Abstract
Publisher Summary The Ca 2+ /PS/DAG-stimulated protein kinase C (PKC) subtypes are a family of closely related enzymes highly abundant in the CNS. These enzymes exhibit distinct biochemical characteristics, cellular and subcellular localizations, and developmental expression; however, direct evidence linking the activation of each of these enzymes with a particular response is not yet available. Selective subcellular localizations of these enzymes have thus far provided the best indication of possible functional distinction among these enzymes. Because of the unusual association of PKC isozymes with distinct cellular compartments, this chapter investigates the membrane lipid components capable of conferring such as specificity. Among those tested, the inositol-containing phospholipids appear to provide the best selectivity for PKC I. Thus, association of PKC I with these phospholipids not only places this enzyme near the site of its activator, DAG, generated by the activation of phospholipase C, but also its substrates that share the same binding affinity for these phospholipids as PKC I.
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