Blood Clotting

Blood Clotting

HRF, INC.

 

Factor V

Factor V is a form of the protein of the coagulation system that is usually referred to as a labile or proaccelerin factor. However, in contrast to most of other coagulation factors, this form of the component is not enzymatically active, but it tends to function as a cofactor. The deficiency of V factor component leads to predisposition for hemorrhage. Besides that, it is also argued that some mutations such as Factor v Leiden predispose to thrombosis^[1].

Factor VII

This is a form of blood coagulation factor Villa that is usually activated blood coagulation factor VII that was previously regarded as proconvertin which is one of the proteins that causes blood to clot in the coagulation cascade. Furthermore, this component is said to be an enzyme of the serine protease class. A recombinant form of human factor Villa is composed of U.S Food and Drug Administration approval for uncontrolled bleeding in the case of hemophilia patients. The component in some instances is also applied in unlicensed in severe uncontrollable bleeding. However; various forms of safety concerns have also been addressed^[2].

Factor VIII

This is a form of a component that is important in blood-clotting protein. The component is also referred to as the anti hemophilic factor. In human beings, this factor(Factor VIII) is usually encoded using F8 gene. The defects as a result of these genes usually result in hemophilia A, a recessive X-linked coagulation disorder. The component is produced in liver sinusoidal cells and also the endothelial cells that exist outside the liver in the entire body. Furthermore, this form of protein circulates in the blood stream using the inactive form that is bound to another molecule that is known as von Willebrand factor. This happens until an injury that damages blood vessels occurs.

Factor IX

This factor belongs to the family of peptidase S1.In many cases, the deficiency of this form of protein component leads to hemophilia B.This component was established in the year 1952 when a young kid by name Stephen Christmas lacked this form of the factor that led to the existence of hemophilia in his health status. This factor is usually produced by zymogen which is a form of inactive precurse that is processed to extract signal peptide, glycosylated and then being cleared by factor Xlla^[3].

Factor X

This form of the factor is also called eponym or Stuart-Prower factor which is an enzyme of the coagulation cascade. This protein exists as serine ednopeptidase that belongs to protease group S1, the PA clan. This factor is usually developed in the liver and also needs the presence of vitamin k for the synthesis to take place. Regarding the structure of this form of protein, the protein was deposited in 1993.However, up to date,191 crystal structures of this facts in conjunction with inhibitors have been developed in the protein data bank^[4].

Factor X1

This protein is also regarded as plasma thromboplastin antecedent that exists in the zymogene form of factor Xlla which is one of the enzymes that is needed in the coagulation cascade. This is like any other coagulation components. In human beings, this component is usually encoded using the F11 gene. Besides that, the factor (Fx1) is normally yielded by the liver and moves as homo-dimer in its inactive state. The half-life of plasma Fx1 is usually fifty-two hours. The zymogene factor is usually activated by factor Xlla by factor Xlla thrombin and Fxla itself.However,due to the inactivity state,FXI emerges to be a member of the contact pathway. When focusing on the structure, every chain in this structure is composed of a relative molecular mass of about 80000.A typical plasma concentrations of Fx1 are normally about 5ug/ml which corresponds to a plasma concentration of about 30nM^[5].

Factor XII

This is a form of the protein component that is also regarded to as coagulation factor XII or Hageman factor. This exists as a form of plasma protein. The protein exists as a form of zymogen form of factor Xlla, which is an enzyme of the serine protease class. However, in humans, the factor is encoded using the F12 genes. In terms of the structure of the Factor XII protein, it is composed of 596 amino acids long and also composed of two domains which are the heavy chains and the light chains that are held together using disulfide bond, The protein F xii is also composed of about 80,000 daltons and the heavy chains also contains two fibronectin type domains and two peridermal growth factor-like domains and also the kringle domains. Regarding the functionality, factor xII is part of the coagulation cascade and activates factor XI and prekallikrein into vitro^[6].Besides that, this factor is also activated by factor Xlla using negatively charged regions such as the glass. In laboratory studies, this factor can also be used to initialize coagulation cascades. Regarding the role of this factor when focusing on the diseases, Factor XII deficiency is usually the rare disorder that is inherited in an autosomal recessive method^[7].

HRF, INC. provides all of these specialty blood plasma products and while they are located in the United States, they do have many European clients from Spain, France, England, Germany, as well as other regions including Asia and Latin America.

 

 

 

References List

Almeida, Alzira Maria Paiva de, and Nilma Cintra Leal. Advances In Yersinia Research. New York: Springer, 2012.

Clemons, Karl V, Rafael Laniado-Laborin, and David A Stevens. Coccidioidomycosis. Boston, Mass.: Published by Blackwell Pub. on behalf of the New York Academy of Sciences, 2007.

Sonenshine, Daniel, E. “Molecular Characterization And Related Aspects Of The Innate Immune Response In Ticks”. Frontiers in Bioscience Volume, no. 13 (2008): 7046.

YE, P. “Naked DNA Transfer Of Factor VIII Induced Transgene-Specific, Species-Independent Immune Response In Hemophilia A Mice”. Molecular Therapy (2004).

 

^[1] Alzira Maria Paiva de Almeida and Nilma Cintra Leal, Advances In Yersinia Research (New York: Springer, 2012).

^[2] Alzira Maria Paiva de Almeida and Nilma Cintra Leal, Advances In Yersinia Research (New York: Springer, 2012).

^[3] Karl V Clemons, Rafael Laniado-Laborin and David A Stevens, Coccidioidomycosis (Boston, Mass.: Published by Blackwell Pub. on behalf of the New York Academy of Sciences, 2007)

^[4] Karl V Clemons, Rafael Laniado-Laborin and David A Stevens, Coccidioidomycosis (Boston, Mass.: Published by Blackwell Pub. on behalf of the New York Academy of Sciences, 2007)

^[5] Daniel, E. Sonenshine, “Molecular Characterization And Related Aspects Of The Innate Immune Response In Ticks”, Frontiers in Bioscience Volume, no. 13 (2008): 7046.

^[6] Daniel, E. Sonenshine, “Molecular Characterization And Related Aspects Of The Innate Immune Response In Ticks”, Frontiers in Bioscience Volume, no. 13 (2008): 7046.

^[7] P YE, “Naked DNA Transfer Of Factor VIII Induced Transgene-Specific, Species-Independent Immune Response In Hemophilia A Mice”, Molecular Therapy (2004).