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Significance of RGD Loop and C-Terminal Domain of Echistatin for Recognition of  IIb 3 and v3 Integrins and Expression of Ligand-Induced Binding Site
Cezary Marcinkiewicz,
Senadhi Vijay-Kumar,
Mary Ann McLane, and
Stefan Niewiarowski
From the Department of Physiology, Sol Sherry Thrombosis Research Center and Fels Research Institute, Temple University School of Medicine, Philadelphia, PA.
Echistatin is a viper venom disintegrin containing RGD loop maintained by disulfide bridges. It binds with a high affinity to  v 3 and IIb3 and it induces extensive conformational changes in these integrins resulting in expression of ligand-induced binding site (LIBS) epitopes. We investigated the activities of echistatin and its three analogues (R24A, D27W, echistatin 1-41). R24A echistatin did not react with IIb3 and v3 integrins and did not cause LIBS effect. D27W echistatin showed increased binding to IIb3 and decreased binding to v3. This substitution impaired the ability of echistatin to induce LIBS in v3 integrin. Deletion of nine C-terminal amino acids of echistatin decreased its ability to bind IIb3 and inhibit platelet aggregation. Truncated echistatin failed to induce LIBS epitopes on cells transfected with IIb3 and v3 genes. The ability of echistatin 1-41 to compete with binding of vitronectin to immobilized v3 and monoclonal antibody 7E3 to platelets and to VNRC3 cells was decreased, although this analogue, after immobilization, retained its ability to bind purified v3. We propose a hypothesis in which echistatin's RGD loop determines selective recognition of IIb3 and v3 integrin, whereas the C-terminal domain supports its binding to resting integrin and significantly contributes to the expression of LIBS epitope and to conformational changes of the receptor, leading to a further increase of the binding affinity of echistatin and of the inhibitory effect.
Blood, Vol. 90 No. 4 (August 15), 1997:
pp. 1565-1575
© 1997 by The American Society of Hematology.
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