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J. Biol. Chem., Vol. 275, Issue 30, 22905-22915, July 28, 2000
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From the Department of Medicine and Center for Molecular Genetics,
University of California, and San Diego Veterans Affairs Healthcare
System, San Diego, California 92161
The catestatin fragment of chromogranin A is an
inhibitor of catecholamine release, but its occurrence in
vivo has not yet been verified, nor have its precise cleavage
sites been established. Here we found extensive processing of
catestatin in chromogranin A, as judged by catestatin radioimmunoassay
of size-fractionated chromaffin granules. On mass spectrometry, a major
catestatin form was bovine chromogranin A332-364; identity
of the peptide was confirmed by diagnostic Met346
oxidation. Further analysis revealed two additional forms: bovine chromogranin A333-364 and A343-362. Synthetic
longer (chromogranin A332-364) and shorter (chromogranin
A344-364) versions of catestatin each inhibited
catecholamine release from chromaffin cells, with superior potency for
the shorter version (IC50 ~2.01 versus
~0.35 µM). Radioimmunoassay demonstrated catestatin release from the regulated secretory pathway in chromaffin cells. Human
catestatin was cleaved in pheochromocytoma chromaffin granules, with
the major form, human chromogranin A340-372, bounded by
dibasic sites. We conclude that catestatin is cleaved extensively in vivo, and the peptide is released by exocytosis. In
chromaffin granules, the major form of catestatin is cleaved at dibasic
sites, while smaller carboxyl-terminal forms also occur. Knowledge of cleavage sites of catestatin from chromogranin A may provide a useful
starting point in analysis of the relationship between structure and
function for this peptide.
Formation of the Catecholamine Release-inhibitory Peptide
Catestatin from Chromogranin A
DETERMINATION OF PROTEOLYTIC CLEAVAGE SITES IN HORMONE STORAGE
GRANULES*
*
This work was supported by grants from the Department of
Veterans Affairs, the National Institutes of Health, and the American Heart Association.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Medicine and Center for Molecular Genetics (9111H), University of
California, San Diego, 3350 La Jolla Village Dr., San Diego, CA 92161. Tel.: 858-552-8585 (ext. 7373); Fax: 858-642-6331; E-mail:
doconnor@ucsd.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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