Proteolytic release of human angiotensin-converting enzyme expressed in Chinese hamster ovary cells is enhanced by phorbol ester.

Abstract:

: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 levels 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.

authors

Ehlers MR,Scholle RR,Riordan JF

doi

10.1006/bbrc.1995.1077

subject

Has Abstract

pub_date

1995-01-17 00:00:00

pages

541-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(85)71077-7

journal_volume

206

pub_type

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