Leukoregulin-induced translocation of protein kinase C activity in K562 cells

Barnett, S. C. and Evans, C.H. (1988) Leukoregulin-induced translocation of protein kinase C activity in K562 cells. Clinical and Experimental Immunology, 73(3), pp. 505-509. (PMID:2850124) (PMCID:PMC1541748)

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Leukoregulin's effect on biochemical pathways involving Ca2+ was assessed in K562 erythroleukemia cells in which the antitumor lymphokine induces a rapidly reversible increase in plasma membrane permeability. Leukoregulin exposure activates protein kinase C but does not alter levels of phosphoinositol metabolites, calmodulin or cAMP. The activation pattern of protein kinase C differs from that induced by phorbol myristic acid (PMA), a potent activator of protein kinase C. PMA-induced translocation of protein kinase C from the cytosol to the plasma membrane is maximal by 2 min after addition of PMA whereas after leukoregulin treatment protein kinase C translocation reaches a maximum at 2 h. This suggests that leukoregulin activates protein kinase C via a non-classical phosphoinositol pathway as opposed to direct binding to protein kinase C as occurs with PMA. The temporal kinetics of the protein kinase C translocation and the increase in membrane permeability induced by leukoregulin are similar suggesting that phosphorylation of a membrane protein may be involved in the target cell destabilization of the plasma membrane by this lymphokine.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Barnett, Professor Susan
Authors: Barnett, S. C., and Evans, C.H.
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity
Journal Name:Clinical and Experimental Immunology
ISSN (Online):1365-2249

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