       Document 0621
 DOCN  M9640621
 TI    Adhesion of human neuroblasts to HIV-1 tat.
 DT    9604
 AU    Cornaglia-Ferraris P; De Maria A; Cirillo C; Cara A; Alessandri G;
       Department of Pediatric Hematology/Oncology, G. Gaslini; Children's
       Hospital, Genoa, Italy.
 SO    Pediatr Res. 1995 Nov;38(5):792-6. Unique Identifier : AIDSLINE
       MED/96124129
 AB    Several neuropathologic findings in infants and children with human
       immunodeficiency virus type-1 (HIV-1) infection are different from those
       observed in adults, probably related to the fact that the retroviral
       infection occurs in the setting of neuro-development. This report
       describes the interaction and biologic activity of tat, the HIV-1
       trans-activating protein on human neuroblasts. Two human neuroblastoma
       cell lines, LAN-5 and GI-CA-N, have been studied for their capability to
       adhere to tat (full recombinant protein) and to two different peptide
       residues of it. Both cells adhere to tat and tat46-60 basic domain,
       although not to tat65-80 residue, which contains the RGD
       (arginine-glycine-aspartic acid) motif. Adhesion to collagen I was
       inhibited by preincubating GI-CA-N cells with tat,46-60 although not
       with tat,65-80 indicating the capability of the basic residue to
       interfere with collagen I-induced cellular adhesion. The expression of
       200-kD neurofilaments induced by collagen I was not induced by tat,46-60
       indicating that neural differentiation along the same pathway is not
       mimicked by this peptide. Neuroblast cell proliferation was not affected
       by adhesion to tat46-60 nor to tat.65-80 GI-CA-N cells are not
       permissive to HIV-1 infection. However, proviral DNA was documented in
       the cell lysate for 14 consecutive in vitro passages, whereas HIV-1
       transcription was never detectable. This would exclude the possibility
       that tat would be transduced by these cells. GI-CA-N stained negative
       for CD4, although positive for Gal-C, which may explain HIV-1 entry.
       Results show that immature human neural cells interact with tat protein
       and/or its basic residue in vitro. A mechanism similar to that herein
       described would possibly be active in vivo, which may help in clarifying
       the pathogenic mechanisms of neurologic dysfunction and destruction of
       the CNS observed in infants infected with HIV-1.
 DE    Amino Acid Sequence  Cell Adhesion  Cell Division  Extracellular
       Matrix/METABOLISM  Gene Products, tat/*METABOLISM  Human
       HIV-1/*METABOLISM  Integrins/METABOLISM  Molecular Sequence Data
       Neurofilament Proteins/METABOLISM  Neurons/*VIROLOGY  Protein Binding
       Structure-Activity Relationship  Tumor Cells, Cultured  JOURNAL ARTICLE

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

