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Intracellular activation of protein kinase C and regulation of the surface transferrin receptor by diacylglycerol is a spontaneously reversible process that is associated with rapid formation of phosphatidic acid

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)

The effect of the synthetic diacylglcerol, sn-1,2-dioctanoylglycerol (diC/sub 8/), on the expression of the surface transferrin receptor reveals that exogenous diC/sub 8/ can act as an intracellular activator of protein kinase C and stimulate both down-regulation and increased receptor phosphorylation in a manner similar to that induced by the active tumor promotor, 4..beta..-phorbol 12,13-dibutyrate. Unlike the spontaneously irreversible effect noted when 4..beta..-phorbol 12,13-dibutyrate is added, this same effect mediated by diC/sub 8/ is brief, lasting only minutes, and is spontaneously reversible. The rate of reversibility is dependent on the concentration of diC/sub 8/ added, and it is associated with rapid formation of a newly detected intracellular phospholipid that corresponds to sn-1,2-dioctanoyl phosphatidic acid. These data, in conjunction with findings that demonstrate that exogenous diacylglycerols (including diC/sub 8/) when added to cells do not stimulate cellular phospholipase A/sub 2/ or C, argue that protein kinase C is activated only briefly in this system since exogenous diC/sub 8/ is subject to rapid intracellular metabolism to phosphatidic acid.

Research Organization:
Johns Hopkins Univ. School of Medicine, Baltimore, MD
OSTI ID:
5402340
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 83:5; ISSN PNASA
Country of Publication:
United States
Language:
English

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