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Literature DB >> 3485425

Translocation of phospholipid/Ca2+-dependent protein kinase in B-lymphocytes activated by phorbol ester or cross-linking of membrane immunoglobulin.

A E Nel, M W Wooten, G E Landreth, P J Goldschmidt-Clermont, H C Stevenson, P J Miller, R M Galbraith.

Abstract

Stimulation of peripheral-blood B-lymphocytes with phorbol ester or anti-immunoglobulin demonstrated intracellular translocation of phospholipid/Ca2+-dependent protein kinase (C-kinase) activity from cytosol to membrane fractions. This phenomenon, which was dose- and time-dependent, was found in both normal and chronic-lymphocytic-leukemia B-cells. This suggests that C-kinase-dependent protein phosphorylation may be related to membrane receptor occupation and may therefore be important in B-lymphocyte responses.

Entities: Chemical Disease

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Year: 1986 PMID： 3485425 PMCID： PMC1152996 DOI： 10.1042/bj2330145

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

30 in total

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14 in total

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7. 12-Deoxyphorbol-13-O-phenylacetate 20 acetate [an agonist of protein kinase C beta 1 (PKC beta 1)] induces DNA synthesis, interleukin-2 (IL-2) production, IL-2 receptor alpha-chain (CD25) and beta-chain (CD122) expression, and translocation of PKC beta isozyme in human peripheral blood lymphocytes: evidence for a role of PKC beta 1 in human T cell activation.

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