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Science 8 November 1991:
Vol. 254. no. 5033, pp. 845 - 847
DOI: 10.1126/science.1948065
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Articles
Science, Vol 254, Issue 5033, 845-847
Copyright © 1991 by American Association for the Advancement of Science
Modulation of the affinity of integrin alpha IIb beta 3 (GPIIb-IIIa) by the cytoplasmic domain of alpha IIb
TE O'Toole,
D Mandelman,
J Forsyth,
SJ Shattil,
EF Plow,
and
MH Ginsberg
Committee on Vascular Biology, Scripps Research Institute, La Jolla, CA 92037.
Intracellular signaling alters integrin adhesive functions in inflammation, immune responses, hemostasis, thrombosis, and retinal development. By truncating the cytoplasmic domain of alpha IIb, the affinity of integrin alpha IIb beta 3 for ligand was increased. Reconstitution with the cytoplasmic domain from integrin alpha 5 did not reverse the increased affinity. Thus, the cytoplasmic domain of the alpha subunit of GPIIb-IIIa controls ligand binding affinity, which suggests mechanisms for inside-out transmembrane signaling through integrins. These findings imply the existence of hitherto unappreciated hereditary and acquired thrombotic disorders in humans.
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