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Volumn 19, Issue 6, 2000, Pages 1187-1194

Secreted cathepsin L generates endostatin from collagen XVIII

Author keywords

Cathepsin L; Collagen XVIII; Endostatin; LHVS; Metalloproteases

Indexed keywords

CATHEPSIN L; COLLAGEN; COLLAGEN XVIII; ENDOSTATIN; METALLOPROTEINASE; UNCLASSIFIED DRUG;

EID: 0034653421     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.6.1187     Document Type: Article
Times cited : (421)

References (41)
  • 1
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments
    • Aimes, R.T. and Quigley, J.P. (1995) Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. J. Biol. Chem., 270, 5872-5876.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 2
    • 0010712792 scopus 로고    scopus 로고
    • Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity
    • Brooks, P.C., Silletti, S., von Schalscha, T.L., Friedlander, M. and Cheresh, D.A. (1998) Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity. Cell, 92, 391-400.
    • (1998) Cell , vol.92 , pp. 391-400
    • Brooks, P.C.1    Silletti, S.2    Von Schalscha, T.L.3    Friedlander, M.4    Cheresh, D.A.5
  • 3
    • 0000456939 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors
    • Teicher, B.A. (ed.). Human Press, Totowa, NJ
    • Brown, P.D. and Whittaker, M. (1999) Matrix metalloproteinase inhibitors. In Teicher, B.A. (ed.), Antiangiogenic Agents in Cancer Therapy. Human Press, Totowa, NJ, pp. 205-223.
    • (1999) Antiangiogenic Agents in Cancer Therapy , pp. 205-223
    • Brown, P.D.1    Whittaker, M.2
  • 4
    • 0027236943 scopus 로고
    • The 16-kilodalton N-terminal fragment of human prolactin is a potent inhibitor of angiogenesis
    • Clapp, C., Martial, J.A., Guzman, R.C., Rentier-Delrue, F. and Weiner, R.I. (1993) The 16-kilodalton N-terminal fragment of human prolactin is a potent inhibitor of angiogenesis. Endocrinology, 133, 1292-1299.
    • (1993) Endocrinology , vol.133 , pp. 1292-1299
    • Clapp, C.1    Martial, J.A.2    Guzman, R.C.3    Rentier-Delrue, F.4    Weiner, R.I.5
  • 5
    • 0025772668 scopus 로고
    • Collagenolytic cysteine proteinases of bone tissue. Cathepsin B, (pro)cathepsin L and a cathepsin L-like 70 kDa proteinase
    • Delaissé, J.M., Ledern, P. and Vaes, G. (1991) Collagenolytic cysteine proteinases of bone tissue. Cathepsin B, (pro)cathepsin L and a cathepsin L-like 70 kDa proteinase. Biochem. J., 279, 167-174.
    • (1991) Biochem. J. , vol.279 , pp. 167-174
    • Delaissé, J.M.1    Ledern, P.2    Vaes, G.3
  • 6
    • 0030998660 scopus 로고    scopus 로고
    • Macrophage-derived metalloelastase is responsible for the generation of angiostatin in Lewis lung carcinoma
    • Dong, Z., Kumar, R., Yang, X. and Fidler, I.J. (1997) Macrophage-derived metalloelastase is responsible for the generation of angiostatin in Lewis lung carcinoma. Cell, 88, 801-810.
    • (1997) Cell , vol.88 , pp. 801-810
    • Dong, Z.1    Kumar, R.2    Yang, X.3    Fidler, I.J.4
  • 9
    • 0028465482 scopus 로고
    • 31P-MRS measurements of extracellular pH of tumors using 3-aminopropylphosphonate
    • 31P-MRS measurements of extracellular pH of tumors using 3-aminopropylphosphonate. Am. J. Physiol., 267, C195-C203.
    • (1994) Am. J. Physiol. , vol.267
    • Gillies, R.J.1    Liu, Z.2    Bhujwalla, Z.3
  • 10
    • 0029098320 scopus 로고
    • A potent inhibitor of endothelial cell proliferation is generated by proteolytic cleavage of the chemokine platelet factor 4
    • Gupta, S.K., Hassel, T. and Singh, J.P. (1995) A potent inhibitor of endothelial cell proliferation is generated by proteolytic cleavage of the chemokine platelet factor 4. Proc. Natl Acad. Sci. USA, 92, 7799-7803.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7799-7803
    • Gupta, S.K.1    Hassel, T.2    Singh, J.P.3
