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(Received for publication, April 15, 1997, and in revised form, July 1, 1997)
From the Departments of This study examines the interactions of
Volume 272, Number 46,
Issue of November 14, 1997
pp. 29380-29389
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
The
v
3 Integrin Regulates
51-mediated Cell Migration toward
Fibronectin
,
,
and
Bone Biology and Osteoporosis
and § Pharmacology, Merck Research Laboratories,
West Point, Pennsylvania 19486
v
3 and
51 in the regulation of cell migration.
Human embryonic kidney (HEK) 293 cells that express
51 endogenously were transfected with
v3 and 3 mutants, and
their attachment and migration to fibronectin (Fn) and vitronectin (Vn)
were measured. An v3 blocking antibody and the v3 ligand cyclic G-Pen-GRGDSPC-A
inhibited 51-mediated migration toward
Fn, but not attachment to Fn. This function was v3-specific since
v5 transfection and
v5 blocking antibody did not produce this
effect. Mutations introduced into the 3 integrin subunit
to dissect this phenomenon revealed the following. Disruption of the
ligand binding domain by the Glanzmann thrombasthenia mutation
3-D119Y constitutively abolished migration toward both Vn and Fn, and attachment to Vn but not to Fn. Insertion of the Glanzmann mutation 3-S752P into the cytoplasmic domain
or its truncation (3-
717) abolished binding to Vn but
not to Fn. Inhibition of migration toward Fn was inhibited in these
cells by v3 blocking antibody.
v3-mediated inhibition was, however,
abolished by truncation of the transmembrane domain
(3-693). These findings demonstrate
v3 regulation of
51-mediated cell migration and suggest
that the 3 transmembrane domain is essential for this function.
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