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Blood, 15 February 2005, Vol. 105, No. 4, pp. 1500-1507.
Prepublished online as a Blood First Edition Paper on October 5, 2004; DOI 10.1182/blood-2004-02-0608.
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Submitted February 18, 2004
Accepted September 27, 2004
A role for the thiol isomerase protein ERP5 in platelet function
Peter A Jordan, Joanne M Stevens, Gary P Hubbard, Natasha E Barrett, Tanya Sage, Kalwant S Authi, and Jonathan M Gibbins*
School of Animal and Microbial Sciences, University of Reading, Reading, UK
Cardiovascular Division, King's College London, New Hunt's House, Guy's Campus, London, UK
* Corresponding author; email: j.m.gibbins{at}reading.ac.uk.
Formation and rearrangement of disulphide bonds during the correct folding of nascent proteins is modulated by a family of enzymes known as thiol isomerases, which include protein disulphide isomerase (PDI), 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 remodelling 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 mainly resident 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 upon the disruption of integrin function as we observed that ERP5 becomes physically associated with the integrin  3 subunit during platelet stimulation. These results provide new insights into the involvement of thiol isomerases and regulation of platelet activation.
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