  • 11
    • 0032566501 scopus 로고    scopus 로고
    • Collagen XVIII is a basement membrane heparan sulfate proteoglycan
    • Halfter, W., Dong, S., Schurer, B. and Cole, G.J. (1998) Collagen XVIII is a basement membrane heparan sulfate proteoglycan. J. Biol. Chem., 273, 25404-25412.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25404-25412
    • Halfter, W.1    Dong, S.2    Schurer, B.3    Cole, G.J.4
  • 12
    • 0015076928 scopus 로고
    • Hemangioma with thrombocytopenia and microangiopathic anemia (Kasabach-Merritt syndrome): An animal model
    • Hoak, J.C., Warner, E.D., Cheng, H.F., Fry, G.L. and Hankenson, R.R. (1971) Hemangioma with thrombocytopenia and microangiopathic anemia (Kasabach-Merritt syndrome): an animal model. J. Lab. Clin. Med., 77, 941-950.
    • (1971) J. Lab. Clin. Med. , vol.77 , pp. 941-950
    • Hoak, J.C.1    Warner, E.D.2    Cheng, H.F.3    Fry, G.L.4    Hankenson, R.R.5
  • 13
    • 0022252997 scopus 로고
    • Heparin-binding fragments of fibronectin are potent inhibitors of endothelial cell growth
    • Homandberg, G.A., Williams, J.E., Grant, D., Schumacher, B. and Eisenstein, R. (1985) Heparin-binding fragments of fibronectin are potent inhibitors of endothelial cell growth. Am. J. Pathol., 120, 327-332.
    • (1985) Am. J. Pathol. , vol.120 , pp. 327-332
    • Homandberg, G.A.1    Williams, J.E.2    Grant, D.3    Schumacher, B.4    Eisenstein, R.5
  • 14
    • 0032030785 scopus 로고    scopus 로고
    • Cleavage of native type I collagen by human neutrophil elastase
    • Kafienah, W., Buttle, D.J., Burnett, D. and Hollander, A.P. (1998) Cleavage of native type I collagen by human neutrophil elastase. Biochem. J., 330, 897-902.
    • (1998) Biochem. J. , vol.330 , pp. 897-902
    • Kafienah, W.1    Buttle, D.J.2    Burnett, D.3    Hollander, A.P.4
  • 15
    • 0002832738 scopus 로고    scopus 로고
    • Cathepsin L.
    • Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (eds). Academic Press, San Diego, CA
    • Kirschke, H. (1998) Cathepsin L. In Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (eds), Handbook of Proteolytic Enzymes. Academic Press, San Diego, CA, pp. 617-621.
    • (1998) Handbook of Proteolytic Enzymes , pp. 617-621
    • Kirschke, H.1
  • 16
    • 0030804282 scopus 로고    scopus 로고
    • Properties of the extracellular calcium binding module of the proteoglycan testican
    • Kohfeldt, E., Maurer, P., Vannahme, C. and Timpl, R. (1997) Properties of the extracellular calcium binding module of the proteoglycan testican. FEBS Lett., 414, 557-561.
    • (1997) FEBS Lett. , vol.414 , pp. 557-561
    • Kohfeldt, E.1    Maurer, P.2    Vannahme, C.3    Timpl, R.4
  • 17
    • 0031774869 scopus 로고    scopus 로고
    • Inhibition of tumor cell invasion by protease inhibitors: Correlation with the protease profile
    • Kolkhorst, V., Stürzebecher, J. and Wiederanders, B. (1998) Inhibition of tumor cell invasion by protease inhibitors: correlation with the protease profile. J. Cancer Res. Clin. Oncol., 124, 598-606.
    • (1998) J. Cancer Res. Clin. Oncol. , vol.124 , pp. 598-606
    • Kolkhorst, V.1    Stürzebecher, J.2    Wiederanders, B.3
  • 18
    • 0031685364 scopus 로고    scopus 로고
    • Cysteine proteinases and their endogenous inhibitors: Target proteins for prognosis, diagnosis and therapy in cancer
    • Kos, J. and Lah, T.T. (1998) Cysteine proteinases and their endogenous inhibitors: target proteins for prognosis, diagnosis and therapy in cancer. Oncol. Rep., 5, 1349-1361.
    • (1998) Oncol. Rep. , vol.5 , pp. 1349-1361
    • Kos, J.1    Lah, T.T.2
  • 19
    • 0026027556 scopus 로고
    • Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation
    • Liotta, L.A., Steeg, P.S. and Stetler-Stevenson, W.G. (1991) Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation. Cell, 64, 327-336.
