Processing of chromogranin A within chromaffin granules starts at C- and N-terminal cleavage sites.
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.
Wohlfarter
T
T
Department of Pharmacology, University of Innsbruck, Austria.
Fischer-Colbrie
R
R
Hogue-Angeletti
R
R
Eiden
L E
LE
Winkler
H
H
D000818:Animals; D002417:Cattle; D002837:Chromaffin Granules / Q000378:metabolism*; D002838:Chromaffin System / Q000378:metabolism*; D053379:Chromogranin A; D002864:Chromogranins / Q000235:genetics*; D007106:Immune Sera; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000235:genetics*; D010446:Peptide Fragments / Q000032:analysis / Q000276:immunology; D011499:Protein Processing, Post-Translational
D053379:Chromogranin A; D002864:Chromogranins; D007106:Immune Sera; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments