, D.H.5    Gujrati, M.6    Rao, J.S.7
  • 62
    • 0034711762 scopus 로고    scopus 로고
    • Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates
    • Li, Z., Hou, W.S., and Bromme, D. (2000). Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates. Biochemistry 39, 529-536.
    • (2000) Biochemistry , vol.39 , pp. 529-536
    • Li, Z.1    Hou, W.S.2    Bromme, D.3
  • 63
    • 0037047275 scopus 로고    scopus 로고
    • Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate
    • Li, Z., Hou, W.S., Escalante-Torres, C.R., Gelb, B.D., and Bromme, D. (2002). Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate. J. Biol. Chem. 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
  • 64
  • 65
    • 0033567263 scopus 로고    scopus 로고
    • Exocytosis of active cathepsin B enzyme activity at pH 7.0, inhibition and molecular mass
    • Linebaugh, B.E., Sameni, M., Day, N.A., Sloane, B.F., and Keppler, D. (1999). Exocytosis of active cathepsin B enzyme activity at pH 7.0, inhibition and molecular mass. Eur. J. Biochem. 264, 100-109.
    • (1999) Eur. J. Biochem , vol.264 , pp. 100-109
    • Linebaugh, B.E.1    Sameni, M.2    Day, N.A.3    Sloane, B.F.4    Keppler, D.5
  • 67
    • 29344465604 scopus 로고    scopus 로고
    • Cathepsin B and its interacting proteins, bikunin and TSRC1, correlate with TNF-induced apoptosis of ovarian cancer cells OV-90
    • Liu, J., Guo, Q., Chen, B., Yu, Y., Lu, H., and Li, Y.Y. (2006a). Cathepsin B and its interacting proteins, bikunin and TSRC1, correlate with TNF-induced apoptosis of ovarian cancer cells OV-90. FEBS Lett. 580, 245-250.
    • (2006) FEBS Lett , vol.580 , pp. 245-250
    • Liu, J.1    Guo, Q.2    Chen, B.3    Yu, Y.4    Lu, H.5    Li, Y.Y.6
  • 68
    • 33750701833 scopus 로고    scopus 로고
    • Human homologue of SETA binding protein 1 interacts with cathepsin B and participates in TNF-induced apoptosis in ovarian cancer cells
    • Liu, J.P., Liu, N.S., Yuan, H.Y., Guo, Q., Lu, H., and Li, Y.Y. (2006b). Human homologue of SETA binding protein 1 interacts with cathepsin B and participates in TNF-induced apoptosis in ovarian cancer cells. Mol. Cell. Biochem. 292, 189-195.
    • (2006) Mol. Cell. Biochem , vol.292 , pp. 189-195
    • Liu, J.P.1    Liu, N.S.2    Yuan, H.Y.3    Guo, Q.4    Lu, H.5    Li, Y.Y.6
  • 69
    • 0027932822 scopus 로고
    • Differential sorting of lysosomal enzymes in mannose 6-phosphate receptor-deficient fibroblasts
    • Ludwig, T., Munier-Lehmann, H., Bauer, U., Hollinshead, M., Ovitt, C., Lobel, P., and Hoflack, B. (1994). Differential sorting of lysosomal enzymes in mannose 6-phosphate receptor-deficient fibroblasts. EMBO J. 13, 3430-3437.
    • (1994) EMBO J , vol.13 , pp. 3430-3437
    • Ludwig, T.1    Munier-Lehmann, H.2    Bauer, U.3    Hollinshead, M.4    Ovitt, C.5    Lobel, P.6    Hoflack, B.7
  • 70
    • 0024599360 scopus 로고
    • Immunodetection of cathepsins B and L present in and secreted from human pre-malignant and malignant colorectal tumour cell lines
    • Maciewicz, R.A., Wardale, R.J., Etherington, D.J., and Paraskeva, C. (1989). Immunodetection of cathepsins B and L present in and secreted from human pre-malignant and malignant colorectal tumour cell lines. Int. J. Cancer 43, 478-486.
    • (1989) Int. J. Cancer , vol.43 , pp. 478-486
    • Maciewicz, R.A.1    Wardale, R.J.2    Etherington, D.J.3    Paraskeva, C.4
  • 71
    • 0034725119 scopus 로고    scopus 로고
    • Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells
    • Mai, J., Finley, R.L. Jr., Waisman, D.M., and Sloane, B.F. (2000). Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells. J. Biol. Chem. 275, 12806-12812.
    • (2000) J. Biol. Chem , vol.275 , pp. 12806-12812
    • Mai, J.1    Finley Jr., R.L.2    Waisman, D.M.3    Sloane, B.F.4
  • 73
    • 0024361284 scopus 로고
    • Collagenase gene expression in fibroblasts is regulated by a three-dimensional contact with collagen
    • Mauch, C., Adelmann-Grill, B., Hatamochi, A., and Krieg, T. (1989). Collagenase gene expression in fibroblasts is regulated by a three-dimensional contact with collagen. FEBS Lett. 250, 301-305.
    • (1989) FEBS Lett , vol.250 , pp. 301-305
    • Mauch, C.1    Adelmann-Grill, B.2    Hatamochi, A.3    Krieg, T.4
  • 74
    • 0027238714 scopus 로고
    • Secretion of cathepsin B by human gliomas in vitro
    • McCormick, D. (1993). Secretion of cathepsin B by human gliomas in vitro. Neuropathol. Appl. Neurobiol. 19, 146-151.
    • (1993) Neuropathol. Appl. Neurobiol , vol.19 , pp. 146-151
    • McCormick, D.1
  • 75
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: Multifunctional enzymes in cancer
    • Mohamed, M.M. and Sloane, B.F. (2006). Cysteine cathepsins: multifunctional enzymes in cancer. Nat. Rev. Cancer 6, 764-775.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 77
    • 0040366645 scopus 로고    scopus 로고
    • Human cathepsin X: A cysteine protease with unique carboxypeptidase activity
    • Nagler, D.K., Zhang, R., Tam, W., Sulea, T., Purisima, E.O., and Menard, R. (1999). Human cathepsin X: a cysteine protease with unique carboxypeptidase activity. Biochemistry 38, 12648-12654.
    • (1999) Biochemistry , vol.38 , pp. 12648-12654
    • Nagler, D.K.1    Zhang, R.2    Tam, W.3    Sulea, T.4    Purisima, E.O.5    Menard, R.6
  • 79
    • 0030966971 scopus 로고    scopus 로고
    • Inhibition of carcinoma cell invasion and liver metastases formation by the cysteine proteinase inhibitor E-64
    • Navab, R., Mort, J.S., and Brodt, P. (1997). Inhibition of carcinoma cell invasion and liver metastases formation by the cysteine proteinase inhibitor E-64. Clin. Exp. Metastasis 15, 121-129.
    • (1997) Clin. Exp. Metastasis , vol.15 , pp. 121-129
    • Navab, R.1    Mort, J.S.2    Brodt, P.3
  • 81
    • 18144394763 scopus 로고    scopus 로고
    • Capturing protein interactions in the secretory pathway of living cells
    • Nyfeler, B., Michnick, S.W., and Hauri, H.P. (2005). Capturing protein interactions in the secretory pathway of living cells. Proc. Natl. Acad. Sci. USA 102, 6350-6355.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6350-6355
    • Nyfeler, B.1    Michnick, S.W.2    Hauri, H.P.3
  • 82
    • 3042595457 scopus 로고    scopus 로고
    • Characterization of murine cathepsin W and its role in cell-mediated cytotoxicity
    • Ondr, J.K. and Pham, C.T. (2004). Characterization of murine cathepsin W and its role in cell-mediated cytotoxicity. J. Biol. Chem. 279, 27525-27533.
    • (2004) J. Biol. Chem , vol.279 , pp. 27525-27533
    • Ondr, J.K.1    Pham, C.T.2
  • 83
    • 0033587689 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo
    • Pham, C.T. and Ley, T.J. (1999). Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc. Natl. Acad. Sci. USA 96, 8627-8632.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8627-8632
    • Pham, C.T.1    Ley, T.J.2
  • 84
    • 1542495341 scopus 로고    scopus 로고
    • Cathepsin B and its role(s) in cancer progression
    • Podgorski, I. and Sloane, B.F. (2003). Cathepsin B and its role(s) in cancer progression. Biochem. Soc. Symp. 70, 263-276.
    • (2003) Biochem. Soc. Symp , vol.70 , pp. 263-276
    • Podgorski, I.1    Sloane, B.F.2
  • 85
    • 0017822028 scopus 로고
    • Differences in secretion of the proteinase cathepsin B at the edges of human breast carcinomas and fibroadenomas
    • Poole, A.R., Tiltman, K.J., Recklies, A.D., and Stoker, T.A. (1978). Differences in secretion of the proteinase cathepsin B at the edges of human breast carcinomas and fibroadenomas. Nature 273, 545-547.
