AI Article Synopsis
- Integrins are transmembrane receptors that help cells move and stick to the extracellular matrix (ECM), and their activation is regulated by changes in disulfide bonds.
- The research shows that when integrin ligands bind, it triggers alterations in thiol patterns on the cell surface, leading to the activation of integrin subunit α11.
- Tools like co-immunoprecipitation and surface plasmon resonance demonstrated that Protein Disulfide Isomerase (PDI) forms complexes with integrin α11β1 and directly interacts with integrin subunit α11.
Article 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.
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| http://dx.doi.org/10.1016/j.bbrc.2017.11.186 | DOI Listing |
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