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.A.1    Steeg, P.S.2    Stetler-Stevenson, W.G.3
  • 20
    • 0024263314 scopus 로고
    • A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen
    • Maciewicz, R.A. and Etherington, D.J. (1988) A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen. Biochem. J., 256, 433-440.
    • (1988) Biochem. J. , vol.256 , pp. 433-440
    • Maciewicz, R.A.1    Etherington, D.J.2
  • 21
    • 0033574733 scopus 로고    scopus 로고
    • Angiostatin's partners
    • Martínez-Zaguilán, R. (1999) Angiostatin's partners. Science, 284, 433-434.
    • (1999) Science , vol.284 , pp. 433-434
    • Martínez-Zaguilán, R.1
  • 23
    • 0023462882 scopus 로고
    • The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L.
    • Mason, R.W., Gal, S. and Gottesman, M.M. (1987) The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L. Biochem. J., 248, 449-454.
    • (1987) Biochem. J. , vol.248 , pp. 449-454
    • Mason, R.W.1    Gal, S.2    Gottesman, M.M.3
  • 24
    • 0032850748 scopus 로고    scopus 로고
    • Angiogenesis inhibitor endostatin is a distinct component of elastic fibers in vessel walls
    • Miosge, N., Sasaki, T. and Timpl, R. (1999) Angiogenesis inhibitor endostatin is a distinct component of elastic fibers in vessel walls. FASEB J., 13, 1743-1750.
    • (1999) FASEB J. , vol.13 , pp. 1743-1750
    • Miosge, N.1    Sasaki, T.2    Timpl, R.3
  • 26
    • 0031002846 scopus 로고    scopus 로고
    • Regulation of vascular morphogenesis by the matricellular protein SPARC
    • Motamed, K. and Sage, E.H. (1997) Regulation of vascular morphogenesis by the matricellular protein SPARC. Kidney Int., 51, 1383-1387.
    • (1997) Kidney Int. , vol.51 , pp. 1383-1387
    • Motamed, K.1    Sage, E.H.2
  • 27
    • 0028981205 scopus 로고
    • Mouse Col18a1 is expressed in a tissue-specific manner as three alternative variants and is localized in basement membrane zones
    • Muragaki, Y., Timmons, S., Griffith, C.M., Oh, S.P., Fadel, B., Quertermous, T. and Olsen, B.R. (1995) Mouse Col18a1 is expressed in a tissue-specific manner as three alternative variants and is localized in basement membrane zones. Proc. Natl Acad. Sci. USA, 92, 8763-8767.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8763-8767
    • Muragaki, Y.1    Timmons, S.2    Griffith, C.M.3    Oh, S.P.4    Fadel, B.5    Quertermous, T.6    Olsen, B.R.7
  • 28
    • 0027970092 scopus 로고
    • Angiostatin: A novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma
    • O'Reilly, M.S. et al. (1994) Angiostatin: a novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma. Cell, 79, 315-328.
    • (1994) Cell , vol.79 , pp. 315-328
    • O'Reilly, M.S.1
  • 29
    • 0031454617 scopus 로고    scopus 로고
    • Endostatin: An endogenous inhibitor of angiogenesis and tumor growth
    • O'Reilly, M.S. et al. (1997) Endostatin: an endogenous inhibitor of angiogenesis and tumor growth. Cell, 88, 277-285.
    • (1997) Cell , vol.88 , pp. 277-285
    • O'Reilly, M.S.1
  • 30
    • 0033578910 scopus 로고    scopus 로고
    • Antiangiogenic activity of the cleaved conformation of the serpin antithrombin
    • O'Reilly, M.S., Pirie-Shepherd, S., Lane, W.S. and Folkman, J. (1999) Antiangiogenic activity of the cleaved conformation of the serpin antithrombin. Science, 285, 1926-1928.
    • (1999) Science , vol.285 , pp. 1926-1928
    • O'Reilly, M.S.1    Pirie-Shepherd, S.2    Lane, W.S.3    Folkman, J.4
  • 31
    • 0025171645 scopus 로고
    • A hemangioendothelioma-derived cell line: Its use as a model for the study of endothelial cell biology
    • Obeso, J., Weber, J. and Auerbach, R. (1990) A hemangioendothelioma-derived cell line: its use as a model for the study of endothelial cell biology. Lab. Invest., 63, 259-269.
