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J. Cell Biol.,
Volume 143, Number 1, October 5, 1998 241-252
v
3 and
5
1 Integrin Ligands

* Microcirculation Research Institute and Departments of Medical Physiology, Vasoactive effects of soluble matrix proteins
and integrin-binding peptides on arterioles are mediated by
Pathology and Laboratory Medicine,
Texas A & M University Health Science Center, College Station, Texas 77843-1114
v
3 and
5
1 integrins. To examine the underlying mechanisms, we measured L-type Ca2+ channel
current in arteriolar smooth muscle cells in response to
integrin ligands. Whole-cell, inward Ba2+ currents were
inhibited after application of soluble cyclic RGD peptide, vitronectin (VN), fibronectin (FN), either of two
anti-
3 integrin antibodies, or monovalent
3 antibody.
With VN or
3 antibody coated onto microbeads and
presented as an insoluble ligand, current was also inhibited. In contrast, beads coated with FN or
5 antibody
produced significant enhancement of current after bead
attachment. Soluble
5 antibody had no effect on current but blocked the increase in current evoked by FN-coated beads and enhanced current when applied in
combination with an appropriate IgG. The data suggest
that
v
3 and
5
1 integrins are differentially linked
through intracellular signaling pathways to the L-type Ca2+ channel and thereby alter control of Ca2+ influx in
vascular smooth muscle. This would account for the vasoactive effects of integrin ligands on arterioles and
provide a potential mechanism for wound recognition
during tissue injury.
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