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Volumn 85, Issue 10, 1999, Pages 906-911

Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding a novel vasoconstrictor

Author keywords

Endothelin; Metalloproteinase; Vasculature

Indexed keywords

ENDOTHELIN 1; GELATINASE A;

EID: 0032719798     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.85.10.906     Document Type: Article
Times cited : (337)

References (30)
  • 2
    • 0028073883 scopus 로고
    • The role of metalloproteinases and their inhibitors in tumor, metastasis, and angiogenesis
    • Ray JM, Stetler-Stevenson WG. The role of metalloproteinases and their inhibitors in tumor, metastasis, and angiogenesis. Eur Respir J. 1994;7: 2062-2072.
    • (1994) Eur Respir J. , vol.7 , pp. 2062-2072
    • Ray, J.M.1    Stetler-Stevenson, W.G.2
  • 3
    • 0029150795 scopus 로고
    • Proteolytic remodeling of extracellular matrix
    • Birkedal-Hansen H. Proteolytic remodeling of extracellular matrix. Curr Opinion Cell Biol. 1995;7:728-735.
    • (1995) Curr Opinion Cell Biol. , vol.7 , pp. 728-735
    • Birkedal-Hansen, H.1
  • 4
    • 0032916924 scopus 로고    scopus 로고
    • Increased expression of matrix metalloproteinase-2 in the thickened intima of aged rats
    • Li Z, Froehlich J, Galis ZS, Lakatta EG. Increased expression of matrix metalloproteinase-2 in the thickened intima of aged rats. HypertenSion. 1999;33:116-123.
    • (1999) Hypertension , vol.33 , pp. 116-123
    • Li, Z.1    Froehlich, J.2    Galis, Z.S.3    Lakatta, E.G.4
  • 5
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 is an interstitial collagenase: Inhibitor-free enzyme catalyzes the cleavage of type I collagen generating the specific 3/4- And 1/4-length fragments
    • Aimes RT, Quigley JP. Matrix metalloproteinase-2 is an interstitial collagenase: inhibitor-free enzyme catalyzes the cleavage of type I collagen generating the specific 3/4- and 1/4-length fragments. J Biol Chem. 1995; 270:5872-5876.
    • (1995) J Biol Chem. , vol.270 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 7
    • 0030946445 scopus 로고    scopus 로고
    • Release of gelantinase a during platelet activation mediates aggregation
    • Sawicki G, Salas E, Murat J, Miszta-Lane H, Radomski, MW. Release of gelantinase A during platelet activation mediates aggregation. Nature. 1997;386:616-619.
    • (1997) Nature , vol.386 , pp. 616-619
    • Sawicki, G.1    Salas, E.2    Murat, J.3    Miszta-Lane, H.4    Radomski, M.W.5
  • 9
    • 0028889178 scopus 로고
    • Secretion of endothelin-1 and endothelin-3 by human cultured vascular smooth muscle cells
    • Yu JC, Davenport AP. Secretion of endothelin-1 and endothelin-3 by human cultured vascular smooth muscle cells. Br J Pharmacol. 1995; 114:551-557.
    • (1995) Br J Pharmacol. , vol.114 , pp. 551-557
    • Yu, J.C.1    Davenport, A.P.2
  • 10
    • 0027992642 scopus 로고
    • ECE-1 a membrane-bound metalloprotease that catalyzes the proteolytic activition of big endothelin-1
    • Xu D, Emoto N, Giaid A, Slaughter C, Kaw S, de Wit D, Yanagisawa M. ECE-1 a membrane-bound metalloprotease that catalyzes the proteolytic activition of big endothelin-1. Cell. 1994;78:473-485.
    • (1994) Cell , vol.78 , pp. 473-485
    • Xu, D.1    Emoto, N.2    Giaid, A.3    Slaughter, C.4    Kaw, S.5    De Wit, D.6    Yanagisawa, M.7
  • 12
    • 0025975337 scopus 로고
    • Phosphoramidon blocks the pressor activity of porcine big endothelin-1 (1-39) in vivo and conversion of big endothelin-1 (1-39) to endothelin-1 (1-21) in vitro
