6533b854fe1ef96bd12ae017
RESEARCH PRODUCT
Alteration of DNA topoisomerase II activity during infection of H9 cells by human immunodeficiency virus type 1 in vitro: a target for potential therapeutic agents.
A. MaidhofHeinz C. SchröderEckart MatthesBarbara E. WeilerKarin RenneisenP. LangenHans BrachwitzWerner E. G. M�llersubject
T-LymphocytesMitogen-activated protein kinase kinaseIn Vitro TechniquesMAP2K7Cell LineLactonesVirologyAnimalsPhosphorylationProtein kinase AProtein kinase CProtein Kinase CPharmacologybiologyCyclin-dependent kinase 2LysophosphatidylcholinesRats Inbred StrainsDNA topoisomerase II activityBryostatinsProtein kinase RMolecular biologyRatsDNA Topoisomerases Type Ibiology.proteinHIV-1Tetradecanoylphorbol AcetateCyclin-dependent kinase 9Electrophoresis Polyacrylamide GelMacrolidesdescription
Infection of H9 cells with human immunodeficiency virus type 1 (HIV-1) was found to decrease the phosphorylation of DNA topoisomerase II during the initial phase of infection. Simultaneously, with a later overshoot of phosphorylation and the subsequent activation of DNA topoisomerase II, the production of HIV-1 started. Applying three new protein kinase C inhibitors from the class of O-alkylglycerophospholipids we demonstrated that inhibition of protein kinase C-mediated phosphorylation of DNA topoisomerase II resulted in an inhibition of HIV-1 production. Based on the differential effect of the two protein kinase C activators, phorbol ester and bryostatin, we conclude that phosphorylation of DNA topoisomerase II is mediated by the form alpha and gamma of protein kinase C. These data suggest that agents which inhibit these two forms of protein kinase C are also potential candidates for an anti-HIV therapy.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1990-06-01 | Antiviral research |