Secretory proteins from adrenal medullary cells are carboxyl-methylated in vivo and released under their methylated form by acetylcholine.
The carboxyl methylation of secretory proteins in vivo was investigated in bovine adrenal medullary cells in culture. Chromogranin A, the major intragranular secretory protein in adrenal medullary cells, and other secretory proteins were found to be carboxyl-methylated within secretory vesicles. The in vivo labeling pattern using [methyl-3H]methionine and the in vitro labeling pattern using S-adenosyl-[methyl-14C]methionine of intravesicular secretory proteins were similar. The detection of methylated chromogranin A in mature secretory vesicles required 3-6 h, a time consistent with the synthesis and storage of secretory proteins in this tissue. Carboxyl-methylated chromogranin A was secreted from medullary cells by exocytosis via activation of nicotinic cholinergic receptor and recovered still under the methylated form in the incubation medium. Since protein-carboxyl-methylase is cytosolic, these results suggest that methylation of secretory proteins is a cotranslational phenomenon.
D000109:Acetylcholine / Q000378:metabolism*; D000313:Adrenal Medulla / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002837:Chromaffin Granules / Q000378:metabolism; D053379:Chromogranin A; D002864:Chromogranins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008745:Methylation; D009419:Nerve Tissue Proteins / Q000378:metabolism*
D053379:Chromogranin A; D002864:Chromogranins; D009419:Nerve Tissue Proteins; D000109:Acetylcholine