    • (1978) Nature , vol.273 , pp. 545-547
    • Poole, A.R.1    Tiltman, K.J.2    Recklies, A.D.3    Stoker, T.A.4
  • 86
    • 0037442576 scopus 로고    scopus 로고
    • Intracellular and extracellular cathepsin B facilitate invasion of MCF-10A neoT cells through reconstituted extracellular matrix in vitro
    • Premzl, A., Zavasnik-Bergant, V., Turk, V., and Kos, J. (2003). Intracellular and extracellular cathepsin B facilitate invasion of MCF-10A neoT cells through reconstituted extracellular matrix in vitro. Exp. Cell Res. 283, 206-214.
    • (2003) Exp. Cell Res , vol.283 , pp. 206-214
    • Premzl, A.1    Zavasnik-Bergant, V.2    Turk, V.3    Kos, J.4
  • 87
    • 0029881827 scopus 로고    scopus 로고
    • The murine homolog of TB2/DP1, a gene of the familial adenomatous polyposis (FAP) locus
    • Prieschl, E.E., Pendl, G.G., Harrer, N.E., and Baumruker, T. (1996). The murine homolog of TB2/DP1, a gene of the familial adenomatous polyposis (FAP) locus. Gene 169, 215-218.
    • (1996) Gene , vol.169 , pp. 215-218
    • Prieschl, E.E.1    Pendl, G.G.2    Harrer, N.E.3    Baumruker, T.4
  • 89
    • 0034930528 scopus 로고    scopus 로고
    • Towards specific functions of lysosomal cysteine peptidases: Phenotypes of mice deficient for cathepsin B or cathepsin L
    • Reinheckel, T., Deussing, J., Roth, W., and Peters, C. (2001). Towards specific functions of lysosomal cysteine peptidases: phenotypes of mice deficient for cathepsin B or cathepsin L. Biol. Chem. 382, 735-741.
    • (2001) Biol. Chem , vol.382 , pp. 735-741
    • Reinheckel, T.1    Deussing, J.2    Roth, W.3    Peters, C.4
  • 93
    • 0038215389 scopus 로고    scopus 로고
    • Pericellular cathepsin B and malignant progression
    • Roshy, S., Sloane, B.F., and Moin, K. (2003). Pericellular cathepsin B and malignant progression. Cancer Metastasis Rev. 22, 271-286.
    • (2003) Cancer Metastasis Rev , vol.22 , pp. 271-286
    • Roshy, S.1    Sloane, B.F.2    Moin, K.3
  • 95
    • 0028618307 scopus 로고
    • Pericellular pH affects distribution and secretion of cathepsin B in malignant cells
    • Rozhin, J., Sameni, M., Ziegler, G., and Sloane, B.F. (1994). Pericellular pH affects distribution and secretion of cathepsin B in malignant cells. Cancer Res. 54, 6517-6525.
    • (1994) Cancer Res , vol.54 , pp. 6517-6525
    • Rozhin, J.1    Sameni, M.2    Ziegler, G.3    Sloane, B.F.4
  • 99
    • 0242577116 scopus 로고    scopus 로고
    • Functional imaging of proteolysis: Stromal and inflammatory cells increase tumor proteolysis
    • Sameni, M., Dosescu, J., Moin, K., and Sloane, B.F. (2003). Functional imaging of proteolysis: stromal and inflammatory cells increase tumor proteolysis. Mol. Imaging 2, 159-175.
    • (2003) Mol. Imaging , vol.2 , pp. 159-175
    • Sameni, M.1    Dosescu, J.2    Moin, K.3    Sloane, B.F.4
  • 100
    • 0032522413 scopus 로고    scopus 로고
    • Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas
    • Santamaria, I., Velasco, G., Cazorla, M., Fueyo, A., Campo, E., and Lopez-Otin, C. (1998). Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. Cancer Res. 58, 1624-1630.
    • (1998) Cancer Res , vol.58 , pp. 1624-1630
    • Santamaria, I.1    Velasco, G.2    Cazorla, M.3    Fueyo, A.4    Campo, E.5    Lopez-Otin, C.6
  • 101
    • 0034599498 scopus 로고    scopus 로고
    • Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
    • Shi, G.P., Bryant, R.A., Riese, R., Verhelst, S., Driessen, C., Li, Z., Bromme, D., Ploegh, H.L., and Chapman, H.A. (2000). Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J. Exp. Med. 191, 1177-1186.
