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Volumn 425, Issue , 1997, Pages 89-97

Proteases and protease inhibitors in tumor progression

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGENASE; CYTOSTATIC AGENT; GELATINASE A; GELATINASE B; MATRILYSIN; MATRIX METALLOPROTEINASE; PLASMIN; PLASMINOGEN ACTIVATOR; PLASMINOGEN ACTIVATOR INHIBITOR 2; PROTEINASE; PROTEINASE INHIBITOR; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 0031470482     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-5391-5_9     Document Type: Article
Times cited : (117)

References (27)
  • 1
    • 0019195010 scopus 로고
    • Metastatic potential correlates with enzymatic degradation of basement membrane collagen
    • Liotta LA, Tryggvason K, Garbisa S, Hart I, Foltz CM, Shafie S (1980) Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature 284: 67-68.
    • (1980) Nature , vol.284 , pp. 67-68
    • Liotta, L.A.1    Tryggvason, K.2    Garbisa, S.3    Hart, I.4    Foltz, C.M.5    Shafie, S.6
  • 3
    • 0025413394 scopus 로고
    • Cathepsin B and cystatins: Evidence for a role in cancer progression
    • Sloane BF (1990) Cathepsin B and cystatins: evidence for a role in cancer progression. Semin Cancer Biol 1: 137-152.
    • (1990) Semin Cancer Biol , vol.1 , pp. 137-152
    • Sloane, B.F.1
  • 6
    • 0026559860 scopus 로고
    • Increased expression of cathepsins L and B and decreased activity of their inhibitors in metastatic, ras-rransformed NIH 3T3 cells
    • Chambers AF, Colella R, Denhardt DT, Wilson SM (1992) Increased expression of cathepsins L and B and decreased activity of their inhibitors in metastatic, ras-rransformed NIH 3T3 cells. Mol Carcinog 5: 238-245.
    • (1992) Mol Carcinog , vol.5 , pp. 238-245
    • Chambers, A.F.1    Colella, R.2    Denhardt, D.T.3    Wilson, S.M.4
  • 8
    • 0027787819 scopus 로고
    • Cathepsin-D in human breast cancer: Correlation with vascular invasion and other clinical and histopathological characteristics
    • Hahnel R, Harvey J, Robbins P, Sterrett G (1993) Cathepsin-D in human breast cancer: correlation with vascular invasion and other clinical and histopathological characteristics. Anticancer Res 13:2131-2135.
    • (1993) Anticancer Res , vol.13 , pp. 2131-2135
    • Hahnel, R.1    Harvey, J.2    Robbins, P.3    Sterrett, G.4
  • 9
  • 11
    • 0023784140 scopus 로고
    • In vitro degradation of extracellular matrix with Mr 52,000 cathepsin D secreted by breast cancer cells
    • Briozzo P, Morisset M, Capony F, Rougeot C, Rochefort H (1988) In vitro degradation of extracellular matrix with Mr 52,000 cathepsin D secreted by breast cancer cells. Cancer Res 48: 3688-3692.
    • (1988) Cancer Res , vol.48 , pp. 3688-3692
    • Briozzo, P.1    Morisset, M.2    Capony, F.3    Rougeot, C.4    Rochefort, H.5
  • 12
    • 0027015335 scopus 로고
    • Physiological mechanisms for metalloproteinase activation
    • Murphy G, Ward R, Gavrilovic J, Atkinson S (1992) Physiological mechanisms for metalloproteinase activation. Matrix Suppl 1: 224-230.
    • (1992) Matrix Suppl , vol.1 , pp. 224-230
    • Murphy, G.1    Ward, R.2    Gavrilovic, J.3    Atkinson, S.4
  • 13
    • 0027179188 scopus 로고
    • Effects of membrane-associated cathepsin B on the activation of receptor-bound prourokinase and subsequent invasion of reconstituted basement membranes
    • Kobayashi H, Moniwa N, Sugimura M, Shinohara H, Ohi H, Terao T (1993) Effects of membrane-associated cathepsin B on the activation of receptor-bound prourokinase and subsequent invasion of reconstituted basement membranes. Biochim Biophys Acta 1178: 55-62.
    • (1993) Biochim Biophys Acta , vol.1178 , pp. 55-62
    • Kobayashi, H.1    Moniwa, N.2    Sugimura, M.3    Shinohara, H.4    Ohi, H.5    Terao, T.6
  • 14
    • 0027499073 scopus 로고
    • Melanoma-mediated dissolution of extracellular matrix: Contribution of urokinase-dependent and metalloproteinase-dependent proteolytic pathways
    • Montgomery AM, DeClerck YA, Langley KE, Reisfeld RA, Mueller BM (1993) Melanoma-mediated dissolution of extracellular matrix: contribution of urokinase-dependent and metalloproteinase-dependent proteolytic pathways. Cancer Res 53: 693-700.
    • (1993) Cancer Res , vol.53 , pp. 693-700
    • Montgomery, A.M.1    DeClerck, Y.A.2    Langley, K.E.3    Reisfeld, R.A.4    Mueller, B.M.5
  • 15
    • 0028794828 scopus 로고
    • Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II
    • Suzuki K, Lees M, Newlands GFJ, Nagase H, Woolley DE (1995) Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II. Biochem J 305: 301-306.
    • (1995) Biochem J , vol.305 , pp. 301-306
    • Suzuki, K.1    Lees, M.2    Gfj, N.3    Nagase, H.4    De Woolley5
  • 16
    • 0028767542 scopus 로고
    • Tumour biology. Membrane proteases in focus [news; comment]
    • Vassalli JD, Pepper MS (1994) Tumour biology. Membrane proteases in focus [news; comment]. Nature 370: 14-15.
    • (1994) Nature , vol.370 , pp. 14-15
    • Vassalli, J.D.1    Pepper, M.S.2
  • 17
    • 0029885707 scopus 로고    scopus 로고
    • Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase a and express intrinsic matrix-degrading activity
    • Pei D, Weiss SJ (1996) Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J Biol Chem 271: 9135-9140.
    • (1996) J Biol Chem , vol.271 , pp. 9135-9140
    • Pei, D.1    Weiss, S.J.2
  • 18
    • 0029962937 scopus 로고    scopus 로고
    • Independent regulation of matrix metalloproteinases and plasminogen activators in human fibrosarcoma cells
    • Lim YT, Sugiura Y, Laug WE, Sun B, Garcia A, DeClerck YA (1996) Independent regulation of matrix metalloproteinases and plasminogen activators in human fibrosarcoma cells. J Cell Physiol 167: 333-340.
    • (1996) J Cell Physiol , vol.167 , pp. 333-340
    • Lim, Y.T.1    Sugiura, Y.2    Laug, W.E.3    Sun, B.4    Garcia, A.5    DeClerck, Y.A.6
  • 19
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei D, Weiss SJ (1995) Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 375: 244-247.
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 20
    • 0027459149 scopus 로고
    • Characterization of the functional domain of tissue inhibitor of metalloproteinases-2 (TIMP-2)
    • DeClerck YA, Yean TD, Lee Y, Tomich JM, Langley KE (1993) Characterization of the functional domain of tissue inhibitor of metalloproteinases-2 (TIMP-2). Biochem J 289: 65-69.
    • (1993) Biochem J , vol.289 , pp. 65-69
    • DeClerck, Y.A.1    Yean, T.D.2    Lee, Y.3    Tomich, J.M.4    Langley, K.E.5
  • 21
    • 0028116127 scopus 로고
    • Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3
    • Pei D, Majmudar G, Weiss SJ (1994) Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3. J Biol Chem 269: 25849-25855.
    • (1994) J Biol Chem , vol.269 , pp. 25849-25855
    • Pei, D.1    Majmudar, G.2    Weiss, S.J.3
  • 22
    • 0027435065 scopus 로고
    • Tissue inhibitor of metalloproteinases (TIMP, aka EPA): Structure, control of expression and biological functions
    • Denhardt DT, Feng B, Edwards DR, Cocuzzi ET, Malyankar UM (1993) Tissue inhibitor of metalloproteinases (TIMP, aka EPA): structure, control of expression and biological functions. Pharmacol Ther 59:329-341.
    • (1993) Pharmacol Ther , vol.59 , pp. 329-341
    • Denhardt, D.T.1    Feng, B.2    Edwards, D.R.3    Cocuzzi, E.T.4    Malyankar, U.M.5
  • 23
    • 0006506596 scopus 로고
    • Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2
    • Goldberg GI, Marner BL, Grant GA, Eisen AZ, Wilhelm S, He CS (1989) Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2. Proc Natl Acad Sci U S A 86: 8207-8211.
    • (1989) Proc Natl Acad Sci U S a , vol.86 , pp. 8207-8211
    • Goldberg, G.I.1    Marner, B.L.2    Grant, G.A.3    Eisen, A.Z.4    Wilhelm, S.5    He, C.S.6
  • 24
    • 0026630048 scopus 로고
    • Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin
    • Goldberg GI, Strongin A, Collier IE, Genrich LT, Marmer BL (1992) Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin. J Biol Chem 267: 4583-4591.
    • (1992) J Biol Chem , vol.267 , pp. 4583-4591
    • Goldberg, G.I.1    Strongin, A.2    Collier, I.E.3    Genrich, L.T.4    Marmer, B.L.5
  • 25
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase.Isolation of the activated form of the membrane metalloprotease
    • Strongin AY, Collier I, Bannikov, Marmer BL, Grant GA, Goldberg GI (1995) Mechanism of cell surface activation of 72-kDa type IV collagenase.Isolation of the activated form of the membrane metalloprotease. J Biol Chem 270: 5331-5338.
    • (1995) J Biol Chem , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 26
    • 0025809874 scopus 로고
    • Inhibition of autoproteolytic activation of interstitial procollagenase by recombinant metalloproteinase inhibitor MI/TIMP-2
    • DeClerck YA, Yean TD, Lu HS, Ting J, Langley KE (1991) Inhibition of autoproteolytic activation of interstitial procollagenase by recombinant metalloproteinase inhibitor MI/TIMP-2. J Biol Chem 266: 3893-3899.
    • (1991) J Biol Chem , vol.266 , pp. 3893-3899
    • Declerck, Y.A.1    Yean, T.D.2    Lu, H.S.3    Ting, J.4    Langley, K.E.5
  • 27
    • 0028787122 scopus 로고
    • Biological and clinical aspects of plasminogen activator inhibitor type 2
    • Kruithof EK, Baker MS, Bunn CL(1995) Biological and clinical aspects of plasminogen activator inhibitor type 2. Blood 86: 4007-4024.
    • (1995) Blood , vol.86 , pp. 4007-4024
    • Kruithof, E.K.1    Baker, M.S.2    Bunn, C.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.