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Volumn 51, Issue 3, 1996, Pages 259-266

The conformation of human big endothelin-1 favours endopeptidase hydrolysis of the TRP21-VAL22 bond

Author keywords

Blood pressure; Endothelin converting enzyme; Endothelium; Vascular smooth muscle; Vasoconstriction

Indexed keywords

BIG ENDOTHELIN 1; ENDOTHELIN 1; ENDOTHELIN CONVERTING ENZYME; PHLORETIC ACID N HYDROXYSUCCINIMIDE ESTER; PROTEIN DERIVATIVE; PROTEINASE; S ACETYLTHIOGLYCOLIC ACID N HYDROXYSUCCINIMIDE ESTER; SUCCINIMIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0030020655     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/0006-2952(95)02164-7     Document Type: Article
Times cited : (5)

References (40)
  • 1
    • 0024553103 scopus 로고
    • Putative precursors of endothelin have less vasoconstrictor activity in vitro but a potent pressor effect in vivo
    • Kashiwabara T, Inagaki Y, Ohta H, Iwamatsu A, Nomizu M, Morita A and Nishikori K, Putative precursors of endothelin have less vasoconstrictor activity in vitro but a potent pressor effect in vivo. FEBS Letts 247: 73-76, 1989.
    • (1989) FEBS Letts , vol.247 , pp. 73-76
    • Kashiwabara, T.1    Inagaki, Y.2    Ohta, H.3    Iwamatsu, A.4    Nomizu, M.5    Morita, A.6    Nishikori, K.7
  • 3
    • 0026081855 scopus 로고
    • Responses to endothelin-1, human proendothelin (1-38) and porcine proendothelin (1-39) in the rat on intravenous administration and in the blood perfused mesentery
    • Douglas SA and Hiley CR, Responses to endothelin-1, human proendothelin (1-38) and porcine proendothelin (1-39) in the rat on intravenous administration and in the blood perfused mesentery. Neurochem Int 18: 445-454, 1991.
    • (1991) Neurochem Int , vol.18 , pp. 445-454
    • Douglas, S.A.1    Hiley, C.R.2
  • 4
    • 0027370749 scopus 로고
    • Regional haemodynamic responses to intravenous and intraarterial endothelin-1 and big endothelin-1 in conscious rats
    • Gardiner SM, Kemp PA and Bennett T, Regional haemodynamic responses to intravenous and intraarterial endothelin-1 and big endothelin-1 in conscious rats. Br J Pharmacol 110: 1532-1536, 1993.
    • (1993) Br J Pharmacol , vol.110 , pp. 1532-1536
    • Gardiner, S.M.1    Kemp, P.A.2    Bennett, T.3
  • 6
    • 0025072065 scopus 로고
    • Phosphoramidon, a metalloproteinase inhibitor, suppresses the hypertensive effect of big endothelin-1
    • Matsumura Y, Hisaki K, Takaoka M and Morimoto S, Phosphoramidon, a metalloproteinase inhibitor, suppresses the hypertensive effect of big endothelin-1. Eur J Pharmacol 185: 103-106, 1990.
    • (1990) Eur J Pharmacol , vol.185 , pp. 103-106
    • Matsumura, Y.1    Hisaki, K.2    Takaoka, M.3    Morimoto, S.4
  • 7
    • 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 and 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 USA 88: 703-707, 1991.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 703-707
    • McMahon, E.G.1    Palomo, Ma.2    Moore, W.M.3    McDonald, J.F.4    Stern, M.K.5
  • 8
    • 0025914135 scopus 로고
    • The effects of phosphoramidon on the regional haemodynamic responses to human proendothelin-1 [1-38] in conscious rats
    • Gardiner SM, Compton AM, Kemp PA and Bennett T, The effects of phosphoramidon on the regional haemodynamic responses to human proendothelin-1 [1-38] in conscious rats. Br J Pharmacol 103: 2009-2015, 1991.
    • (1991) Br J Pharmacol , vol.103 , pp. 2009-2015
    • Gardiner, S.M.1    Compton, A.M.2    Kemp, P.A.3    Bennett, T.4
  • 9
    • 0028843045 scopus 로고
    • Radioimmunoassay evidence that the pressor effect of big endothelin-1 is due to local conversion to endothelin-1
    • Corder R and Vane JR, Radioimmunoassay evidence that the pressor effect of big endothelin-1 is due to local conversion to endothelin-1. Biochem Pharmacol 49: 375-380, 1995.
    • (1995) Biochem Pharmacol , vol.49 , pp. 375-380
    • Corder, R.1    Vane, J.R.2
  • 10
    • 0028261084 scopus 로고
    • Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells
    • Shimada K, Takahashi M and Tanzawa K, Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells. J Biol Chem 269: 18275-18278, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 18275-18278
    • Shimada, K.1    Takahashi, M.2    Tanzawa, K.3
  • 11
    • 0027992642 scopus 로고
    • ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1
    • Xu D, Emoto N, Giaid A, Slaughter C, Kaw S, deWit D and Yanagisawa M, ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1. Cell 78: 473-485, 1994.
    • (1994) Cell , vol.78 , pp. 473-485
    • Xu, D.1    Emoto, N.2    Giaid, A.3    Slaughter, C.4    Kaw, S.5    Dewit, D.6    Yanagisawa, M.7
  • 15
    • 0028923422 scopus 로고
    • Cloning and sequencing of a human endothelin converting enzyme in renal adenocarcinoma (ACHN) cells producing endothelin-2
    • Yorimitsu K, Moroi K, Inagaki N, Saito T, Masuda Y, Masaki T, Seino S and Kimura S, Cloning and sequencing of a human endothelin converting enzyme in renal adenocarcinoma (ACHN) cells producing endothelin-2. Biochem Biophys Res Commun 208: 721-727, 1995.
    • (1995) Biochem Biophys Res Commun , vol.208 , pp. 721-727
    • Yorimitsu, K.1    Moroi, K.2    Inagaki, N.3    Saito, T.4    Masuda, Y.5    Masaki, T.6    Seino, S.7    Kimura, S.8
  • 17
    • 0025939090 scopus 로고
    • Phosphoramidon inhibits the generation of endothelin-1 from exogenously applied big endothelin-1 in cultured vascular endothelial cells and smooth muscle cells
    • Ikegawa R, Matsumura Y, Tsukahara Y, Takaoka M and Morimoto S, Phosphoramidon inhibits the generation of endothelin-1 from exogenously applied big endothelin-1 in cultured vascular endothelial cells and smooth muscle cells. FEBS Letts 293: 45-48, 1991.
    • (1991) FEBS Letts , vol.293 , pp. 45-48
    • Ikegawa, R.1    Matsumura, Y.2    Tsukahara, Y.3    Takaoka, M.4    Morimoto, S.5
  • 18
    • 0028898414 scopus 로고
    • A simple method for isolating human endothelin converting enzyme free from contamination by neutral endopeptidase 24.11
    • Corder R, Khan N and Harrison VJ, A simple method for isolating human endothelin converting enzyme free from contamination by neutral endopeptidase 24.11. Biochem Biophys Res Commun 207: 355-362, 1995.
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 355-362
    • Corder, R.1    Khan, N.2    Harrison, V.J.3
  • 19
    • 0027158198 scopus 로고
    • Phosphoramidon-sensitive endothelin converting enzyme in cultured vascular smooth muscle cells converts big endothelin-3 to endothelin-3
    • Tsukahara Y, Matsumura Y, Kuninobu K, Kojima T, Takaoka M and Morimoto S, Phosphoramidon-sensitive endothelin converting enzyme in cultured vascular smooth muscle cells converts big endothelin-3 to endothelin-3. Life Sci 53: 465-471, 1993.
    • (1993) Life Sci , vol.53 , pp. 465-471
    • Tsukahara, Y.1    Matsumura, Y.2    Kuninobu, K.3    Kojima, T.4    Takaoka, M.5    Morimoto, S.6
  • 20
    • 0027316871 scopus 로고
    • Endothelium-independent pressor effect of big endothelin-1 and its inhibition by phosphoramidon in rat mesenteric artery
    • Hisaki K, Matsumura Y, Nishiguchi S, Fujita K, Takaoka M and Morimoto S, Endothelium-independent pressor effect of big endothelin-1 and its inhibition by phosphoramidon in rat mesenteric artery. Eur J Pharmacol 241: 75-81, 1993.
    • (1993) Eur J Pharmacol , vol.241 , pp. 75-81
    • Hisaki, K.1    Matsumura, Y.2    Nishiguchi, S.3    Fujita, K.4    Takaoka, M.5    Morimoto, S.6
  • 21
    • 85029985265 scopus 로고
    • Modification of big endothelin-1 decreases pressor activity and conversion by endothelin converting enzyme
    • Corder R and Vane JR, Modification of big endothelin-1 decreases pressor activity and conversion by endothelin converting enzyme. FASEB J 8: A104, 1994.
    • (1994) FASEB J , vol.8
    • Corder, R.1    Vane, J.R.2
  • 22
    • 0027725151 scopus 로고
    • Effects of phosphoramidon in endothelial cell cultures on the endogenous synthesis of endothelin-1 and on conversion of exogenous big endothelin-1 to endothelin-1