    • (2000) J. Exp. Med , vol.191 , pp. 1177-1186
    • Shi, G.P.1    Bryant, R.A.2    Riese, R.3    Verhelst, S.4    Driessen, C.5    Li, Z.6    Bromme, D.7    Ploegh, H.L.8    Chapman, H.A.9
  • 103
    • 0027531160 scopus 로고
    • Localization of a biotinylated cathepsin B oligonucleotide probe in human prostate including invasive cells and invasive edges by in situ hybridization
    • Sinha, A.A., Gleason, D.F., Deleon, O.F., Wilson, M.J., and Sloane, B.F. (1993). Localization of a biotinylated cathepsin B oligonucleotide probe in human prostate including invasive cells and invasive edges by in situ hybridization. Anat. Rec. 235, 233-240.
    • (1993) Anat. Rec , vol.235 , pp. 233-240
    • Sinha, A.A.1    Gleason, D.F.2    Deleon, O.F.3    Wilson, M.J.4    Sloane, B.F.5
  • 104
    • 0028909688 scopus 로고
    • Immunohistochemical localization of cathepsin B in neoplastic human prostate
    • Sinha, A.A., Wilson, M.J., Gleason, D.F., Reddy, P.K., Sameni, M., and Sloane, B.F. (1995). Immunohistochemical localization of cathepsin B in neoplastic human prostate. Prostate 26, 171-178.
    • (1995) Prostate , vol.26 , pp. 171-178
    • Sinha, A.A.1    Wilson, M.J.2    Gleason, D.F.3    Reddy, P.K.4    Sameni, M.5    Sloane, B.F.6
  • 105
    • 0019797924 scopus 로고
    • Lysosomal cathepsin B: Correlation with metastatic potential
    • Sloane, B.F., Dunn, J.R., and Honn, K.V. (1981). Lysosomal cathepsin B: correlation with metastatic potential. Science 212, 1151-1153.
    • (1981) Science , vol.212 , pp. 1151-1153
    • Sloane, B.F.1    Dunn, J.R.2    Honn, K.V.3
  • 106
    • 0028273525 scopus 로고
    • Membrane association of cathepsin B can be induced by transfection of human breast epithelial cells with c-Ha-ras oncogene
    • Sloane, B.F., Moin, K., Sameni, M., Tait, L.R., Rozhin, J., and Ziegler, G. (1994). Membrane association of cathepsin B can be induced by transfection of human breast epithelial cells with c-Ha-ras oncogene. J. Cell Sci. 107, 373-384.
    • (1994) J. Cell Sci , vol.107 , pp. 373-384
    • Sloane, B.F.1    Moin, K.2    Sameni, M.3    Tait, L.R.4    Rozhin, J.5    Ziegler, G.6
  • 111
    • 0028206784 scopus 로고
    • Immunohistochemical distributions of cathepsin B and basement membrane antigens in human lung adenocarcinoma: Association with invasion and metastasis
    • Sukoh, N., Abe, S., Nakajima, I., Ogura, S., Isobe, H., Inoue, K., and Kawakami, Y. (1994). Immunohistochemical distributions of cathepsin B and basement membrane antigens in human lung adenocarcinoma: association with invasion and metastasis. Virchow's Arch. 424, 33-38.
    • (1994) Virchow's Arch , vol.424 , pp. 33-38
    • Sukoh, N.1    Abe, S.2    Nakajima, I.3    Ogura, S.4    Isobe, H.5    Inoue, K.6    Kawakami, Y.7
  • 112
    • 0035870263 scopus 로고    scopus 로고
    • An intracellular form of cathepsin B contributes to invasiveness in cancer
    • Szpaderska, A.M. and Frankfater, A. (2001). An intracellular form of cathepsin B contributes to invasiveness in cancer. Cancer Res. 61, 3493-3500.
    • (2001) Cancer Res , vol.61 , pp. 3493-3500
    • Szpaderska, A.M.1    Frankfater, A.2
  • 113
    • 22144493871 scopus 로고    scopus 로고
    • G1P3, an interferon inducible gene 6-16, is expressed in gastric cancers and inhibits mitochondrialmediated apoptosis in gastric cancer cell line TMK-1 cell
    • Tahara, E. Jr., Tahara, H., Kanno, M., Naka, K., Takeda, Y., Matsuzaki, T., Yamazaki, R., Ishihara, H., Yasui, W., Barrett, J.C., et al. (2005). G1P3, an interferon inducible gene 6-16, is expressed in gastric cancers and inhibits mitochondrialmediated apoptosis in gastric cancer cell line TMK-1 cell. Cancer Immunol. Immunother. 54, 729-740.
