By H. Krebs, W. Schramm (auth.), Professor Dr.med. Inge Scharrer, Professor Dr.med. Wolfgang Schramm (eds.)
This ebook includes the contribution to the thirty sixth Hemophilia Symposium, Hamburg 2005. the most themes are epidemiolgy, hemophilia remedy, orthopedic therapy in hemophiliacs, hemostaseologic prognosis and pediatric hemostaseology. the quantity is rounded off by means of various unfastened papers and posters on hemophilia, inhibitors in hemophilia and diagnostics.
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Additional info for 36th Hemophilia Symposium Hamburg 2005
Schramm Haberland Hafften Hähling Hallek Heine Herold Hesse Höffken Hofmann Holfeld Holstein Horneff Horst Kabus Karl Kemkes-Matthes Kentouche Kiesewetter Kirchmaier Klamroth Klare Klinge Knöfler Köhler-Vajta Körholz Koscielny Kosterij Krebs Kreibich Kretschmer Kreuz Kurnik Lenk Lentz Loreth Maak Meyer Mittler Möller Mondorf Mößeler Niekrens Nimtz-Talaska Notheis Nowak-Göttl Oldenburg Pindur Pollmann Pralle Reiter Ries Scharf Scharrer Schilling Schmeltzer Schneppenheim Schobeß Schramm Schubert Schumacher Siemens Sirb Stuckert Suttorp Syrbe Wedemeyer Weigel Weippert Weisser Wendisch Winkelmann Zimmermann Zintl Development of the German Hemophilia Register B.
Low density lipoprotein receptor-related protein (LRP) mediates the clearance of factor VIII in vWF-deficient mice. Blood 1999; 94: 647a. 11. Turecek PL, Schwarz HP, Binder BR. In vivo inhibition of low density lipoprotein receptorrelated protein improves survival of factor VIII in the absence of von Willebrand factor. Blood 2000; 95: 3637–8. 12. Neels JG, Horn IR, van den Berg BMM, Pannekoek H, van Zonneveld A-J. Ligand-receptor interactions of the low density lipoprotein receptor-related protein, a multi-ligand endocytic receptor.
The high-affinity interaction (Kd ~ 15 nM) between FVIIIa and FIXa is provided by residues 1811-1818 of the A3 domain of LCh . Binding of the A2 domain to FIXa, although with low-affinity (Kd~300 nM), modulates the active site of FIXa and in this way amplifies the enzymatic activity of FIXa by 100-fold . Specifically, the A2 residues 484-509 were shown to be involved in this interaction . The FX-binding site was localized to A1 residues 349-372 of FVIII. Current Knowledge on Receptor-Mediated Catabolism of Factor VIII While the structure and role of FVIII in the functional Xase complex are well characterized, the mechanisms of FVIII turnover remained unknown less than a decade ago.