Glycoprotein IX

Wright S. D., Michaelides K., Johnson D. J. D., West N. C., Tuddenham E. G. D. Double heterozygosity for mutations in the platelet glycoprotein IX gene in threee siblings with Bemard-Soulier syndrome. Blood 1993 81,2339-47. 

Hickey MJ, Deaven LL, Roth GJ. Human platelet glycoprotein IX Characterization of cDNA and localization of the gene to chromosome 3. FEBS Lett. 1990 274 189-192. 

Miisd>ek L, Ltposata M Glycoprotrin Ib and glycoprotein IX in human platelets are acylated with palmitic acid through thioester linkages. JBiol Chem 1989 264 9716-9. 

Sdiidc PK, Walker J. The acylation of megakaryocyte proteins glycoprotein IX is primarily myristoylated while glycoprotein Ib is palmitoylated. Blood 1996 87 1377-84. 

NodaM, FujiimiraK, TakaliitaT, Shimomura T, Fuji T, Katsutani S, Fujimoto T, Kuramoto A, Yamazaki T, Mochizuki T, Matsuzaki M, Sano M. A point mutation in glycoprotein IX coding sequence (Cys73 (TGI) to ly TAT)) causes impaired surface expression of GPIb/IX V ccanplex in two families with Bemard-Soulier syi cane. Thromb Haemost 1996 76 874-8. 

Burgess K,Lopez A,GaudryLE, Chong BH Rifampicin-dependent antibodies bind a similar or identical epitope to glycoprotein IX-specific quinine-dependent antibodies. Blood 2000 95 1988-92. 

Coagulation Factors II, III, VII, IX, X, XI, and Xlla fragments, thrombin, and plasmin are classified as serine proteases because each possesses a serine residue with neighboring histidine and asparagine residues at its enzymatically active site (Table 3). Factors II, VII, IX, and X, Protein C, Protein S, and Protein Z are dependent on the presence of vitamin K [84-80-0] for their formation as biologically functionally active procoagulant glycoproteins. 

Factor VII. This is a vitamin K-dependent serine protease that functions in the extrinsic coagulation pathway and catalyzes the activation of Factors IX and X. Factor VII is present constitutively in the surface membrane of pericytes and fibroblasts in the adventitia of blood vessels, vascular endothehum, and monocytes. It is a single-chain glycoprotein of approximately 50,000 daltons. 

Factor IX. This factor is dependent on the presence of vitamin K for its activity as a biologicaUy functional procoagulant glycoprotein. Factor IX is converted to its active form by XIa in the classic scheme of the intrinsic pathway. However, it can also be activated via interaction with Factor Xa or the complex Factor III plus Factor VII in the presence of calcium. 

The von Willebrand factor (vWf) is a heterogeneous multimeric plasma glycoprotein produced by megakaryocytes and endothelial cells which is found in platelets, plasma and the subendothelium. Subendothelial vWf facilitates platelet adhesion, especially under high shear stress, by binding to glycoprotein GPIb-V-IX, a complex of four leucine-rich repeat proteins on platelets. 

The second ligninolytic enzyme, MnP, has been identified (U), purified and characterized (13-16). MnP is an H O -dependent heme glycoprotein (M -46,000) with an iron protoporphyrin iX prosthetic group. MnP catalyzes the Mn -dependent oxidation of a variety of phenols and phenolic lignin model compounds (6,8.13-15,17). Electronic absorption... 

Kiefel, V., Santoso, S., Kaufmann, E., etal., Autoantibodies against platelet glycoprotein Ib/IX A frequent finding in autoimmune toombocytopenic purpura. Br.J. Haematol. 79,256-262 (1991). 

BeneFIX (Nonacog alfa) Wyeth [CHO-expressed glycoprotein-recombinant human coagulation factor IX]... 

IX Christmas Factor MW 47kD single-chain glycoprotein absence - Hemophilia B. 

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