       Document 0796
 DOCN  M9460796
 TI    Human immunodeficiency virus type 1 interaction with the membrane of
       CD4+ cells induces the synthesis and nuclear translocation of 70K heat
       shock protein.
 DT    9404
 AU    Furlini G; Vignoli M; Re MC; Gibellini D; Ramazzotti E; Zauli G; La
       Placa M; Institute of Microbiology, University of Bologna, St Orsola;
       General Hospital, Italy.
 SO    J Gen Virol. 1994 Jan;75 ( Pt 1):193-9. Unique Identifier : AIDSLINE
       MED/94157462
 AB    In the last few years a growing body of experimental evidence has
       indicated that the interaction of human immunodeficiency virus type 1
       (HIV-1) surface glycoprotein (gp120) with the membrane of CD4+ cells may
       deliver negative signals, eventually leading to programmed cell death
       (apoptosis) of either mature CD4+ lymphocytes or CD34+ haematopoietic
       progenitor cells, in the absence of cell infection with HIV-1. However,
       information on the possible activation of the classical signal
       transduction pathway through gp120 engagement of cell surface CD4 is
       contradictory. Heat shock proteins (hsp) or 'stress' proteins' are
       involved in protecting cells from the deleterious effects of heat and
       other stresses and perform various cell roles. In mammalian cells there
       is evidence that hsp70 is involved in the transport of proteins to
       lysosomes, mitochondria and the nucleus. The results obtained in our
       study demonstrate that early (3 h) after the exposure of permissive CD4+
       cells to HIV-1 (or to purified recombinant gp120) a peak of increased
       synthesis and nuclear translocation of a 70K hsp (and possibly other
       proteins) is observed. These data indicate that gp120 possesses the
       capacity to trigger a cascade of events through a transmembrane
       signalling activity.
 DE    Apoptosis/PHYSIOLOGY  Biological Transport  Cell
       Membrane/METABOLISM/MICROBIOLOGY  Cell Nucleus/*METABOLISM  Cells,
       Cultured  Heat  Heat-Shock Proteins/*METABOLISM  Human  HIV Envelope
       Protein gp120/PHYSIOLOGY  HIV-1/*PHYSIOLOGY  Signal
       Transduction/*PHYSIOLOGY  Support, Non-U.S. Gov't  T4
       Lymphocytes/METABOLISM/*MICROBIOLOGY  JOURNAL ARTICLE

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

