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Protein disulfide isomerase mediates integrin‐dependent adhesion
Author(s) -
Lahav J.,
Gofer-Dadosh N.,
Luboshitz J.,
Hess O.,
Shaklai M.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01630-6
Subject(s) - integrin , protein disulfide isomerase , chemistry , adhesion , cell adhesion , microbiology and biotechnology , ligand (biochemistry) , biochemistry , receptor , collagen receptor , disulfide bond , biology , organic chemistry
Cell adhesion is mediated by the integrin adhesion receptors. Receptor–ligand interaction involves conformational changes in the receptor, but the underlying mechanism remains unclear. Our earlier work implied a role for sulfhydryls in integrin response to ligand binding in the intact blood platelet. We now show that non‐penetrating blockers of free sulfhydryls inhibit β 1 and β 3 integrin‐mediated platelet adhesion regardless of the affinity state of the integrin. Removal of the inhibitors prior to adhesion fully restores adhesion despite the irreversible nature of inhibitor–thiol interaction, indicating sulfhydryl exposure in response to adhesion. We further show that blocking protein disulfide isomerase (PDI) inhibits adhesion. These data indicate that: (a) ecto‐sulfhydryls are necessary for integrin‐mediated platelet adhesion; (b) disulfide exchange takes place during this process; (c) surface PDI is involved in integrin‐mediated adhesion.