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The purpose of this study is to investigate safety and efficacy of prophylactic fibrinogen infusion in patients with fibrinogen levels in lower normal range undergoing coronary artery bypass grafting (CABG).
Primary effect variables is efficacy of fibrinogen infusion on number of transfusions with blood products during hospital stay. Secondary effects variables are effects of fibrinogen on bleeding volume after surgery, postoperative haemoglobin levels 12 and 24 hours after surgery, pharmacoeconomic effects, and effects of fibrinogen infusions on laboratory variables assessing global hemostasis, coagulation, fibrinolysis and platelet function.
Allocation: Randomized, Control: Placebo Control, Endpoint Classification: Safety/Efficacy Study, Intervention Model: Crossover Assignment, Masking: Double Blind (Subject, Caregiver, Investigator), Primary Purpose: Prevention
Cardiothoracic Surgery unit, Sahlgrenska University Hospital
Sahlgrenska University Hospital, Sweden
Published on BioPortfolio: 2014-08-27T03:19:43-0400
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Fibrinogen denaturation is an important phenomenon in biology and medicine. It has been previously investigated with bulk methods and characterized by parameters, which refer to big protein ensembles....
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Receptors that bind FIBRINOGEN through distinct adhesive sequences on the fibrinogen molecule. Although MACROPHAGE-1 ANTIGEN is considered an important signaling molecule for fibrinogen interaction, a variety of INTEGRINS from all three major families, (beta1, beta2, and beta3) have been shown to bind fibrinogen.
Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products.
Clotting time of PLASMA mixed with a THROMBIN solution. It is a measure of the conversion of FIBRINOGEN to FIBRIN, which is prolonged by AFIBRINOGENEMIA, abnormal fibrinogen, or the presence of inhibitory substances, e.g., fibrin-fibrinogen degradation products, or HEPARIN. BATROXOBIN, a thrombin-like enzyme unaffected by the presence of heparin, may be used in place of thrombin.
Fibrinogens which have a functional defect as the result of one or more amino acid substitutions in the amino acid sequence of normal fibrinogen. Abnormalities of the fibrinogen molecule may impair any of the major steps involved in the conversion of fibrinogen into stabilized fibrin, such as cleavage of the fibrinopeptides by thrombin, polymerization and cross-linking of fibrin. The resulting dysfibrinogenemias can be clinically silent or can be associated with bleeding, thrombosis or defective wound healing.
Soluble protein fragments formed by the proteolytic action of plasmin on fibrin or fibrinogen. FDP and their complexes profoundly impair the hemostatic process and are a major cause of hemorrhage in intravascular coagulation and fibrinolysis.
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