Processing of chromogranin A within chromaffin granules starts at C‐ and N‐terminal cleavage sites

FEBS Letters

Hogue-Angeletti, Ruth¹  Eiden, Lee E.²  Fischer-Colbrie, Reiner³  Winkler, Hans³  Wohlfarter, Thomas³ 

[1] Department of Pathology and Laboratory Medicine, Division of Neuropathology, University of Pennsylvania, Philadelphia, USA;Laboratory of Cell Biology, National Institutes of Mental Health, Bethesda, Maryland, USA;Department of Pharmacology, University of Innsbruck, Austria

关键词: Chromogranin A;    Chromaffin granule;    Proteolytic processing;   

DOI  :  10.1016/0014-5793(88)80704-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Specific antisera were raised against synthetic peptide fragments of bovine chromogranin A. The soluble proteins of bovine chromaffin granules were subjected to two-dimensional immunoblotting with these antisera. The endogenous breakdown products of chromogranin A gave distinct patterns of immunostaining which enabled us to correlate these peptides with defined regions of the chromogranin A molecule. The results establish that within chromaffin granules degradation of chromogranin A by the endogenous proteases can start either at the C- or the N-terminal site.

【 授权许可】

Unknown