In vitro metabolism of LVV-Hemorphin-7 by renal cytosol and purified prolyl endopeptidase

被引：16

作者：

Fruitier-Arnaudin, I

Cohen, M

Coitoux, C

Piot, JM

机构：

[1] Univ Rochelle, Lab Genie Proteique & Cellulaire, F-17042 La Rochelle 1, France

[2] Inst Univ Technol, Dept Genie Biol, F-17026 La Rochelle, France

来源：

PEPTIDES | 2003年 / 24卷 / 08期

关键词：

hemorphin; peptide hydrolysis; metabolism; homogenate; renal cytosol; subcellular fractions; prolyl endopeptidase;

D O I：

10.1016/j.peptides.2003.07.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The metabolism of LVVH7, an endogenous peptide obtained by cathepsin D hydrolysis of the beta chain of hemoglobin, was studied, in vitro, in the presence of cytosol of rat kidney and compared with angiotensin IV. High metabolic activity was found against these two peptides (half life time < 2 min) in this subcellular fraction. The main products of LVVH7 metabolism by renal cytosol are VVH7, H7 and LVVH6 suggesting both aminopeptidase and carboxypeptidase activities. The use of PEP inhibitor in kidney cytosol permitted to demonstrate the major role of prolyl endopeptidase (PEP) in LVVH7 degradation. This fact was reinforced by a kinetic study investigated with purified enzyme (K-m/V-max about 238 mM(-1) s(-1) and close to that observed for angiotensin related peptides). (C) 2003 Elsevier Inc. All rights reserved.

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页码：1201 / 1206

页数：6

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