       Document 0857
 DOCN  M9650857
 TI    [Bovine protein kinase C isotypes transduced into Molt-4/HIV-1 cells
       augment the expression of HIV-1 genome]
 DT    9605
 AU    Izumi T; Department of Microbiology, Hokkaido University School of;
       Medicine, Sapporo, Japan.
 SO    Hokkaido Igaku Zasshi. 1995 Nov;70(6):861-83. Unique Identifier :
       AIDSLINE MED/96143485
 AB    Protein kinase C (PKC) is known to be an ubiquitous enzyme found in a
       variety of mammalian tissue and has been shown to require Ca2+ and
       phospholipid, and to be further activated by diacylglycerol, which
       increased the affinity of the kinase for both Ca2+ and phospholipid. PKC
       is composed with a family of multiple isotypes with closely related
       structures, although the detailed functions of each isotype have not yet
       been clarified. We tried to clarify the difference of biological
       functions among the isotypes of PKC. Three PKC isotypes (alpha, beta 1,
       gamma) were purified from bovine brain by L-threonine-Sepharose affinity
       column, and fractions containing alpha and beta 1 forms (Peak A) and
       gamma form (Peak B) were obtained. Each peak integrated into
       erythrocytic ghost was transduced into cells persistently infected with
       HIV-1 (Molt-4/HIV-1) by fusion method. Peak A containing PKC alpha and
       beta 1 isotypes induced TNF-alpha production, HIV-1 cDNA titer and P24
       antigen in culture of Molt-4/HIV-1 cells, but Peak B containing PKC
       gamma did not show any effects on Molt-4/HIV-1 cells. The effect of PKC
       alpha and beta 1 on the production of TNF-alpha and the augmentation of
       HIV-1 replication are inhibited by both anti-TNF-alpha antibody and
       staurosporine, a potent PKC inhibitor.
 DE    Animal  Antigens, Viral  Cattle  English Abstract  Erythrocyte Membrane
       *Genome, Viral  HIV-1/*GENETICS/*METABOLISM  Isoenzymes/ISOLATION &
       PURIF/*PHYSIOLOGY  Protein Kinase C/ISOLATION & PURIF/*PHYSIOLOGY  Tumor
       Necrosis Factor/METABOLISM  Virus Replication  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

