Literature DB >> 25851619

Selective disruption of heparin and antithrombin-mediated regulation of human factor IX.

P R Westmark1, P Tanratana2,3, J P Sheehan1.   

Abstract

BACKGROUND: Interaction with antithrombin and heparin regulates distribution, activity, and clearance of factor IXa (FIXa). Hemophilia B prophylaxis targets plasma FIX levels > 1% but neglects extravascular FIX, which colocalizes with antithrombin-heparan sulfate.
OBJECTIVE: Combined mutagenesis of FIX was undertaken to selectively disrupt heparin- and antithrombin-mediated regulation of the protease.
METHODS: Human FIX alanine substitutions in the heparin (K126A and K132A) and antithrombin (R150A) exosites were characterized with regard to coagulant activity, plasma thrombin generation, antithrombin inhibition, and plasma half-life.
RESULTS: Single or combined (K126A/R150A or K132A/R150A) exosite mutations variably reduced coagulant activity relative to wild-type (WT) for FIX (27-91%) and FIXa (25-91%). Double mutation in the heparin exosite (K126A/K132A and K126A/K132A/R150A) markedly reduced coagulant activity (7-21%) and plasma TG. In contrast to coagulant activity, FIX K126A (1.8-fold), R150 (1.6-fold), and K132A/R150A (1.3-fold) supported increased tissue factor-initiated plasma TG, while FIX K132A and K126A/R150A were similar to WT. FIXa K126A/R150A and K132A/R150A (1.5-fold) demonstrated significantly increased FIXa-initiated TG, while FIXa K132A, R150A, and K126A (0.8-0.9-fold) were similar to WT. Dual mutations in the heparin exosite or combined mutations in both exosites synergistically reduced the inhibition rate for antithrombin-heparin. The half-life of FIXa WT in FIX-deficient plasma was remarkably lengthy (40.9 ±1.4 min) and further prolonged for FIXa R150A, K126A/R150A, and K132A/R150A (> 2 h).
CONCLUSION: Selective disruption of exosite-mediated regulation by heparin and antithrombin can be achieved with preserved or enhanced thrombin generation capacity. These proteins should demonstrate enhanced therapeutic efficacy for hemophilia B.
© 2015 International Society on Thrombosis and Haemostasis.

Entities:  

Keywords:  antithrombin III; blood coagulation; factor IX; hemophilia B; heparin

Mesh:

Substances:

Year:  2015        PMID: 25851619     DOI: 10.1111/jth.12960

Source DB:  PubMed          Journal:  J Thromb Haemost        ISSN: 1538-7836            Impact factor:   5.824


  5 in total

1.  Hyperactivity of factor IX Padua (R338L) depends on factor VIIIa cofactor activity.

Authors:  Benjamin J Samelson-Jones; Jonathan D Finn; Lindsey A George; Rodney M Camire; Valder R Arruda
Journal:  JCI Insight       Date:  2019-06-20

2.  Elevated Plasma Factor IXa Activity in Premenopausal Women on Hormonal Contraception.

Authors:  Pansakorn Tanratana; Paul Ellery; Pamela Westmark; Alan E Mast; John P Sheehan
Journal:  Arterioscler Thromb Vasc Biol       Date:  2017-11-02       Impact factor: 8.311

3.  Anticoagulant Protein S Targets the Factor IXa Heparin-Binding Exosite to Prevent Thrombosis.

Authors:  William E Plautz; Vijaya Satish Sekhar Pilli; Brian C Cooley; Rima Chattopadhyay; Pamela R Westmark; Todd Getz; David Paul; Wolfgang Bergmeier; John P Sheehan; Rinku Majumder
Journal:  Arterioscler Thromb Vasc Biol       Date:  2018-02-01       Impact factor: 8.311

Review 4.  Antithrombin and Its Role in Host Defense and Inflammation.

Authors:  Christine Schlömmer; Anna Brandtner; Mirjam Bachler
Journal:  Int J Mol Sci       Date:  2021-04-20       Impact factor: 5.923

Review 5.  New developments in the management of moderate-to-severe hemophilia B.

Authors:  Moniba Nazeef; John P Sheehan
Journal:  J Blood Med       Date:  2016-04-01
  5 in total

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