A role for the thiol isomerase. protein ERP5 in platelet function

Jordan, P. A., Stevens, J. M., Hubbard, G. P., Barrett, N. E. ORCID: https://orcid.org/0000-0001-9123-1100, Sage, T., Authi, K. S. and Gibbins, J. M. ORCID: https://orcid.org/0000-0002-0372-5352 (2005) A role for the thiol isomerase. protein ERP5 in platelet function. Blood, 105 (4). pp. 1500-1507. ISSN 0006-4971 doi: 10.1182/blood-2004-02-0608

Abstract/Summary

Formation and rearrangement of disulfide bonds during the correct folding of nascent proteins is modulated by a family of enzymes known as thiol isomerases, which include protein disulfide isomerase (PDI), endoplasmic reticulum protein 5 (ERP5), and ERP57. Recent evidence supports an alternative role for this family of proteins on the surface of cells, where they are involved in receptor 'remodeling and recognition. In platelets, blocking PDI with inhibitory antibodies inhibits a number of platelet activation pathways, including aggregation, secretion, and fibrinogen binding. Analysis of human platelet membrane fractions identified the presence of the thiol isomerase protein ERP5. Further study showed that ERP5 is resident mainly on platelet intracellular membranes, although it is rapidly recruited to the cell, surface in response to a range of platelet agonists. Blocking cell-surface ERP5 using inhibitory antibodies leads to a decrease in platelet aggregation in response to agonists, and a decrease in fibrinogen binding and P-selectin exposure. It is Possible that this is based on the disruption of integrin function, as we observed that ERP5 becomes physically associated with the integrin beta(3) subunit during platelet stimulation. These results provide new insights into the involvement of thiol isomerases and regulation of platelet activation. (C) 2005 by The American Society of Hematology.

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Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/10344
Item Type	Article
Refereed	Yes
Divisions	Life Sciences > School of Biological Sciences
Uncontrolled Keywords	CATALYZED DISULFIDE EXCHANGE, FREE-FLOW ELECTROPHORESIS, CELL ADHESION, MOLECULE-1, PLASMA-MEMBRANE, INTEGRIN ALPHA(IIB)BETA(3), PROTEINDISULFIDE ISOMERASE, TYROSINE PHOSPHORYLATION, ENDOPLASMIC-RETICULUM, ACTIVATED PLATELETS, SURFACE EXPRESSION
Additional Information	The full text of this article is freely available via Pubmed using the link supplied below at Related URLs.
Publisher	American Society of Hematology
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