메뉴 건너뛰기




Volumn 58, Issue 14, 1998, Pages 2957-2960

Tissue inhibitor of metalloproteinase-2 protection of matrix metalloproteinase-2 from degradation by plasmin is reversed by divalent cation chelator EDTA and the bisphosphonate alendronate

Author keywords

[No Author keywords available]

Indexed keywords

ALENDRONIC ACID; CHELATING AGENT; EDETIC ACID; GELATINASE A; PLASMIN; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 0032527618     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (25)

References (20)
  • 1
    • 0027223141 scopus 로고
    • Regulation of matrix metalloproteinases: Their role in tumour invasion and metastasis
    • Cottam, D. W., and Rees, R. C. Regulation of matrix metalloproteinases: their role in tumour invasion and metastasis. Int. J. Oncol., 2: 861-872, 1993.
    • (1993) Int. J. Oncol. , vol.2 , pp. 861-872
    • Cottam, D.W.1    Rees, R.C.2
  • 2
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumour invasion
    • Mignatti, P., and Rifkin, D. B. Biology and biochemistry of proteinases in tumour invasion. Physiol. Rev., 73: 161-195, 1993.
    • (1993) Physiol. Rev. , vol.73 , pp. 161-195
    • Mignatti, P.1    Rifkin, D.B.2
  • 3
    • 0023919959 scopus 로고
    • H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloproteinase capable of degrading basement membrane collagen
    • Collier, I. E., Wilhelm, S. M., Eisen, A. Z., Manner, B. L., Grant, G. A., Seltzer, J. L., Kornberger, A., He, C., Bauer, E. A., and Goldberg, G. I. H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloproteinase capable of degrading basement membrane collagen. J. Biol. Chem., 263: 6579-6587, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6579-6587
    • Collier, I.E.1    Wilhelm, S.M.2    Eisen, A.Z.3    Manner, B.L.4    Grant, G.A.5    Seltzer, J.L.6    Kornberger, A.7    He, C.8    Bauer, E.A.9    Goldberg, G.I.10
  • 4
    • 0025651681 scopus 로고
    • Studies on the ability of 65-kDa and 92-kDa tumour cell gelatinases to degrade type IV collagen
    • Mackay, A. R., Hartzler, J. L., Pelina, M. D., and Thorgeirsson, U. P. Studies on the ability of 65-kDa and 92-kDa tumour cell gelatinases to degrade type IV collagen. J. Biol. Chem., 265: 21929-21934, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21929-21934
    • Mackay, A.R.1    Hartzler, J.L.2    Pelina, M.D.3    Thorgeirsson, U.P.4
  • 5
    • 0024394212 scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP-2): A new member of the metalloproteinase inhibitor family
    • Stetler-Stevenson, W. G., Krutzsch, H. C., and Liotta, L. A. Tissue inhibitor of metalloproteinase (TIMP-2): a new member of the metalloproteinase inhibitor family. J. Biol. Chem., 264: 17374-17387, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17374-17387
    • Stetler-Stevenson, W.G.1    Krutzsch, H.C.2    Liotta, L.A.3
  • 6
    • 0026521973 scopus 로고
    • The C-terminal domain of 72-kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases
    • Murphy, G., Willenbrook, F., Ward, R, V., Cockett, M. I., Eaton, D., and Docherty, A. J. P. The C-terminal domain of 72-kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases. Biochem. J., 283: 637-641, 1992.
    • (1992) Biochem. J. , vol.283 , pp. 637-641
    • Murphy, G.1    Willenbrook, F.2    Ward, R.V.3    Cockett, M.I.4    Eaton, D.5    Docherty, A.J.P.6
  • 7
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase, H. Activation mechanisms of matrix metalloproteinases. Biol. Chem., 378: 151-160, 1997.
    • (1997) Biol. Chem. , vol.378 , pp. 151-160
    • Nagase, H.1
  • 9
    • 0027014773 scopus 로고
    • Activation mechanisms of the precursor of matrix metalloproteinases 1, 2 and 3
    • Nagase, H., Suzuki, K., Morodomi, T., Enghild, J. J., and Salvensen, G. Activation mechanisms of the precursor of matrix metalloproteinases 1, 2 and 3. Matrix Suppl., 1: 237-244, 1991.
    • (1991) Matrix Suppl. , vol.1 , pp. 237-244
    • Nagase, H.1    Suzuki, K.2    Morodomi, T.3    Enghild, J.J.4    Salvensen, G.5
  • 10
    • 0030977009 scopus 로고    scopus 로고
    • Control of type IV collagenase activity by components of the urokinase-plasmin system: A regulatory mechanism with cell bound reactants
    • Mazzieri, R., Masiero, L., Zanetta, L., Monea, S., Onisto, M., Garbisa, S., and Mignatti, P. Control of type IV collagenase activity by components of the urokinase-plasmin system: a regulatory mechanism with cell bound reactants. EMBO J., 9: 2319-2332, 1997.
    • (1997) EMBO J. , vol.9 , pp. 2319-2332
    • Mazzieri, R.1    Masiero, L.2    Zanetta, L.3    Monea, S.4    Onisto, M.5    Garbisa, S.6    Mignatti, P.7
  • 11
    • 0031588367 scopus 로고    scopus 로고
