Chromogranins, widespread in endocrine and nervous tissue, bind Ca2+.
The proteinaceous components of the secretory vesicle contents isolated from bovine adrenal medulla bind Ca2+ (number of binding sites, 152 +/- 52 nmol Ca2+ per mg protein; dissociation constant, 54 +/- 8 microM (n = 5)). SDS-polyacrylamide gel electrophoresis and 45Ca2+ binding of the proteins following their separation and blotting on nitrocellulose revealed that Ca2+ binds to chromogranins. Moreover, it was shown that the chromogranins, like other known Ca2+-binding proteins, can be specifically stained with a cationic carbocyanine dye. The Ca2+-binding function of the chromogranins described here, in conjunction with recent findings concerning Ca2+ transport across chromaffin vesicle membranes and the widespread distribution findings concerning Ca2+ transport across chromaffin vesicle membranes and the widespread distribution of chromogranins in many different endocrine and nerve cells, points to the general importance of these proteins in the metabolism of Ca2+.
D000313:Adrenal Medulla / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002417:Cattle; D002837:Chromaffin Granules / Q000378:metabolism; D002864:Chromogranins / Q000378:metabolism*; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000378:metabolism*
D002864:Chromogranins; D009419:Nerve Tissue Proteins; D002118:Calcium