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- W2163476768 abstract "Ca 2+ /calmodulin-dependent protein kinases I and II, initially identified in brain on the basis of their ability to phosphorylate synapsin I, have been implicated in the regulation of Ca 2+ -dependent synaptic neurosecretion. Specific recombinant and synthetic peptide antibodies were used to examine the distribution of CaM kinases I and II in the rat pancreas and other tissues. The CaM kinase I antibodies detected a doublet of cytosolic proteins of ∼38 and ∼42 kD by immunoblot. CaM kinase I was observed in glucagon-containing A-cells at the periphery of the islet of Langerhans but had little or no overlap with pancreatic polypeptide or somatostatin cells. In contrast, CaM kinase II was localized to somatostatin-containing D-cells. CaM kinase I co-localized with glucagon secretory granules. CaM kinase II was not associated with the somatostatin granule but rather was enriched in areas of the cells that contained relatively little somatostatin. Because glucagon secretion is Ca 2+ -dependent, it is attractive to speculate that CaM kinase I may play a regulatory role in glucagon secretion. Glucagon and somatostatin cells both utilize intracellular Ca 2+ for signaling. Therefore, specific CaM kinases may act as effectors of Ca 2+ in these different cell types." @default.
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- W2163476768 date "1998-04-01" @default.
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- W2163476768 title "Cellular Localization of Calmodulin-dependent Protein Kinases I and II to A-cells and D-cells of the Endocrine Pancreas" @default.
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- W2163476768 doi "https://doi.org/10.1177/002215549804600412" @default.
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