Abnormal factor VIII coagulant antigen in patients with renal dysfunction and in those with disseminated intravascular coagulation
| Autor: | G W Schmitt, J H Troll, L E Chute, M J Weinstein, Kenneth A. Bauer, R H Hamburger, Daniel Deykin, Janson Pa |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
congenital
hereditary and neonatal diseases and abnormalities medicine.medical_specialty chemistry.chemical_compound Thrombin Antigen Von Willebrand factor Renal Dialysis Neoplasms hemic and lymphatic diseases Internal medicine von Willebrand Factor mental disorders Mole medicine Humans Polyacrylamide gel electrophoresis Aged Disseminated intravascular coagulation Creatinine Factor VIII biology General Medicine Disseminated Intravascular Coagulation Middle Aged medicine.disease In vitro Molecular Weight Endocrinology chemistry Immunology biology.protein Kidney Failure Chronic Kidney Diseases Prothrombin Research Article medicine.drug |
| Zdroj: | Journal of Clinical Investigation. 76:1406-1411 |
| ISSN: | 0021-9738 |
| DOI: | 10.1172/jci112117 |
| Popis: | Factor VIII antigen (VIII:CAg) exhibits molecular weight heterogeneity in normal plasma. We have compared the relative quantities of VIII:CAg forms present in normal individuals (n = 22) with VIII:CAg forms in renal dysfunction patients (n = 19) and in patients with disseminated intravascular coagulation (DIC; n = 7). In normal plasma, the predominant VIII: CAg form, detectable by sodium dodecyl sulfate polyacrylamide gel electrophoresis, was of molecular weight 2.4 X 10(5), with minor forms ranging from 8 X 10(4) to 2.6 X 10(5) D. A high proportion of VIII:CAg in renal dysfunction patients, in contrast, was of 1 X 10(5) mol wt. The patients' high 1 X 10(5) mol wt VIII: CAg level correlated with increased concentrations of serum creatinine, F1+2 (a polypeptide released upon prothrombin activation), and with von Willebrand factor. Despite the high proportion of the 1 X 10(5) mol wt VIII:CAg form, which suggests VIII:CAg proteolysis, the ratio of Factor VIII coagulant activity to total VIII:CAg concentration was normal in renal dysfunction patients. These results could be simulated in vitro by thrombin treatment of normal plasma, which yielded similar VIII:CAg gel patterns and Factor VIII coagulant activity to antigen ratios. DIC patients with high F1+2 levels but no evidence of renal dysfunction had an VIII:CAg gel pattern distinct from renal dysfunction patients. DIC patients had elevated concentrations of both the 1 X 10(5) and 8 X 10(4) mol wt VIII:CAg forms. We conclude that an increase in a particular VIII:CAg form correlates with the severity of renal dysfunction. The antigen abnormality may be the result of VIII:CAg proteolysis by a thrombinlike enzyme and/or prolonged retention of proteolyzed VIII:CAg fragments. |
| Databáze: | OpenAIRE |
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