PROTEOLYTIC RELEASE OF HUMAN ANGIOTENSIN-CONVERTING ENZYME EXPRESSED IN CHINESE-HAMSTER OVARY CELLS IS ENHANCED BY PHORBOL ESTER

被引：15

作者：

EHLERS, MRW ^{[1
]}

SCHOLLE, RR ^{[1
]}

RIORDAN, JF ^{[1
]}

机构：

[1] HARVARD UNIV, SCH MED, CTR BIOCHEM & BIOPHYS SCI & MED, BOSTON, MA 02115 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 206卷 / 02期

关键词：

D O I：

10.1006/bbrc.1995.1077

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：

Membrane-bound angiotensin-converting enzyme (ACE) expressed in Chinese hamster ovary (CHO) cells is proteolytically released in soluble form into the medium. We find that this release is stimulated up to 50-fold by phorbol-12, 13-dibutyrate and also by the addition of fresh, serum-containing media. Concomitant with the enhanced release is a marked decrease in levels of membrane-bound ACE, down to 7% of resting revels in the case of phorbol ester stimulation. Staurosporine, a protein kinase C (PKC) inhibitor, abolishes the phorbol ester effect. Kinetic analysis of the stimulated release rate indicates that it is first order, likely due to substrate depletion; calculated half times, t1/2 are 174 +/- 12 min and 40 +/- 6 min for the media-change and phorbol ester stimulated rates, respectively. Thus, release of membrane-bound ACE in CHO cells is regulated, in part, by a PKC-dependent mechanism. (C) 1995 Academic Press, Inc.

引用

页码：541 / 547

页数：7

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