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In previous studies, we showed that lacrimal gland acini express three isoforms of protein kinase C (PKC): PKCα,-δ, and -ε. In the present study, we report the identification of two other PKC isoforms, namely PKCμ and -ι/λ. Using immunofluorescence techniques, we showed that these isoforms are differentially located. PKCα and -μ showed the most prominent membrane localization, whereas PKCδ, -ε and -ι/λ were mainly cytosolic. Using cell fractionation and western blotting techniques, we showed that the phorbol ester, phorbol 12, 13-dibutyrate (PdBu, 10−6 m), translocated all PKC isoforms, except PKCι/λ, from the soluble fraction into the particulate fraction. The effect was maximum at 5 min and persisted at 10 min. PKCε was the most responsive to PdBu reaching almost maximal translocation at a PdBu concentration as low as 10−9 m. The cholinergic agonist, carbachol (10−5 and 10−3 m), induced translocation which was transient for PKCδ, and -μ, but persisted for 10 min for PKCε. Carbachol did not translocate PKCα and, like PdBu, did not translocate PKCι/λ. We concluded that lacrimal gland PKC isoforms are differentially localized and that they translocate differentially in response to phorbol esters and cholinergic agonists.
The Journal of Membrane Biology – Springer Journals
Published: May 15, 1997
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