The PKC isozyme family

Studies of phorbol ester effects mediated by PKC have revealed a number of mechanisms which may lead to the observed heterogeneity in the biological responses. Using oligonucleotide probes generated from the partial amino acid sequence of purified bov ine brain PKC, studies revealed that PKC exists as a family of closely related enzymes. Four subspecies (a, (31, pll and y) emerged from the initial screening of a variety of cDNA libraries. Additionally, three other species (8, e, £) were identified from rat and rabbit cDNA libraries using a mixture of a, (ill, and y cDNAs as probes. In addition to certain structural differences, members of the PKC family differ in substrate specificity, ability to be activated by phospholipid, calcium, diacylglycerol and arachi-donic acid. Members of this family also differ in tissue distribution and intracellular localization. While there is little evidence relating a specific function for each PKC family member, each subspecies may have a distinct role in the modulation of a variety of cellular responses, thus leading to the observed heterogeneity in PKC-mediated effects.

The primary structure of members of the PKC family consists of a single polypeptide chain (68-83 kDa) containing a regulatory and catalytic domain connected by a trypsin-sensitive hinge region

Regulatory domain

Catalytic domain

Proteolytic cleavage ATP ' binding

Proteolytic ATP cleavage bindin

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