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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Ehlers MR,Scholle RR,Riordan JFdoi
10.1006/bbrc.1995.1077subject
Has Abstractpub_date
1995-01-17 00:00:00pages
541-7issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(85)71077-7journal_volume
206pub_type
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