fibrin and Blood-Protein-Disorders

Topics: Arteriosclerosis; Aspirin; Blood Platelets; Blood Protein Disorders; Cell Survival; Coronary Disease; Endothelium; Fibrin; Humans; Lipid Metabolism; Lipoproteins; Phagocytosis; Platelet Adhesiveness; Prostaglandins; Pyrazoles; Pyrimidines; Thrombosis

Topics: Adult; Afibrinogenemia; Blood Coagulation; Blood Protein Disorders; Blood Transfusion; Child; Child, Preschool; Factor XIII; Female; Fibrin; Fibrinogen; Glutaminase; Hemorrhage; Humans; Infant, Newborn; Male; Prothrombin Time

Topics: Blood Protein Disorders; Disseminated Intravascular Coagulation; Disulfides; Electrophoresis, Polyacrylamide Gel; Fibrin; Fibrinogen; Fibrinolysis; Humans; Molecular Conformation; Molecular Weight; Peptide Fragments; Streptokinase; Thrombosis; Urokinase-Type Plasminogen Activator; Venoms

Topics: Abdomen; Antibodies; Blood Coagulation Tests; Blood Protein Disorders; Chromatography; Cold Temperature; Diagnosis, Differential; Ecchymosis; Electrophoresis; Factor XIII; Female; Fibrin; Fibrinogen; Hematuria; Hemorrhagic Disorders; Humans; Immunoglobulin G; Isoniazid; Middle Aged; Pain; Sarcoidosis

Topics: Afibrinogenemia; Aged; Blood Coagulation Tests; Blood Platelets; Blood Protein Disorders; Factor VIII; Female; Fibrin; Hemorrhagic Disorders; Humans; Immunoglobulin G; Japan; Male; Middle Aged; Multiple Myeloma; Thromboplastin; Waldenstrom Macroglobulinemia

A dysfibrinogenemia (fibrinogen Bethesda) was detected in a 9 yr old male of Mexican-English extraction who had a lifelong history of mild bleeding diathesis. The prothrombin and partial thromboplastin times were moderately prolonged; the thrombin and Reptilase times were markedly prolonged. The plasma fibrinogen level was normal by conventional methods but was markedly reduced by the Clauss method. Results of all other tests for clotting factors, fibrinolysis, antithrombin levels, clot stabilization, and fibrin(ogen) degradation products were normal. The patient's plasma and fibrinogen inhibited the clotting of normal plasma or fibrinogen by thrombin. Family studies revealed that the propositus' mother and two siblings exhibited these abnormalities to a lesser degree and indicated an autosomal dominant inheritance. Fibrinogen Bethesda was similar to normal fibrinogen in the following respects: metabolic turnover time (measured in the propositus' mother); immunodiffusion, ultracentrifugal, electrophoretic (on cellulose acetate or polyacrylamide gel), and chromatographic (on DEAE-cellulose) characteristics; sialic acid content; and aggregation of fibrin monomers. By contrast, fibrinogen Bethesda gave an abnormal immunoelectrophoretic pattern especially when whole plasma (as opposed to purified fibrinogen) was examined, and it showed a pronounced decrease in the rate of fibrinopeptide release by thrombin. This decrease, which was shown to involve both fibrinopeptides A and B, distinguishes fibrinogen Bethesda from previously reported dysfibrinogenemias.

Topics: Adult; Blood Protein Disorders; Chromatography, DEAE-Cellulose; England; Ethnicity; Fibrin; Fibrinogen; Genes, Dominant; Humans; Immunoelectrophoresis; Male; Mexico; Middle Aged; Molecular Biology; Peptides; Prothrombin Time; Thrombin; Trichloroacetic Acid

The rate of clotting and the rate of development and degree of turbidity after addition of thrombin to plasma or purified fibrinogen from a patient with fibrinogen Baltimore was delayed when compared with normal, especially in the presence of low concentrations of thrombin. Optimal coagulation and development of translucent, rather than opaque, clots occurred at a lower pH with the abnormal fibrinogen than with normal. Development of turbidity during clotting of the abnormal plasma or fibrinogen was less than normal at each pH tested, but was maximal in both at approximately pH 6.4. The physical quality of clots formed from fibrinogen Baltimore was abnormal, as demonstrated by a decreased amplitude on thromboelastography. The morphologic appearance of fibrin strands formed from fibrinogen Baltimore by thrombin at pH 7.4 was abnormal when examined by phase contrast or electron microscopy, but those formed by thrombin at pH 6.4 or by thrombin and calcium chloride were similar to, though less compact, than normal fibrin. The periodicity of fibrin formed from fibrinogen Baltimore was similar to normal and was 231-233 A.A study of the release of the fibrinopeptides from the patient's fibrinogen and its chromatographic subfractions verified the existence of both a normally behaving and a defective form of fibrinogen in the patient's plasma. The defective form differed from normal in three functionally different ways: (a) the rate of release of fibrinopeptides A and AP was slower than normal; (b) no visible clot formation accompanied either partial or complete release of the fibrinopeptides from the defective form in 0.3 M NaCl at pH 7.4; and (c) the defective component possessed a high proportion of phosphorylated, relative to nonphosphorylated, fibrinopeptide A, while the coagulable component contained very little of the phosphorylated peptide (AP). The high phosphate content of the defective component did not appear to be the cause of the abnormality, but may be the result of an associated metabolic or genetic phenomenon.

Topics: Blood Coagulation; Blood Protein Disorders; Blood Protein Electrophoresis; Calcium; Fibrin; Fibrinogen; Humans; Hydrogen-Ion Concentration; Microscopy, Electron; Molecular Biology; Peptides; Thrombelastography; Thrombin

Topics: Adenocarcinoma; Blood Coagulation Disorders; Blood Coagulation Tests; Blood Platelet Disorders; Blood Protein Disorders; Carcinoma; Colonic Neoplasms; Fibrin; Hemostatics; Humans; Immunoelectrophoresis; Kidney Neoplasms; Male; Middle Aged; Multiple Myeloma; Papain; Plasmapheresis

Topics: Aged; Blood Coagulation Disorders; Blood Coagulation Tests; Blood Platelets; Blood Protein Disorders; Calcium; Collagen; Connective Tissue; Fibrin; Fibrinogen; gamma-Globulins; Hemorrhagic Disorders; Humans; Male; Multiple Myeloma; Nitrogen Mustard Compounds; Plasmapheresis; Prothrombin Time; Thromboplastin; Tryptophan

Topics: Anesthesia; Blood Protein Disorders; Coagulants; Fibrin; Fibrinogen; Hemorrhagic Disorders; Hemostatics; Humans; Postoperative Complications