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CD43 regulates tyrosine phosphorylation of a 93-kD protein in T lymphocytes
N Manjunath and B Ardman
Department of Medicine, New England Medical Center Hospitals, Boston, MA,
USA.
The leukocyte sialyloglycoprotein CD43 exhibits features of a signal
transducing molecule and is thought to be important for T-cell activation
and adhesion. However, cellular biochemical events in which CD43
participates remain poorly understood. Here we provide evidence that CD43
regulates tyrosine phosphorylation of a specific substrate in T cells. A
93-kD tyrosine phosphoprotein was identified specifically in the CD43+
T-cell line CEM, but not in their CD43-deficient counterparts derived by
gene targeting. The 93-kD phosphoprotein was detected in the CD43-deficient
CEM cells after transfection with CD43 cDNA, and it could be specifically
phosphorylated in lysates from the CD43-deficient cells by incubation with
a CD43 immunoprecipitate obtained from the CD43+ cells. Expression of CD43
in HeLa cell transfectants was associated with the appearance of novel
phosphoproteins including one with a molecular weight of approximately 93
kD, confirming that tyrosine phosphorylation of cellular substrates results
specifically from CD43 expression. We conclude that CD43 regulates tyrosine
phosphorylation of a 93-kD T-cell substrate.
Volume 86,
Issue 11,
pp. 4194-4198,
12/01/1995
Copyright © 1995 by The American Society of Hematology
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