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).