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The role of Protein Disulfide Isomerase and thiol bonds modifications in activation of integrin subunit alpha11.

Authors :
Popielarski M
Ponamarczuk H
Stasiak M
Michalec L
Bednarek R
Studzian M
Pulaski L
Swiatkowska M
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2018 Jan 08; Vol. 495 (2), pp. 1635-1641. Date of Electronic Publication: 2017 Dec 02.
Publication Year :
2018

Abstract

Integrins belong to a family of transmembrane receptors that mediate cell migration and adhesion to ECM. Extracellular domains of integrin heterodimers contain cysteine-rich regions, which are potential sites of thiol-disulfide exchanges. Rearrangements of extracellular disulfide bonds regulate activation of integrin receptors by promoting transition from an inactive state into a ligand-binding competent state. Modifications of integrin disulfide bonds dependent on oxidation-reduction can be mediated by Protein Disulfide Isomerse (PDI). This paper provides evidences that binding to integrin ligands initiate changes in free thiol pattern on cell surface and that thiol-disulfide exchange mediated by PDI leads to activation of integrin subunit α11. By employing co-immunoprecipitation and confocal microscopy analysis we showed that α11β1 and PDI create complexes bounded by disulfide bonds. Using surface plasmon resonance we provide biochemical evidence that PDI can interact directly with integrin subunit α11.<br /> (Copyright © 2017 Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1090-2104
Volume :
495
Issue :
2
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
29203246
Full Text :
https://doi.org/10.1016/j.bbrc.2017.11.186