    • McMahon EG, Palomo MA, Moore WM, McDonald JF, Stern MK. Phosphoramidon blocks the pressor activity of porcine big endothelin-1 (1-39) in vivo and conversion of big endothelin-1 (1-39) to endothelin-1 (1-21) in vitro. Proc Natl Acad Sci U S A. 1991;88:703-707.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 703-707
    • McMahon, E.G.1    Palomo, M.A.2    Moore, W.M.3    McDonald, J.F.4    Stern, M.K.5
  • 13
    • 0024521522 scopus 로고
    • Conversion of big endothelin-1 to 21-residue endothelin-1 is essential for expression of full vasoconstrictor activity: Structure-activity relationships of big endothelin-1
    • Kimura S, Kasuya Y, Sawamura T, Osamu S, Yoshiki S, Yanagisawa M, Goto K, Masaki T. Conversion of big endothelin-1 to 21-residue endothelin-1 is essential for expression of full vasoconstrictor activity: structure-activity relationships of big endothelin-1. J Cardiovasc Pharmacol. 1989;13(suppl 5):S5-S7.
    • (1989) J Cardiovasc Pharmacol. , vol.13 , Issue.5 SUPPL.
    • Kimura, S.1    Kasuya, Y.2    Sawamura, T.3    Osamu, S.4    Yoshiki, S.5    Yanagisawa, M.6    Goto, K.7    Masaki, T.8
  • 14
    • 0006755597 scopus 로고
    • Separation and biological activity of the chymotrypsin and cathepsin G cleavage Products of big endothelin (1-39)
    • Abstract
    • Patterson K, MacNaul R, Rubanyi GM, Parker-Botello LH. Separation and biological activity of the chymotrypsin and cathepsin G cleavage Products of big endothelin (1-39). FASEB J. 1990;4:A909. Abstract.
    • (1990) FASEB J. , vol.4
    • Patterson, K.1    MacNaul, R.2    Rubanyi, G.M.3    Parker-Botello, L.H.4
  • 15
    • 0026752817 scopus 로고
    • The two step conversion of big endothelin 1 to endothelin 1 by subcellular fractions from human polymorphonuclear leukocytes
    • Kaw S, Hecker M, Vane JR. The two step conversion of big endothelin 1 to endothelin 1 by subcellular fractions from human polymorphonuclear leukocytes. Proc Natl Acad Sci U S A. 1992;89:6886-6890.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 6886-6890
    • Kaw, S.1    Hecker, M.2    Vane, J.R.3
  • 17
    • 0029017876 scopus 로고
    • Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon sensitive metalloprotease with acidic pH optimum
    • Emoto N, Yanagisawa M. Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon sensitive metalloprotease with acidic pH optimum. J Biol Chem. 1995;270:15262-15268.
    • (1995) J Biol Chem. , vol.270 , pp. 15262-15268
    • Emoto, N.1    Yanagisawa, M.2
  • 19
    • 0029129597 scopus 로고
    • Microscopic localization of active proteases by in situ zymography: Detection of matrix metalloproteinase activity in vascular tissue
    • Galis ZS, Sukhova GK, Libby P. Microscopic localization of active proteases by in situ zymography: detection of matrix metalloproteinase activity in vascular tissue. FASEB J. 1995;9:974-980.
    • (1995) FASEB J. , vol.9 , pp. 974-980
    • Galis, Z.S.1    Sukhova, G.K.2    Libby, P.3
  • 20
    • 0024948683 scopus 로고
    • A new method for mechanically denuding the endothelium of small (50-150 μm) arteries with a human hair
    • Osol GC, Cipolla M, Knutson S. A new method for mechanically denuding the endothelium of small (50-150 μm) arteries with a human hair. Blood Vessels. 1989;26:320-324.
    • (1989) Blood Vessels , vol.26 , pp. 320-324
    • Osol, G.C.1    Cipolla, M.2    Knutson, S.3
  • 21
    • 23544482297 scopus 로고
