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Thromb Haemost 2009; 101(05): 840-844
DOI: 10.1160/TH08-09-0605
Blood Coagulation, Fibrinolysis and Cellular Haemostasis
Schattauer GmbH

Coagulation factor XIII serves as protein disulfide isomerase

Judith Lahav   *
1   Hemostasis Laboratory, Beilinson Hospital, Rabin Medical Center, Petah Tikva, Israel
,
Eli Karniel   *
2   Internal Medicine Department B, Meir Hospital, Kfar Saba, Israel
,
Zsuzsa Bagoly
3   Clinical Research Center, Haemostasis, Thrombosis and Vascular Biology Research Group of the Hungarian Academy of Sciences, University of Debrecen, Medical & Health Science Center, Debrecen, Hungary
,
Vera Sheptovitsky
1   Hemostasis Laboratory, Beilinson Hospital, Rabin Medical Center, Petah Tikva, Israel
,
Rima Dardik
4   Thrombosis and Hemostasis Unit, Sheba Medical Center, Tel Hashomer, Israel
,
Aida Inbal
5   Thrombosis and Hemostasis Unit, Department of Hematology, Beilinson Hospital, Rabin Medical Center, Petah Tikva, and Sackler Faculty of Medicine, Tel Aviv University, Israel
› Author AffiliationsFinancial support: This work was supported in part by the Hungarian National Research Fund Grant (OTKA-NKTH NI>69238).
Further Information

Publication History

Received: 18 September 2008

Accepted after major revision: 12 February 2009

Publication Date:
24 November 2017 (online)

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Summary

Tissue transglutaminase was reported to act as protein disulfide isomerase (PDI). We studied whether plasma transglutaminase – coagulation factor XIII (FXIII) – has PDI activity as well. PDI activity was measured by determining the ability to renature reduced-denatured RNase (rdRNase). We found that FXIII can re-nature rdRNase, with efficiency comparable to commercial PDI. This PDI activity was inhibited by bacitracin. Like tissue transglu-taminase, FXIII-mediated PDI activity is independent of its transglutaminase activity and is located on the A subunit. Surface-associated PDI has been previously shown to catalyse two distinct functions: transnitrosation with subsequent release of intracellular nitric oxide and disulfide bond rearrangement during platelet integrin ligation. Our results imply that FXIII-PDI activity may have a role in platelet function.

Keywords

Factor XIII - PDI - transglutaminase

* These authors contributed equally.


 

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