    • (1990) Lab. Invest. , vol.63 , pp. 259-269
    • Obeso, J.1    Weber, J.2    Auerbach, R.3
  • 32
    • 0001033082 scopus 로고
    • Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-X-Y repeats identify a novel family of collagenous proteins
    • Oh, S.P., Kamagata, Y., Muragaki, Y., Timmons, S., Ooshima, A. and Olsen, B.R. (1994) Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-X-Y repeats identify a novel family of collagenous proteins. Proc. Natl Acad. Sci. USA, 91, 4229-4233.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4229-4233
    • Oh, S.P.1    Kamagata, Y.2    Muragaki, Y.3    Timmons, S.4    Ooshima, A.5    Olsen, B.R.6
  • 33
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • Palmer, J.T., Rasnick, D., Klaus, J.L. and Bromme, D. (1995) Vinyl sulfones as mechanism-based cysteine protease inhibitors. J. Med. Chem., 38, 3193-3196.
    • (1995) J. Med. Chem. , vol.38 , pp. 3193-3196
    • Palmer, J.T.1    Rasnick, D.2    Klaus, J.L.3    Bromme, D.4
  • 34
    • 0028176183 scopus 로고
    • α1 (XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution and homology with type XV collagen
    • Rehn, M. and Pihlajaniemi, T. (1994) α1 (XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution and homology with type XV collagen. Proc. Natl Acad. Sci. USA, 91, 4234-4238.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4234-4238
    • Rehn, M.1    Pihlajaniemi, T.2
  • 35
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • Riese, R.J., Wolf, P.R., Brömme, D., Natkin, L.R., Villadangos, J.A., Ploegh, H.L. and Chapman, H.A. (1996) Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity, 4, 357-366.
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Brömme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6    Chapman, H.A.7
  • 36
    • 0031830711 scopus 로고    scopus 로고
    • The short and long forms of type XVIII collagen show clear tissue specificities in their expression and location in basement membrane zones in humans
    • Saarela, J., Rehn, M., Oikarinen, A., Autio-Harmainen, H. and Pihlajaniemi, T. (1998) The short and long forms of type XVIII collagen show clear tissue specificities in their expression and location in basement membrane zones in humans. Am. J. Pathol., 153, 611-626.
    • (1998) Am. J. Pathol. , vol.153 , pp. 611-626
    • Saarela, J.1    Rehn, M.2    Oikarinen, A.3    Autio-Harmainen, H.4    Pihlajaniemi, T.5
  • 37
    • 0032479999 scopus 로고    scopus 로고
    • Structure, function and tissue forms of the C-terminal globular domain of collagen XVIII containing the angiogenesis inhibitor endostatin
    • Sasaki, T., Fukai, N., Mann, K., Göhring, W., Olsen, B.R. and Timpl, R. (1998) Structure, function and tissue forms of the C-terminal globular domain of collagen XVIII containing the angiogenesis inhibitor endostatin. EMBO J., 17, 4249-4256.
    • (1998) EMBO J. , vol.17 , pp. 4249-4256
    • Sasaki, T.1    Fukai, N.2    Mann, K.3    Göhring, W.4    Olsen, B.R.5    Timpl, R.6
  • 39
    • 0017574530 scopus 로고
    • The effect of human neutrophil elastase and cathepsin g on the collagen of cartilage, tendon and cornea
    • Starkey, P.M. (1977) The effect of human neutrophil elastase and cathepsin G on the collagen of cartilage, tendon and cornea. Acta Biol. Med. Ger., 36, 1549-1554.
    • (1977) Acta Biol. Med. Ger. , vol.36 , pp. 1549-1554
    • Starkey, P.M.1
  • 41
    • 0033575658 scopus 로고    scopus 로고
    • Endos tatin inhibits VEGF-induced endothelial cell migration and tumor growth independently of zinc binding
    • Yamaguchi, N. et al. (1999) Endos tatin inhibits VEGF-induced endothelial cell migration and tumor growth independently of zinc binding. EMBO J., 18, 4414-4423.
    • (1999) EMBO J. , vol.18 , pp. 4414-4423
    • Yamaguchi, N.1


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