    • (2005) Cancer Immunol. Immunother , vol.54 , pp. 729-740
    • Tahara Jr., E.1    Tahara, H.2    Kanno, M.3    Naka, K.4    Takeda, Y.5    Matsuzaki, T.6    Yamazaki, R.7    Ishihara, H.8    Yasui, W.9    Barrett, J.C.10
  • 114
    • 0034502852 scopus 로고    scopus 로고
    • Cathepsin K in thyroid epithelial cells: Sequence, localization and possible function in extracellular proteolysis of thyroglobulin
    • Tepel, C., Bromme, D., Herzog, V., and Brix, K. (2000). Cathepsin K in thyroid epithelial cells: sequence, localization and possible function in extracellular proteolysis of thyroglobulin. J. Cell Sci. 113, 4487-4498.
    • (2000) J. Cell Sci , vol.113 , pp. 4487-4498
    • Tepel, C.1    Bromme, D.2    Herzog, V.3    Brix, K.4
  • 116
    • 1842581507 scopus 로고    scopus 로고
    • The role of cathepsin K in normal bone resorption
    • Troen, B.R. (2004). The role of cathepsin K in normal bone resorption. Drug News Perspect. 17, 19-28.
    • (2004) Drug News Perspect , vol.17 , pp. 19-28
    • Troen, B.R.1
  • 117
    • 33744771928 scopus 로고    scopus 로고
    • The regulation of cathepsin K gene expression
    • Troen, B.R. (2006). The regulation of cathepsin K gene expression. Ann. NY Acad. Sci. 1068, 165-172.
    • (2006) Ann. NY Acad. Sci , vol.1068 , pp. 165-172
    • Troen, B.R.1
  • 118
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk, V., Turk, B., and Turk, D. (2001). Lysosomal cysteine proteases: facts and opportunities. EMBO J. 20, 4629-4633.
    • (2001) EMBO J , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 120
    • 33947604810 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, 385-401.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 385-401
    • Vasiljeva, O.1    Reinheckel, T.2    Peters, C.3    Turk, D.4    Turk, V.5    Turk, B.6
  • 122
    • 0032572579 scopus 로고    scopus 로고
    • Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme
    • Vollenweider, F., Kappeler, F., Itin, C., and Hauri, H.P. (1998). Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme. J. Cell Biol. 142, 377-389.
    • (1998) J. Cell Biol , vol.142 , pp. 377-389
    • Vollenweider, F.1    Kappeler, F.2    Itin, C.3    Hauri, H.P.4
  • 123
    • 33646827205 scopus 로고    scopus 로고
    • Cathepsin S controls angiogenesis and tumor growth via matrix-derived angiogenic factors
    • Wang, B., Sun, J., Kitamoto, S., Yang, M., Grubb, A., Chapman, H.A., Kalluri, R., and Shi, G.P. (2006). Cathepsin S controls angiogenesis and tumor growth via matrix-derived angiogenic factors. J. Biol. Chem. 281, 6020-6029.
    • (2006) J. Biol. Chem , vol.281 , pp. 6020-6029
    • Wang, B.1    Sun, J.2    Kitamoto, S.3    Yang, M.4    Grubb, A.5    Chapman, H.A.6    Kalluri, R.7    Shi, G.P.8
  • 125
    • 0035881830 scopus 로고    scopus 로고
    • Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum
    • Wex, T., Buhling, F., Wex, H., Gunther, D., Malfertheiner, P., Weber, E., and Bromme, D. (2001). Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum. J. Immunol. 167, 2172-2178.
    • (2001) J. Immunol , vol.167 , pp. 2172-2178
    • Wex, T.1    Buhling, F.2    Wex, H.3    Gunther, D.4    Malfertheiner, P.5    Weber, E.6    Bromme, D.7
  • 127
    • 4344670363 scopus 로고    scopus 로고
    • Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
    • Yasuda, Y., Li, Z., Greenbaum, D., Bogyo, M., Weber, E., and Bromme, D. (2004). Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J. Biol. Chem. 279, 36761-36770.
    • (2004) J. Biol. Chem , vol.279 , pp. 36761-36770
    • Yasuda, Y.1    Li, Z.2    Greenbaum, D.3    Bogyo, M.4    Weber, E.5    Bromme, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.