Thrombin-Independent Activation of Platelet Factor XIII by Endogenous Platelet Acid Protease

Garry W Lynch; Sharron L Pfueller

doi:10.1055/s-0038-1647498

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1988; 59(03): 372-377
DOI: 10.1055/s-0038-1647498

Original Article

Schattauer GmbH Stuttgart

Thrombin-Independent Activation of Platelet Factor XIII by Endogenous Platelet Acid Protease

Authors

Garry W Lynch

The Monash University Department of Medicine, Alfred Hospital, Prahran, Victoria Australia
Sharron L Pfueller

The Monash University Department of Medicine, Alfred Hospital, Prahran, Victoria Australia

Abstract

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Summary

Platelets contain factor XIII, an A subunit zymogen form of transglutaminase (TGase), that is activated by thrombin. In addition a thrombin-independent TGase (A^#) was observed. A^# was formed in platelet preparations lysed at acid pH, and its generation inhibited by protease inhibitors and alkaline pH. When maximal A^# activity was generated in acidified lysates no further TGase activity could be induced by subsequent treatment with thrombin. Both FXIII zymogen and A^# copurified as for F XIII, from either alkaline or from acidified platelet lysates respectively, by the conventional procedure. The pH optima, Km’s for NN dimethyl casein, molecular weights, heat lability of active forms, requirements for calcium and reducing agents, and immunological characteristics of both TGases were the same. Studies with inhibitor substrates suggested that a thrombin-like cathepsin C or carboxypeptidase was responsible for A^# formation. Purified F XIII zymogen could be activated directly by cathepsin C. Thus, the predominant, and probably only, TGase of platelets is factor XIII, which may be activated either by thrombin or by endogenous platelet acid protease(s).

Keywords

Platelet factor XIII - Transglutaminase - Acid protease - Cathepsin

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References

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