Coagulation factor XIII variants with altered thrombin activation rates
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Mette Dahl Andersen
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.
©2009 by Walter de Gruyter Berlin New York
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- Acknowledgment
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- Contents Volume 390, 2009
- Contents Biological Chemistry, Volume 390, 2009
- Author Index
- Author Index
- Subject Index
- Subject Index
Articles in the same Issue
- Reviews
- Chemokines in tumor-associated angiogenesis
- The mammalian aryl hydrocarbon (Ah) receptor: from mediator of dioxin toxicity toward physiological functions in skin and liver
- The mechanism of ATP-dependent RNA unwinding by DEAD box proteins
- Protein Structure and Function
- Crystal structure of 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum
- Factors regulating tachyphylaxis triggered by N-terminal-modified angiotensin II analogs
- Cancer Osaka thyroid (Cot) phosphorylates Polo-like kinase (PLK1) at Ser137 but not at Thr210
- Coagulation factor XIII variants with altered thrombin activation rates
- Cell Biology and Signaling
- Stimulation of fibroblast proliferation by the plant cysteine protease CMS2MS2 is independent of its proteolytic activity and requires ERK activation
- EFEMP1 binds the EGF receptor and activates MAPK and Akt pathways in pancreatic carcinoma cells
- Identification of collagen IV derived danger/alarm signals in insect immunity by nanoLC-FTICR MS
- Proteolysis
- Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage
- Acknowledgment
- Acknowledgment
- Contents Volume 390, 2009
- Contents Biological Chemistry, Volume 390, 2009
- Author Index
- Author Index
- Subject Index
- Subject Index
