TY - JOUR
T1 - Close Colocalization of CD4 and a Serine Esterase Tryptase TL2 on the Cell Surface of Human Monocytoid and CD4+ Lymphoid Cells
AU - Inoue, M.
AU - Hoshino, T.
AU - Fukuma, T.
AU - Niwa, Y.
AU - Kido, H.
PY - 1994/6/30
Y1 - 1994/6/30
N2 - 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 crossreact 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.
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 crossreact 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.
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U2 - 10.1006/bbrc.1994.1857
DO - 10.1006/bbrc.1994.1857
M3 - Article
C2 - 7912927
AN - SCOPUS:0028068913
SN - 0006-291X
VL - 201
SP - 1390
EP - 1395
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -
