The C-terminal acidic region in the A1 domain of factor VIII facilitates thrombin-catalyzed activation and cleavage at Arg<sup>372</sup>
Author:
Affiliation:
1. 奈良県立医科大学血栓止血先端医学講座
Publisher
Japanese Society on Thrombosis and Hemostasis
Subject
General Medicine
Link
https://www.jstage.jst.go.jp/article/jjsth/34/4/34_2023_JJTH_34_4_480-487/_pdf
Reference21 articles.
1. 1) Eaton D, Rodriguez H, Vehar GA: Proteolytic processing of human factor VIII. Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity. Biochemistry 25: 505–512, 1986.
2. 2) Fay PJ, Mastri M, Koszelak ME, et al.: Cleavage of factor VIII heavy chain is required for the functional interaction of a2 subunit with factor IXA. J Biol Chem 276: 12434–12439, 2001.
3. 3) Donath MS, Lenting PJ, van Mourik JA, et al.: The role of cleavage of the light chain at positions Arg1689 or Arg1721 in subunit interaction and activation of human blood coagulation factor VIII. J Biol Chem 270: 3648–3655, 1995.
4. 4) Regan LM, Fay PJ: Cleavage of factor VIII light chain is required for maximal generation of factor VIIIa activity. J Biol Chem 270: 8546–8552, 1995.
5. 5) Fay PJ: Activation of factor VIII and mechanisms of cofactor action. Blood Rev 18: 1–15, 2004.
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