The activation peptide of coagulation factor IX and X serves as a high affinity receptor to cationic ligands

Andreas Griessner; Thomas Zögg; Hans Brandstetter

doi:10.1160/TH13-01-0051

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 2013; 110(03): 620-622
DOI: 10.1160/TH13-01-0051

Letters to the Editor

Schattauer GmbH

The activation peptide of coagulation factor IX and X serves as a high affinity receptor to cationic ligands

Andreas Griessner

¹Department of Molecular Biology, University of Salzburg, Austria

²Current address: Biochemistry Centre (BZH), University of Heidelberg, Germany

,

Thomas Zögg

¹Department of Molecular Biology, University of Salzburg, Austria

,

Hans Brandstetter

¹Department of Molecular Biology, University of Salzburg, Austria

› Author Affiliations

Abstract

Full Text

References

References
1 Lenting PJ, ter Maat H, Clijsters PP. et al. Cleavage at arginine 145 in human blood coagulation factor IX converts the zymogen into a factor VIII binding enzyme. J Biol Chem 1995; 270: 14884-14890.
2 Bode W, Huber R. Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin. FEBS Lett 1976; 68: 231-236.
3 Altieri DC, Etingin OR, Fair DS. et al. Structurally homologous ligand binding of integrin Mac-1 and viral glycoprotein C receptors. Science 1991; 254: 1200-1202.
4 Iino M, Takeya H, Nishioka J. et al. The role of human factor X activation peptide in activation of factor X by factor IXa. J Biochem 1994; 116: 335-340.
5 Johansson L, Karpf DM, Hansen L. et al. Activation peptides prolong the murine plasma half-life of human factor VII. Blood 2011; 117: 3445-3452.
6 Gabriel B, Stubbs MT, Bergner A. et al. Design of benzamidine-type inhibitors of factor Xa. J Med Chem 1998; 41: 4240-4250.
7 Renatus M, Bode W, Huber R. et al. Structural mapping of the active site specificity determinants of human tissue-type plasminogen activator. Implications for the design of low molecular weight substrates and inhibitors. The J Biol Chem 1997; 272: 21713-21719.
8 Zogg T, Brandstetter H. Structural basis of the cofactor- and substrate-assisted activation of human coagulation factor IXa. Structure 2009; 17: 1669-1678.
9 Hopfner KP, Brandstetter H, Karcher A. et al. Converting blood coagulation factor IXa into factor Xa: dramatic increase in amidolytic activity identifies important active site determinants. EMBO J 1997; 16: 6626-6635.
10 Iijima K, Murakami M, Kimura O. et al. A dysfunctional factor X (factor X Kurayoshi) with a substitution of Arg 139 for Ser at the carboxyl-terminus of the light chain. Thromb Res 2001; 101: 311-316.
11 Kim DJ, Thompson AR, Nash DR. et al. Factors XWenatchee I and II: compound heterozygosity involving two variant proteins. Biochim Biophys Acta 1995; 1271: 327-334.
12 Kasai K, Ishii S. Studies on the interaction of immobilized trypsin and specific ligands by quantitative affinity chromatography. J Biochem 1978; 84: 1061-1069.
13 Bergman DA, Winzor DJ. Quantitative affinity chromatography: increased versatility of the technique for studies of ligand binding. Analyt Biochem 1986; 153: 380-386.