Document 0003
 DOCN  M9480003
 TI    Close co-localization of CD4 and a serine esterase tryptase TL2 on the
       cell-surface of human monocytoid and CD4+ lymphoid cells.
 DT    9410
 AU    Inoue M; Hoshino T; Fukuma T; Niwa Y; Kido H; Department of
       Parasitology, Kurume University School of Medicine,; Fukuoka, Japan.
 SO    Biochem Biophys Res Commun. 1994 Jun 30;201(3):1390-5. Unique Identifier
       : AIDSLINE MED/94296414
 AB    Tryptase TL2, a serine esterase in the membrane of human monocytoid and
       CD4+ lymphoid cells, specifically binds to the V3 domain of HIV-1 gp120.
       Here we report that monoclonal antibodies against CD4 that recognize the
       epitope interacting with gp120 specifically blocked the immunostaining
       of cell-surface tryptase TL2, although the antibody does not cross-react
       with tryptase TL2. Down-regulation of cell-surface CD4 induced by HIV-1
       Nef prevented this blocking effect. These data suggest that CD4 is
       closely co-localized with tryptase TL2 on the cell surface and that
       regulation of the expression of tryptase TL2 is not associated with that
       of CD4.
 DE    Antibodies, Monoclonal  Antigens, CD4/*METABOLISM  Cell
       Membrane/ULTRASTRUCTURE  Down-Regulation (Physiology)  Human
       Macromolecular Systems  Monocytes/*ULTRASTRUCTURE  Serine
       Proteinases/*METABOLISM  Support, Non-U.S. Gov't  T4
       Lymphocytes/*ULTRASTRUCTURE  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
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