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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred


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Coagulation factor XIII variants with altered thrombin activation rates

Mette Dahl Andersen1 / Marianne Kjalke1 / Susanne Bang1 / Inger Lautrup-Larsen2 / Peter Becker1 / Asser Sloth Andersen2 / Ole Hvilsted Olsen1 / Henning R. Stennicke1

1Biopharmaceutical Research Unit, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark

2Diabetes Research Unit, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark

Corresponding author

Citation Information: Biological Chemistry. Volume 390, Issue 12, Pages 1279–1283, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2009.142, October 2009

Publication History

Received:
2009-04-23
Accepted:
2009-08-17
Published Online:
2009-10-06

Abstract

Coagulation factor XIII (FXIII) is activated by thrombin and catalyses crosslinking between fibrin monomers thereby providing mechanical strength to the fibrin network. V34L is a common FXIII-A polymorphism found in the activation peptide. FXIII-A V34L is activated faster by thrombin and provides formation of a tighter clot at fibrinogen concentrations in the low end of the physiological range. FXIII-A variants with potentially increased activation rates were generated. Introduction of an optimal thrombin cleavage site, V34L+V35T, increased the activation rate 7.6-fold and facilitated the formation of a fibrin network more resistant to fibrinolysis than obtained with wt FXIII-A. In contrast, introduction of fragments of fibrinopeptide A into the activation peptide resulted in severely impaired activation rates.

Keywords: enzyme activation; factor XIII; factor XIII activation peptide; thrombin

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