Document 0417
 DOCN  M9550417
 TI    Human immunodeficiency virus protein gp120 interferes with
       beta-adrenergic receptor-mediated protein phosphorylation in cultured
       rat cortical astrocytes.
 DT    9505
 AU    Bernardo A; Patrizio M; Levi G; Petrucci TC; Laboratory of Cell Biology,
       Istituto Superiore di Sanita, Roma,; Italy.
 SO    Cell Mol Neurobiol. 1994 Apr;14(2):159-73. Unique Identifier : AIDSLINE
       MED/95144734
 AB    1. We have previously shown that acute exposure to the HIV coat protein
       gp120 interferes with the beta-adrenergic regulation of astroglial and
       microglial cells (Levi et al., 1993). In particular, exposure to 100 pM
       gp120 for 30 min depressed the phosphorylation of vimentin and glial
       fibrillary acidic protein (GFAP) induced by isoproterenol in rat
       cortical astrocyte cultures. In the present study we have extended our
       analysis on the effects of gp120 on astroglial protein phosphorylation.
       2. We found that chronic (3-day) treatment of the cells with 100 pM
       gp120 before exposure to isoproterenol was substantially more effective
       than acute treatment in depressing the stimulatory effect of the
       beta-adrenergic agonist on vimentin and GFAP phosphorylation. 3. Even
       after chronic treatment with gp120, no differences were found in the
       levels and solubility of these proteins. 4. Besides stimulating the
       phosphorylation of intermediate filament proteins, isoproterenol
       inhibited the incorporation of 32P into a soluble acidic protein of
       80,000 M(r), which was only minimally present in Triton X-100-insoluble
       extracts. 5. Treatment of astrocytes with a phorbol ester or exposure to
       3H-myristic acid indicated that the acidic 80,000 M(r) protein is a
       substrate for protein kinase C (PKC) and is myristoylated, thus
       suggesting that it is related to the MARCKS family of PKC substrates. 6.
       Acute (30-min) treatment with 100 pM gp120 totally prevented the
       inhibitory effect of isoproterenol on the phosphorylation of the 80,000
       M(r) MARCKS-like protein. 7. Our studies corroborate the hypothesis that
       viral components may contribute to the neuropathological changes
       observed in AIDS through the alteration of signal transduction systems
       in glial cells.
 DE    Animal  Astrocytes/*METABOLISM  Cells, Cultured  Cerebral
       Cortex/METABOLISM  Glial Fibrillary Acidic Protein/METABOLISM  HIV
       Envelope Protein gp120/*METABOLISM  HIV-1/*METABOLISM  Phosphorylation
       Proteins/METABOLISM  Rats  Receptors, Adrenergic, beta/*METABOLISM
       Support, Non-U.S. Gov't  Vimentin/METABOLISM  JOURNAL ARTICLE

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