Metabolism of endothelin-1 and big endothelin-1 by recombinant neutral endopeptidase EC.3.4.24.11.
作者： Zaid A. Abassi , Eliahu Golomb , Robert Bridenbaugh , Harry R. Keiser
DOI: 10.1111/J.1476-5381.1993.TB13724.X
关键词:
摘要: 1. Inhibitors of neutral endopeptidase EC.3.4.24.11 (NEP) have been shown to attenuate the hypertensive effect big-endothelin-1 (BET-1) in rats. To determine whether NEP converts BET-1 endothelin-1 (ET-1), a recombinant (rNEP) on and ET-1 was assessed vitro. 2. Incubation [125I]-ET-1 with 1 microgram ml-1 rNEP resulted degradation peptide within minutes. Increase amount 10 micrograms led total cleavage seconds. 3. Phosphoramidon (10 microM) or SQ-28,603 (100 totally suppressed by rNEP. 4. The [125I]-BET-1 either much slower than that [125I]-ET-1. Again, both phosphoramidon SQ 28,603 protected from degradation. 5. Intact not observed when incubated 6. These data show is an endothelin converting enzyme.
sci-hub.se 参考文章(37)
A. J. Turner, Neuropeptides and their peptidases VCH , Ellis Horwood. ,(1987)
J. Vijayaraghavan, A.G. Scicli, O.A. Carretero, C. Slaughter, C. Moomaw, L.B. Hersh, The hydrolysis of endothelins by neutral endopeptidase 24.11 (enkephalinase). Journal of Biological Chemistry. ,vol. 265, pp. 14150- 14155 ,(1990) , 10.1016/S0021-9258(18)77280-3
C Llorens-Cortes, H Huang, P Vicart, J.M. Gasc, D Paulin, P Corvol, Identification and characterization of neutral endopeptidase in endothelial cells from venous or arterial origins. Journal of Biological Chemistry. ,vol. 267, pp. 14012- 14018 ,(1992) , 10.1016/S0021-9258(19)49671-3
Toru YAMAGUCHI, Hiroshi KIDO, Nobuhiko KATUNUMA, A membrane-bound metallo-endopeptidase from rat kidney. Characteristics of its hydrolysis of peptide hormones and neuropeptides. FEBS Journal. ,vol. 204, pp. 547- 552 ,(1992) , 10.1111/J.1432-1033.1992.TB16666.X
Donna M. Wypij, James S. Nichols, Paul J. Novak, D. Lowell Stacy, Judd Berman, Jeffrey S. Wiseman, Role of mast cell chymase in the extracellular processing of big-endothelin-1 to endothelin-1 in the perfused rat lung Biochemical Pharmacology. ,vol. 43, pp. 845- 853 ,(1992) , 10.1016/0006-2952(92)90252-E
Tatsuya Sawamura, Sadao Kimura, Osamu Shinmi, Yoshiki Sugita, Masashi Yanagisawa, Katsutoshi Goto, Tomoh Masaki, Purification and characterization of putative endothelin converting enzyme in bovine adrenal medulla: Evidence for a cathepsin D-like enzyme Biochemical and Biophysical Research Communications. ,vol. 168, pp. 1230- 1236 ,(1990) , 10.1016/0006-291X(90)91160-T
Yasuo Matsumura, Ruriko Ikegawa, Yaeko Tsukahara, Masanori Takaoka, Shiro Morimoto, Conversion of big endothelin-1 to endothelin-1 by two types of metalloproteinases derived from porcine aortic endothelial cells FEBS Letters. ,vol. 272, pp. 166- 170 ,(1990) , 10.1016/0014-5793(90)80475-X
Jinshyun R. Wu-Wong, Gerald P. Budzik, Edward M. Devine, Terry J. Opgenorth, Characterization of endothelin converting enzyme in rat lung Biochemical and Biophysical Research Communications. ,vol. 171, pp. 1291- 1296 ,(1990) , 10.1016/0006-291X(90)90826-9
Françoise Pons, Caroline Touvay, Vincent Lagente, Jean Michel Mencia-Huerta, Pierre Braquet, Involvement of a phosphoramidon-sensitive endopeptidase in the processing of big endothelin-1 in the guinea-pig. European Journal of Pharmacology. ,vol. 217, pp. 65- 70 ,(1992) , 10.1016/0014-2999(92)90512-3
Kenji Okada, Junji Takada, Yukiko Arai, Kenji Matsuyama, Mitsuo Yano, Importance of the C-terminal region of big endothelin-1 for specific conversion by phosphoramidon-sensitive endothelin converting enzyme. Biochemical and Biophysical Research Communications. ,vol. 180, pp. 1019- 1023 ,(1991) , 10.1016/S0006-291X(05)81167-2