    • In vitro pharmacology of a non-selective (ETA/ETB) endothelin receptor antagonist, PD 142893 (Ac-(β-phenyl)D-Phe-L-Leu-L-Asp-L-Ile-Ile-L-Trp trifluoroacetate)
    • Abstract
    • Hingorani G, Major T, Panek R, Flynn M, Reynolds E, He X, Cody W, Doherty A, Rapundalo S. In vitro pharmacology of a non-selective (ETA/ETB) endothelin receptor antagonist, PD 142893 (Ac-(β-phenyl)D-Phe-L-Leu-L-Asp-L-Ile-Ile-L-Trp trifluoroacetate). FASEB J. 1992;6: A1003. Abstract.
    • (1992) FASEB J. , vol.6
    • Hingorani, G.1    Major, T.2    Panek, R.3    Flynn, M.4    Reynolds, E.5    He, X.6    Cody, W.7    Doherty, A.8    Rapundalo, S.9
  • 23
    • 0027984808 scopus 로고
    • Endothelins: Molecular biology, biochemistry, pharmacology, physiology, and pathophysiology
    • Rubanyi GM, Polokoff MA. Endothelins: molecular biology, biochemistry, pharmacology, physiology, and pathophysiology. Pharmacol Rev. 1994;46:325-415.
    • (1994) Pharmacol Rev. , vol.46 , pp. 325-415
    • Rubanyi, G.M.1    Polokoff, M.A.2
  • 24
    • 0028115798 scopus 로고
    • Endothelin-1 as an aggravating factor of diseminated intravascular coagulation associated with, malignant neoplasms
    • Ishibashi M, Ito N, Fujita M, Furue H, Yamaji T. Endothelin-1 as an aggravating factor of diseminated intravascular coagulation associated with, malignant neoplasms. Cancer. 1994;73:191-195.
    • (1994) Cancer , vol.73 , pp. 191-195
    • Ishibashi, M.1    Ito, N.2    Fujita, M.3    Furue, H.4    Yamaji, T.5
  • 25
    • 0345516003 scopus 로고    scopus 로고
    • Increased expression of membrane-type matrix metalloproteinase and preferential localization of matrix metalloproteinase-2 to the neointima of balloon-injured rat carotid arteries
    • Jenkins GM, Crow MT, Bilato C, Gluzband Y, Ryu WS, Li Z, Stetler-Stevenson W, Nater C, Froehlich JP, Lakatta EG, Cheng L. Increased expression of membrane-type matrix metalloproteinase and preferential localization of matrix metalloproteinase-2 to the neointima of balloon-injured rat carotid arteries. Circulation. 1998;97:82-90.
    • (1998) Circulation , vol.97 , pp. 82-90
    • Jenkins, G.M.1    Crow, M.T.2    Bilato, C.3    Gluzband, Y.4    Ryu, W.S.5    Li, Z.6    Stetler-Stevenson, W.7    Nater, C.8    Froehlich, J.P.9    Lakatta, E.G.10    Cheng, L.11
  • 26
    • 0028030129 scopus 로고
    • Extracelluiar matrix degrading metalloproteinases in the pathogenesis of arteriosclerosis
    • Newby AC, Southgate KM, Davies M. Extracelluiar matrix degrading metalloproteinases in the pathogenesis of arteriosclerosis. Basic Res Cardiol. 1993;89:59-70.
    • (1993) Basic Res Cardiol. , vol.89 , pp. 59-70
    • Newby, A.C.1    Southgate, K.M.2    Davies, M.3
  • 29
    • 0030885556 scopus 로고    scopus 로고
    • The molecular basis of restenosis
    • Libby P, Tanaka H. The molecular basis of restenosis. Prog Cardiovasc Dis. 1997;40:97-106.
    • (1997) Prog Cardiovasc Dis. , vol.40 , pp. 97-106
    • Libby, P.1    Tanaka, H.2
  • 30
    • 0032828541 scopus 로고    scopus 로고
    • Rapid release of matrix metalloproteinase (MMP)-2 by thrombin in the rat aorta: Modulation by protein tyrosine kinase/phosphatase
    • Fernandez-Patron C, Zhang Y, Radomski MW, Hollenberg MD, Davidge ST. Rapid release of matrix metalloproteinase (MMP)-2 by thrombin in the rat aorta: modulation by protein tyrosine kinase/phosphatase. Thromb Haemost. 1999;82:1353-1357.
    • (1999) Thromb Haemost. , vol.82 , pp. 1353-1357
    • Fernandez-Patron, C.1    Zhang, Y.2    Radomski, M.W.3    Hollenberg, M.D.4    Davidge, S.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.