    • Retinoic acid-enhanced invasion through reconstituted basement membrane by human SK-N-SH neuroblastoma cells involves membrane-associated tissue-type plasminogen activator
    • Tiberio, A., Farina, A. R., Tacconelli, A., Cappabianca, L., Gulino, A., and Mackay, A. R. Retinoic acid-enhanced invasion through reconstituted basement membrane by human SK-N-SH neuroblastoma cells involves membrane-associated tissue-type plasminogen activator. Int. J. Cancer, 73: 740-748, 1997.
    • (1997) Int. J. Cancer , vol.73 , pp. 740-748
    • Tiberio, A.1    Farina, A.R.2    Tacconelli, A.3    Cappabianca, L.4    Gulino, A.5    Mackay, A.R.6
  • 12
    • 0027076118 scopus 로고
    • Effect of phorbol ester and cytokines on matrix metalloproteinase and tissue inhibitor of metalloproteinase expression in tumour and normal cell lines
    • Mackay, A. R., Ballin, M., Pelina, M. D., Farina, A. R., Nason, A. M., Hartzler, J. L., and Thorgeirsson, U. P. Effect of phorbol ester and cytokines on matrix metalloproteinase and tissue inhibitor of metalloproteinase expression in tumour and normal cell lines. Invasion Metastasis, 12: 168-184, 1992.
    • (1992) Invasion Metastasis , vol.12 , pp. 168-184
    • Mackay, A.R.1    Ballin, M.2    Pelina, M.D.3    Farina, A.R.4    Nason, A.M.5    Hartzler, J.L.6    Thorgeirsson, U.P.7
  • 13
    • 0026318521 scopus 로고
    • Bisphosphonates. Pharmacology and use in treatment of tumour induced hypercalcaemic and metastatic bone diseases
    • Fleisch, H. Bisphosphonates. Pharmacology and use in treatment of tumour induced hypercalcaemic and metastatic bone diseases. Drugs, 42: 919-944, 1991.
    • (1991) Drugs , vol.42 , pp. 919-944
    • Fleisch, H.1
  • 14
    • 0026320852 scopus 로고
    • Bisphosphonate action. Alendronate localisation in rat bone and effects on osteoclast ultrastructure
    • Sato, M., Grasser, W., Endo, N., Akins, R., Simmons, H., Thompson, D. D., Golub, E., and Rodan, G. A. Bisphosphonate action. Alendronate localisation in rat bone and effects on osteoclast ultrastructure. J. Clin. Invest., 88: 2095-2105, 1991.
    • (1991) J. Clin. Invest. , vol.88 , pp. 2095-2105
    • Sato, M.1    Grasser, W.2    Endo, N.3    Akins, R.4    Simmons, H.5    Thompson, D.D.6    Golub, E.7    Rodan, G.A.8
  • 17
    • 0032479268 scopus 로고    scopus 로고
    • Activation of MMP-2 by the human osteoclast containing, giant cell tumor line, GCT23, by osteopontin, bone sialoprotein and GRGDSP peptide is RGD and cell shape change dependent
    • in press
    • Teti, A., Farina, A. R., Villanova, I., Tacconelli, A., Sciortino, G., Chambers, A. F., Gulino, A., and Mackay, A. R. Activation of MMP-2 by the human osteoclast containing, giant cell tumor line, GCT23, by osteopontin, bone sialoprotein and GRGDSP peptide is RGD and cell shape change dependent. Int. J. Cancer, in press, 1998.
    • (1998) Int. J. Cancer
    • Teti, A.1    Farina, A.R.2    Villanova, I.3    Tacconelli, A.4    Sciortino, G.5    Chambers, A.F.6    Gulino, A.7    Mackay, A.R.8
  • 18
    • 0029965059 scopus 로고    scopus 로고
    • High levels of tissue inhibitor of metalloproteinase-2 (TIMP-2) expression are associated with poor outcome in invasive bladder cancer
    • Grignon, D. J., Sakr, W. S., Toth, M., Ravery, V., Angulo, J., Shamsa, F., Pontes, J. E., Crissman, J. C., and Fridman, R. High levels of tissue inhibitor of metalloproteinase-2 (TIMP-2) expression are associated with poor outcome in invasive bladder cancer. Cancer Res., 56: 1654-1659, 1996.
    • (1996) Cancer Res. , vol.56 , pp. 1654-1659
    • Grignon, D.J.1    Sakr, W.S.2    Toth, M.3    Ravery, V.4    Angulo, J.5    Shamsa, F.6    Pontes, J.E.7    Crissman, J.C.8    Fridman, R.9
  • 19
    • 0010457672 scopus 로고
    • Enhanced expression of tissue inhibitor of metalloproteinases 2 (TIMP-2) in the stroma of breast carcinomas correlates with tumour recurrence
    • Visscher, D. W., Hoyhtya, M., Ottosen, S. K., Liang, C. M., Sarkar, F. H., Crissman, J. D., and Fridman, R. Enhanced expression of tissue inhibitor of metalloproteinases 2 (TIMP-2) in the stroma of breast carcinomas correlates with tumour recurrence. Int. J. Cancer, 58: 1-6, 1994.
    • (1994) Int. J. Cancer , vol.58 , pp. 1-6
    • Visscher, D.W.1    Hoyhtya, M.2    Ottosen, S.K.3    Liang, C.M.4    Sarkar, F.H.5    Crissman, J.D.6    Fridman, R.7
  • 20
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloproteinase
    • Stongin, A. Y., Collier, I., Bannikov, G., Marmer, B. L., Grant, G. A., and Goldberg, G. I. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloproteinase. J. Biol. Chem., 270: 5331-5338, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5331-5338
    • Stongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.