    • Corder R, Harrison VJ, Khan N, Anggard EE and Vane JR, Effects of phosphoramidon in endothelial cell cultures on the endogenous synthesis of endothelin-1 and on conversion of exogenous big endothelin-1 to endothelin-1. J Cardiovasc Pharmacol 22 (Suppl. 8): S73-S76, 1993.
    • (1993) J Cardiovasc Pharmacol , vol.22 , Issue.SUPPL. 8
    • Corder, R.1    Harrison, V.J.2    Khan, N.3    Anggard, E.E.4    Vane, J.R.5
  • 23
    • 0027185110 scopus 로고
    • Use of the endothelin antagonists BQ-123 and PD142893 to reveal three endothelin receptors mediating smooth muscle contraction and the release of EDRF
    • Warner TD, Allcock GH, Corder R and Vane JR, Use of the endothelin antagonists BQ-123 and PD142893 to reveal three endothelin receptors mediating smooth muscle contraction and the release of EDRF. Br J Pharmacol 110: 777-782, 1993.
    • (1993) Br J Pharmacol , vol.110 , pp. 777-782
    • Warner, T.D.1    Allcock, G.H.2    Corder, R.3    Vane, J.R.4
  • 24
    • 0015097243 scopus 로고
    • The smooth muscle cell, II. Growth of smooth muscle in culture and formation of elastic fibres
    • Ross R, The smooth muscle cell, II. Growth of smooth muscle in culture and formation of elastic fibres. J Cell Biol 50: 172-186, 1971.
    • (1971) J Cell Biol , vol.50 , pp. 172-186
    • Ross, R.1
  • 25
    • 0027136030 scopus 로고
    • Big endothelin-1 structure important for specific processing by endothelin-converting enzyme of bovine endothelial cells
    • Okada K, Arai Y, Hata M, Matsuyama K and Yano M, Big endothelin-1 structure important for specific processing by endothelin-converting enzyme of bovine endothelial cells. Eur J Biochem 218: 493-498, 1993.
    • (1993) Eur J Biochem , vol.218 , pp. 493-498
    • Okada, K.1    Arai, Y.2    Hata, M.3    Matsuyama, K.4    Yano, M.5
  • 29
    • 0026331345 scopus 로고
    • Evaluation of endothelin receptor populations using endothelin-1 biotinylated at lysine-9 sidechain
    • Magazine HI, Andersen TT, Goligorsky MS and Malik AB, Evaluation of endothelin receptor populations using endothelin-1 biotinylated at lysine-9 sidechain. Biochem Biophys Res Commun 181: 1245-1250, 1991.
    • (1991) Biochem Biophys Res Commun , vol.181 , pp. 1245-1250
    • Magazine, H.I.1    Andersen, T.T.2    Goligorsky, M.S.3    Malik, A.B.4
  • 30
    • 0027963329 scopus 로고
    • Generation by the phosphoramidon-sensitive peptidases, endopeptidase-24.11 and thermolysin, of endothelin-1 and C-terminal fragment from big endothelin-1
    • Murphy LJ, Corder R, Mallet AI and Turner AJ, Generation by the phosphoramidon-sensitive peptidases, endopeptidase-24.11 and thermolysin, of endothelin-1 and C-terminal fragment from big endothelin-1. Br J Pharmacol 113: 137-142, 1994.
    • (1994) Br J Pharmacol , vol.113 , pp. 137-142
    • Murphy, L.J.1    Corder, R.2    Mallet, A.I.3    Turner, A.J.4
  • 32
    • 0024419448 scopus 로고
    • CDNA cloning and chromosomal assignment of the gene encoding endothelin 3
    • Bloch KD, Eddy RL, Shows TB and Quertermous T, cDNA cloning and chromosomal assignment of the gene encoding endothelin 3. J Biol Chem 264: 18156-18161, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 18156-18161
    • Bloch, K.D.1    Eddy, R.L.2    Shows, T.B.3    Quertermous, T.4
  • 35
  • 37
    • 0024418246 scopus 로고
    • Processing endoprotease recognizes a structural feature at the cleavage site of peptide prohormones
    • Brakch NB, Boussetta H, Rholam M and Cohen P, Processing endoprotease recognizes a structural feature at the cleavage site of peptide prohormones. J Biol Chem 264: 15912-15916, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 15912-15916
    • Brakch, N.B.1    Boussetta, H.2    Rholam, M.3    Cohen, P.4
  • 38
    • 0025162254 scopus 로고
    • Prohormonal cleavage sites are associated with Ω loops
    • Bek E and Berry R, Prohormonal cleavage sites are associated with Ω loops. Biochemistry 29: 178-183, 1990.
    • (1990) Biochemistry , vol.29 , pp. 178-183
    • Bek, E.1    Berry, R.2


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