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1994-09-05
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Document 0859
DOCN M9480859
TI Role of Ca(++)-dependent and Ca(++)-independent protein kinase C
isozymes on activation of HIV-1.
DT 9410
AU Kim C; Lim S; Gollapudi S; Gupta S; University of California, Irvine.
SO Abstr Gen Meet Am Soc Microbiol. 1994;94:483 (abstract no. T-6). Unique
Identifier : AIDSLINE ASM94/94313086
AB Protein kinase C (PKC) plays a crucial role in HIV-1 replication.
Because of the recognized molecular and biochemical heterogeneity of
PKC, we have studied the effects of various PKC isozyme agonists on
HIV-1 activation in chronically infected promonocytic U1 cells that
produce minimal or no virus. U1 cells were incubated with various
concentrations of 12-deoxyphorbol 13-phenylacetate (dPP),
12-deoxyphorbol 13-phenylacetate 20-acetate (dPPA), and thymeleatoxin
(TT) for various time periods and viral production was measured by
reverse transcriptase and HIV-1 p24 antigen ELISA assays. dPP, a broad
PKC isozyme agonist of both Ca(++)-dependent (PKC alpha, PKC beta, and
PKC gamma) and Ca(++)-independent PKC isozymes (PKC delta, PKC epsilon,
and PKC zeta), and TT, an agonist of Ca(++)-dependent PKC isozymes, in a
concentration dependent manner induced HIV-1 production. Whereas
12-deoxyphorbol 13-phenylacetate 20-acetate (dPPA), a PKC beta I isozyme
agonist had minimal effect on viral production at these concentration.
This study demonstrates that activation of both Ca(++)-dependent and
Ca(++)-independent PKC isozymes play a role in the activation of latent
HIV-1. Furthermore, PKC beta I appears to have minimal, if any, role in
HIV-1 activation.
DE Calcium/*METABOLISM/PHARMACOLOGY Cell Line Comparative Study
Enzyme-Linked Immunosorbent Assay Human HIV Core Protein
p24/ANALYSIS/BIOSYNTHESIS HIV-1/*GROWTH & DEVELOPMENT
Isoenzymes/*METABOLISM Phorbol Esters/PHARMACOLOGY Protein Kinase
C/*METABOLISM *Virus Activation MEETING ABSTRACT
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).