Evidence for multiple protein kinase C isoforms in the leukocytes of a marine teleost, Sciaenops ocellatus.

The protein kinase C (PKC) family of isozymes mediates a diverse range of cellular functions, including activation of vertebrate lymphocytes through membrane-bound antigen receptors. The complex role of PKC in mammalian cells may be orchestrated in part by the presence of multiple isoforms, each of which displays a distinctive tissue distribution, substrate specificity and pattern of regulation. In the present study, PKC isoforms were identified in peripheral blood leukocytes of the marine teleost fish Sciaenops ocellatus by immunoprecipitation and Western blot using antibodies to mammalian isoforms. Functional activity was monitored by evaluating translocation of the teleost isoforms from membrane to cytosol in response to phorbol ester treatment. Teleost conventional isoforms PKC alpha and PKC beta (82 kDa) completely translocated out of the cytosol in response to phorbol ester. Phorbol ester did not induce translocation of teleost atypical isoform PKC zeta (67 kDa), as has been shown for its mammalian homologue. Although their identity as distinct isoforms is less clear, proposed teleost novel PKC delta (84, 86 kDa) and PKC eta (83, 85 kDa) also translocated out of the cytosol. The presence of multiple isoforms representing each of the three major classes of PKC in red drum leukocytes implies that the complexity of signal transduction pathways in vertebrates is highly conserved.