A potential second messenger role for arachidonic acid: activation of Ca2+-dependent protein kinase.

Published

Journal Article

A widely distributed Ca2+- and phospholipid-dependent protein kinase, protein kinase C, may play a major role in cellular regulation. We now report that arachidonate can directly activate protein kinase C from human neutrophils. Activation was Ca2+-dependent and was enhanced by diolein, but did not require phosphatidylserine. Arachidonate enhanced the apparent affinity of the kinase for Ca2+ in the presence of phosphatidylserine. Other unsaturated, but not saturated, fatty acids also activated protein kinase C. These results suggest a novel means of leukocyte activation and cellular regulation: arachidonate, which is released by ligand-receptor interactions in neutrophils and many other cell types, could function as a second messenger via activation and modulation of protein kinase C.

Full Text

Duke Authors

Cited Authors

  • McPhail, LC; Clayton, CC; Snyderman, R

Published Date

  • January 1, 1984

Published In

Volume / Issue

  • 97 /

Start / End Page

  • 222 - 231

PubMed ID

  • 6242084

Pubmed Central ID

  • 6242084

International Standard Serial Number (ISSN)

  • 0066-9458

Language

  • eng