Protein disulfide isomerase mediates integrin-dependent adhesion

J. Lahav, N. Gofer-Dadosh, J. Luboshitz, O. Hess, M. Shaklai

Research output: Contribution to journalArticlepeer-review


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 β1 and β3 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. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)89-92
Number of pages4
JournalFEBS Letters
Issue number2
StatePublished - 16 Jun 2000


  • Adhesion
  • Collagen
  • Fibrinogen
  • Integrin
  • Platelet
  • Protein disulfide isomerase


Dive into the research topics of 'Protein disulfide isomerase mediates integrin-dependent adhesion'. Together they form a unique fingerprint.

Cite this