Abstract
Investigations with protein kinase C (PKC) isoform-specific antisera, revealed distinct profiles of PKC isoform content amongst pituitary tissues. Western analysis revealed the α β δ ε ζ and θ isoforms of PKC are present in rat anterior and posterior pituitary tissue as well as in the GH3 somatomammotrophic cell line. AtT-20/D16-V corticotrophic and α T3-1 gonadotrophic murine cell lines contained no PKC-δ. The γ or η isoforms were undetected in any pituitary tissue. PKC activity measurements revealed Ca2+-independent PKCs in αT3-1 and GH3 cells which were more sensitive to activation by phorbol-dibutyrate (PDBu) than the corresponding PKC activity found in COS cells. However, Ca2+-dependent PKC activities were of similar sensitivity to PDBu in GH3, αT3-1 and COS cells, indicating that functional differences observed in PDBu-sensitivity in these cells may be due to differential activation of Ca2+-independent PKC isoforms. Moreover, substrate-specificity of these PKCs were also compared indicating that the amount of Ca2+-dependency of the observed PKC activity from the same pituitary tissue is dependent upon the substrate utilized by the PKC isotypes present. These findings explain differential sensitivities of PKC-mediated actions that have previously been observed in a range of pituitary cells. (Mol Cell Biochem 000-000, 1999)
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MacEwan, D., Johnson, M. & Mitchell, R. Protein kinase C isoforms in pituitary cells displaying differential sensitivity to phorbol ester. Mol Cell Biochem 202, 85–90 (1999). https://doi.org/10.1023/A:1007090718274
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DOI: https://doi.org/10.1023/A:1007090718274