CPR-Total (TAFI and Activated TAFI) Levels in Plasma/Serum of Hemophiliacs
Open Access
- 1 January 2000
- journal article
- research article
- Published by Wiley in Microbiology and Immunology
- Vol. 44 (1) , 77-78
- https://doi.org/10.1111/j.1348-0421.2000.tb01249.x
Abstract
Arginine carboxypeptidase (CPR) is a single‐chain plasma protein generated during coagulation from a precursor (proCPR). proCPR is the same molecule as thrombin activable fibrinolysis inhibitor (TAFI), which retards fibrin clot lysis in vitro and most likely modulates fibrinolysis in vivo. In this study, the amount of CPR‐total, which includes proCPR (TAFI) and CPR (activated TAFI), in hemophiliac patients was evaluated using a newly developed enzyme linked immunosorbent assay (ELISA). The amount of CPR‐total in plasma or serum of most of the hemophiliac patients was in the range of healthy individuals. There was no significant difference in hemophiliac patients with or without HIV‐1 infection. However, two out of the 74 hemophiliac patients showed a significantly high level. The upregulation of CPR‐total might contribute to compensate for inefficient coagulation in some hemophiliac individuals.Keywords
This publication has 9 references indexed in Scilit:
- Arginine Carboxypeptidase (CPR) in Human Plasma Determined with Sandwich ELISAMicrobiology and Immunology, 1999
- TAFI, or Plasma Procarboxypeptidase B, Couples the Coagulation and Fibrinolytic Cascades through the Thrombin-Thrombomodulin ComplexPublished by Elsevier ,1996
- Plasma carboxypeptidases as regulators of the plasminogen system.Journal of Clinical Investigation, 1995
- Purification and Characterization of TAFI, a Thrombin-activable Fibrinolysis InhibitorJournal of Biological Chemistry, 1995
- Pro-Carboxypeptidase R Cleaves Bradykinin following ActivationInternational Archives of Allergy and Immunology, 1994
- Role of cell-surface lysines in plasminogen binding to cells: identification of .alpha.-enolase as a candidate plasminogen receptorBiochemistry, 1991
- An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunitsBiochemical and Biophysical Research Communications, 1989
- Complementary modes of action of tissue-type plasminogen activator and pro-urokinase by which their synergistic effect on clot lysis may be explained.Journal of Clinical Investigation, 1988
- An enzyme in human blood plasma that inactivates bradykinin and kallidinsBiochemical Pharmacology, 1962