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(Received for publication, March 14, 1996, and in revised form, April 22, 1996)
From the Department of Medicine, Jack Bell Research Centre,
University of British Columbia, Vancouver,
British Columbia V6H 3Z6, Canada
Phosphatidylinositol (PI) 3-kinase is activated
as a result of cytokine-induced association of the enzyme with specific
tyrosine-phosphorylated proteins. PI 3-kinase lipid products, PI
3,4-P2 and PI 3,4,5-P3, have been shown,
in vitro, to directly activate novel and atypical protein
kinase C (PKC) isozymes. However, the mechanism by which PI 3-kinase
may be involved in regulation of PKC isoforms in vivo is
presently unknown. We investigated a possible relationship by looking
for associations between these enzymes. We found that in a human
erythroleukemia cell line, as well as in rabbit platelets, PI 3-kinase
and PKC
Volume 271, Number 24,
Issue of June 14, 1996
pp. 14514-14518
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Specifically Associates with
Phosphatidylinositol 3-Kinase Following Cytokine Stimulation
associate in a specific manner that is modulated by cell
activation. Granulocyte-macrophage colony-stimulating factor treatment
of cells caused increased association of PKC and PI 3-kinase as did
treatment of platelets with platelet-activating factor. Results using
two PI 3-kinase inhibitors, wortmannin and LY-294002, showed that the
former inhibited this association, while the latter did not, suggesting
that PI 3-kinase lipid products may not be a prerequisite for the PI
3-kinase/PKC association. Our results also suggest that tyrosine
phosphorylation of PKC is not involved in its association with PI
3-kinase.
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