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Volume 271,
Number 13,
Issue of March 29, 1996 pp. 7659-7664
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Signal
Transduction through the 1 Integrin Family Surface Adhesion
Molecules VLA-4 and VLA-5 of Human B-cell Precursors Activates CD19
Receptor-associated Protein-tyrosine Kinases
(Received for publication, October 26, 1995)
Jun
Xiao,
Yoav
Messinger ,
Jizhong
Jin,
Dorothea E.
Myers ,
Joseph B.
Bolen,
Fatih M.
Uckun
We demonstrate that the CD19 receptor associates with the 1
family integrin receptors on human B-cell precursors as well as mature
B-lymphocytes, and engagement of the 1 family integrin receptors
with monoclonal antibody homoconjugates leads to rapid activation of
the CD19-associated protein-tyrosine kinases (PTK) and results in
hyperphosphorylation of CD19 on tyrosine residues. Our findings prompt
the hypothesis that homoconjugate-induced integrin clustering may
effect the approximation and, by intermolecular cross-phosphorylation,
activation of the CD19-associated PTK and subsequent tyrosine
phosphorylation of the CD19 receptor. The ability of the 1 family
integrin receptors to transmit a biochemical signal triggering the
CD19-linked multifunctional PTK pathway provides a possible explanation
for the pleiotropic biologic responses generated through adhesive
VLA-4- and VLA-5-mediated contacts.

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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.
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