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Receptor tyrosine kinase stimulates cell-matrix adhesion by
phosphatidylinositol 3 kinase and phospholipase C-gamma 1 pathways
T Kinashi, JA Escobedo, LT Williams, K Takatsu and TA Springer
Department of Immunology, University of Tokyo, Japan.
Receptor tyrosine kinases are known to be important in growth and
differentiation. We have recently found that c-kit, the tyrosine kinase
receptor for steel factor, also regulates cell-matrix adhesion. Because
Steel factor helps regulate cell migration and localization, this may be an
important biologic function. Integrin adhesiveness is regulated within
minutes by c-kit. The signaling pathways for tyrosine kinase stimulation of
integrin adhesiveness and their relation to pathways that regulate growth
and differentiation over much longer time periods remain uncharacterized.
We have studied the effector pathways by which receptor tyrosine kinases
regulate cell-matrix adhesion using wild-type and mutant forms of the
platelet-derived growth factor (PDGF) receptor, which is closely related to
c-kit. The PDGF receptor expressed in mast cells is as potent as c-kit in
stimulating adhesion to fibronectin. We show that induction of adhesion is
regulated through two independent pathways of phosphatidylinositol 3 kinase
(PI3K) and phospholipase C- gamma 1 (PLC gamma)-protein kinase C by
elimination of autophosphorylation sites required for activation of PI3K
and PLC gamma or in combination with downregulation of protein kinase C or
wortmannin. By contrast, a receptor mutated in both the PI3K and PLC gamma
association sites can still stimulate mast cell growth, indicating a
crucial role of these effector molecules in regulating adhesion rather than
cell growth.
Volume 86,
Issue 6,
pp. 2086-2090,
09/15/1995
Copyright © 1995 by The American Society of Hematology
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