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M9480003.TXT
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1994-08-09
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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
protected by Copyright Law (Title 17, U.S.Code).