Chemical cross-linking detects different conformational arrangements of platelet integrin alpha IIb beta III (gpIIb/IIIa)

Biochemical and Biophysical Research Communications
K LösterW Reutter

Abstract

Treatment of Triton X-100 solubilized platelet membrane with the homobifunctional cross-linker dithiobis(succinimidyl propionate) resulted in covalent cross-linking of the platelet integrin alpha IIb beta 3 (gpIIb/IIIa), the fibrinogen receptor, into three high-molecular-mass complexes with apparent M of 200, 220 and 240 k. Generation of these cross-linked alpha IIb beta 3 aggregates depended on the presence of a native receptor structure and was not influenced by Ca2+ ions and other experimental conditions. Immunoblotting analysis of purified 200/220/240 kDa aggregates revealed that they were made up exclusively by alpha IIb and beta 3 integrin chains in roughly stoichiometric amounts. We therefore conclude that alpha IIb beta 3 integrin occurs in different conformations in the platelet membrane that can be directly detected by chemical cross-linking.

Citations

Sep 18, 2002·Immunological Reviews·M Amin Arnaout
Jun 8, 2011·Journal of Thrombosis and Haemostasis : JTH·N ManickamD W Essex
Dec 10, 1997·Journal of Chromatography. B, Biomedical Sciences and Applications·K Löster, D Josić
Sep 17, 2002·Current Opinion in Cell Biology·M Amin ArnaoutJian-Ping Xiong

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