Disease relevance of F9

• In contrast, induced expression of F9 fimbriae in E. coli O157:H7 significantly reduced adherence of the bacteria to bovine gastrointestinal explant tissue [1].
• An abnormal blood coagulation factor IX has been isolated from the blood of a hemophilia B patient with a variant of the disease (hemophilia Bm) characterized by a normal concentration of factor IX antigen, negligible factor IX coagulant activity, and a prolonged prothrombin time with bovine tissue factor [2].
• Hemophilia B or Christmas disease is an X-linked condition caused by absent or reduced levels of functional coagulation factor IX [3].

High impact information on F9

• Coagulation factor IX is a serine protease for which high-level expression of biologically active protein in heterologous cells is limited due to inefficient proteolytic removal of the propeptide as well as vitamin K-dependent carboxylation of multiple amino-terminal glutamic acid residues [4].
• The amino acid sequence of bovine blood coagulation Factor IX (Christmas Factor) is presented and compared with the sequences of other vitamin K-dependent plasma proteins and pancreatic trypsinogen [5].
• Coagulation factor IX is a vitamin K-dependent glycoprotein that circulates in blood as a precursor of a serine protease [6].
• We have used chimeras and point mutations of recombinant coagulation factor IX to examine factor IX's specific interaction with bovine endothelial cells [7].
• Bovine blood coagulation factor IX (Christmas factor) contains four asparagine-linked sugar chains in one molecule [8].

Chemical compound and disease context of F9

• In a previous study, we prepared a monoclonal antibody (MoAb) to coagulation factor IX (FIX), designated 65-10, which interfered with the activation of FIX by the activated factor XI/Ca(2+) and neutralized the prolonged ox brain prothrombin time of hemophilia B(M) [11,12] [9].

Biological context of F9

• Coagulation factor IX residues G4-Q11 mediate its interaction with a shared factor IX/IXa binding site on activated platelets but not the assembly of the functional factor X activating complex [10].

Anatomical context of F9

• Induced expression of the fimbriae, designated F9 fimbriae, was used to characterize binding to bovine epithelial cells, bovine gastrointestinal tissue explants, and extracellular matrix components [1].

Associations of F9 with chemical compounds

• Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm [11].
• The epidermal growth factor (EGF)-like domain of the bovine blood coagulation factor IX (45-87) carrying glucose at Ser(53) was synthesized by a solid-phase method using 9-fluorenylmethoxycarbonyl (Fmoc)-amino acids [12].

Other interactions of F9

• Activation of prekallikrein was also observed with bovine plasmin [EC 3.4.21.7], but not with bovine clotting factors Xa (Stuart factor) [EC 3.4.21.6] and IXa (Christmas factor) or thrombin [EC 3.4.21.5] [13].
• Application of Fmoc-amino acid carrying an unmasked carbohydrate to the synthesis of the epidermal growth factor-like domain of bovine blood coagulation factor IX [12].

Analytical, diagnostic and therapeutic context of F9

• The binding properties of the coagulation factor IX/factor X-binding anticoagulant protein (IX/X-bp) isolated from the venom of Trimeresurus flavoviridis (habu snake) were investigated with an enzyme-linked immunosorbent assay [14].
• Analysis of the far-ultraviolet circular dichroism spectrum of bovine blood coagulation factor IX reveals the presence of approximately 14% helical structures 26% beta-sheets, 20% beta-turns, and 40% coils [15].

References