thromboplastin has been researched along with Hepatitis--Viral--Human* in 4 studies
4 other study(ies) available for thromboplastin and Hepatitis--Viral--Human
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Comparison of modes of prothrombin time reporting in patients with advanced liver disease associated with viral hepatitis.
Prothrombin time is widely utilized for evaluation of liver disease severity. However, its standardization of modes of reporting is not established for universal purpose. Variability in thromboplastin reagents leads to large intralaboratory and interlaboratory differences in PT results.. The aim of this study was to establish standardization of modes of PT reporting by the interchangeability analysis of prothrombin time in patients with advanced liver disease associated with viral hepatitis measured with different thromboplastin reagents by the use of various methods of expression, i.e. prothrombin time (PTs), prothrombin activity percentage (PTp), prothrombin time ratio (PTr) and International Normalized Ratio (INR).. we prospectively collected blood samples from 61 patients with advanced liver disease associated with viral hepatitis, control patients were on warfarin (n = 20). PT was measured on a STA-R with six thromboplastin reagents. PT was expressed in PTs, PTr, PTp, and INR. Neoplastin was selected as reference reagent for comparison of methods of reporting.. The study revealed the closest agreement of the results in study population between Neoplastin and the other five reagents, and the regression lines of these reagents were close to each other, when the results were expressed in PTp while INR, PTs and PTr is not valid for comparison of patients with liver disease. In patients on oral anticoagulant therapy, only INR standardize PT results.. we conclude that, in patients with liver disease, only activity percentage expression may provide a common international scale of PT reporting. Topics: Adult; Aged; Female; Hepatitis, Viral, Human; Humans; Male; Middle Aged; Prospective Studies; Prothrombin Time; Thromboplastin | 2010 |
Tissue factor and thrombomodulin in hemodialysis patients: associations with endothelial injury, liver disease, and erythropoietin therapy.
Patients receiving maintenance hemodialysis (HD) present with hemostatic abnormalities, which may be aggravated by comorbid conditions, especially liver disease. The factors that influence plasma levels of thrombomodulin (TM), an initiator of the anticoagulant protein C pathway, and those of tissue factor (TF), which triggers the extrinsic coagulation pathway, were assessed. In 63 HD patients, TM and TF levels were higher than those in healthy controls. In bivariate analysis, TF positively correlated with TM, and both were directly associated with the presence of viral hepatitis B or C marker, serum liver enzymes, use of erythropoietin therapy, hemoglobin levels, and duration of HD therapy, and inversely correlated with body mass index. TF was also positively associated with plasma von Willebrand factor (vWF) antigen, and inversely associated with activated partial thromboplastin time. In multivariate analysis, increased vWF, alanine aminotransferase, and use of erythropoietin independently predicted both TF and TM levels. HD patients with vWF and ALT levels lower than middle, and not treated with erythropoietin had normal TF but increased TM concentrations compared with levels in healthy controls. Increased plasma levels of TM and TF in patients on maintenance HD are surrogates of vascular endothelial injury. Liver disease and use of erythropoietin treatment are also important determinants of these markers, and should be considered in further studies. Topics: Adult; Aged; Aged, 80 and over; Analysis of Variance; Biomarkers; Case-Control Studies; Clinical Enzyme Tests; Cross-Sectional Studies; Endothelium, Vascular; Erythropoietin; Female; Hepatitis, Viral, Human; Humans; Liver Diseases; Male; Middle Aged; Prevalence; Renal Dialysis; Thrombomodulin; Thromboplastin; von Willebrand Factor | 2002 |
Molecular and functional analysis of the human prothrombinase gene (HFGL2) and its role in viral hepatitis.
In the present studies, we report the cloning and structural characterization of the HFGL2 gene and its functional role in human fulminant hepatitis. The HFGL2 gene is approximately 7 kb in length with 2 exons. The putative promoter contains cis element consensus sequences that strongly suggest the inducibility of its expression. From the nucleotide sequence of the human gene, a 439-amino acid long protein is predicted. The overall identity between the murine fgl2 and hfgl2 coded proteins is over 70%. About 225 amino acids at the carboxyl end of these molecules are almost 90% identical, and correspond to a well-conserved fibrinogen-related domain. Both HFGL2 and FGL2 encode a type II transmembrane protein with a predicted catalytic domain toward the amino terminus of the protein. Transient transfection of Chinese hamster ovary (CHO) cells with a full-length cDNA of HFGL2 coding region resulted in high levels of prothrombinase activity. Livers from 8 patients transplanted for fulminant viral hepatitis were examined for extent of necrosis, inflammation, fibrin deposition, and HFGL2 induction. In situ hybridization showed positive staining of macrophages in areas of active hepatocellular necrosis. Fibrin stained positively in these areas and was confirmed by electron microscopy. These studies define a unique prothrombinase gene (HFGL2) and implicate its importance in the pathogenesis of fulminant viral hepatitis. Topics: Adolescent; Adult; Amino Acid Sequence; Animals; Child, Preschool; CHO Cells; Cloning, Molecular; Consensus Sequence; Cricetinae; Female; Fibrin; Fibrinogen; Hepatitis, Viral, Human; Humans; Infant; Liver; Male; Middle Aged; Molecular Sequence Data; Necrosis; Promoter Regions, Genetic; Thromboplastin; Transfection | 2000 |
[Improvement in anti-hemophilic preparations and its problems. 2. Inadequacy of the heat treatment of factor concentrates on the inactivation of non-A, non-B hepatitis virus].
Topics: Drug Contamination; Factor IX; Hepatitis C; Hepatitis, Viral, Human; Hot Temperature; Humans; Thromboplastin | 1988 |