Clinical Chemistry
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Clinical Chemistry 45: 807-813, 1999;
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Web of Science (63)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Schatteman, K. A.
Right arrow Articles by Hendriks, D. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schatteman, K. A.
Right arrow Articles by Hendriks, D. F.
Related Collections
Right arrow Proteomics and Protein Markers
Right arrow Hematology
(Clinical Chemistry. 1999;45:807-813.)
© 1999 American Association for Clinical Chemistry, Inc.


Articles

Assay of Procarboxypeptidase U, a Novel Determinant of the Fibrinolytic Cascade, in Human Plasma

Katinka A. Schatteman1, Filip J. Goossens1, Simon S. Scharpé2, Hugo M. Neels2 and Dirk F. Hendriks1,a

1 Department of Clinical Biochemistry, University of Antwerp, Universiteitsplein 1, B-2610 Wilrijk, Belgium.

2 Laboratory of Clinical Biology, OCMW Hospitals, Antwerp, Belgium.
a Author for correspondence. Fax 32-3-820.27.45; e-mail hendriks{at}uia.ua.ac.be

Background: Procarboxypeptidase U (proCPU) is a novel proenzyme found in human plasma. The active form, carboxypeptidase U (CPU; EC 3.4.17.20), retards the rate of fibrinolysis through its ability to cleave C-terminal lysine residues on fibrin partially degraded by plasmin. This reduces the number of high-affinity plasminogen-binding sites on fibrin.

Methods: We developed an assay to determine the proCPU concentration in human plasma. The assay involved quantitative conversion of proCPU to active CPU by thrombin-thrombomodulin, a very efficient activator of proCPU, followed by determination of the enzymatic activity of CPU with the substrate hippuryl-L-arginine, using an HPLC-assisted determination of the released hippuric acid. Using this method, we established a reference interval based on 490 healthy individuals.

Results: The mean proCPU concentration, determined after activation of the zymogen in diluted plasma and expressed as CPU activity, was 964 U/L, with a SD of 155 U/L. The population showed a gaussian distribution. However, we noticed important differences related to age and the use of hormone preparations.

Conclusions: The sensitivity and precision of the method make it suitable for routine clinical determinations and as a reference procedure.© 1999 American Association for Clinical Chemistry




The following articles in journals at HighWire Press have cited this article:


Home page
J. Biol. Chem.Home page
L. I. Pahlman, P. F. Marx, M. Morgelin, S. Lukomski, J. C. M. Meijers, and H. Herwald
Thrombin-activatable Fibrinolysis Inhibitor Binds to Streptococcus pyogenes by Interacting with Collagen-like Proteins A and B
J. Biol. Chem., August 24, 2007; 282(34): 24873 - 24881.
[Abstract] [Full Text] [PDF]


Home page
Clin. Chem.Home page
J. L. Willemse and D. F. Hendriks
Measurement of Procarboxypeptidase U (TAFI) in Human Plasma: A Laboratory Challenge
Clin. Chem., January 1, 2006; 52(1): 30 - 36.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
S. Asai, T. Sato, T. Tada, T. Miyamoto, N. Kimbara, N. Motoyama, H. Okada, and N. Okada
Absence of Procarboxypeptidase R Induces Complement-Mediated Lethal Inflammation in Lipopolysaccharide-Primed Mice
J. Immunol., October 1, 2004; 173(7): 4669 - 4674.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. F. Marx, S. R. Havik, J. A. Marquart, B. N. Bouma, and J. C. M. Meijers
Generation and Characterization of a Highly Stable Form of Activated Thrombin-activable Fibrinolysis Inhibitor
J. Biol. Chem., February 20, 2004; 279(8): 6620 - 6628.
[Abstract] [Full Text] [PDF]


Home page
Arterioscler. Thromb. Vasc. Bio.Home page
A. Gils, M.-C. Alessi, E. Brouwers, M. Peeters, P. Marx, J. Leurs, B. Bouma, D. Hendriks, I. Juhan-Vague, and P. J. Declerck
Development of a Genotype 325-Specific proCPU/TAFI ELISA
Arterioscler Thromb Vasc Biol, June 1, 2003; 23(6): 1122 - 1127.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. B. Boffa, J. D. Hamill, N. Bastajian, R. Dillon, M. E. Nesheim, and M. L. Koschinsky
A Role for CCAAT/Enhancer-binding Protein in Hepatic Expression of Thrombin-activable Fibrinolysis Inhibitor
J. Biol. Chem., July 5, 2002; 277(28): 25329 - 25336.
[Abstract] [Full Text] [PDF]


Home page
Arterioscler. Thromb. Vasc. Bio.Home page
L. Bajzar
Thrombin Activatable Fibrinolysis Inhibitor and an Antifibrinolytic Pathway
Arterioscler Thromb Vasc Biol, December 1, 2000; 20(12): 2511 - 2518.
[Abstract] [Full Text] [PDF]


Home page
Arterioscler. Thromb. Vasc. Bio.Home page
I. Juhan-Vague, J. F. Renucci, M. Grimaux, P. E. Morange, J. Gouvernet, Y. Gourmelin, and M. C. Alessi
Thrombin-Activatable Fibrinolysis Inhibitor Antigen Levels and Cardiovascular Risk Factors
Arterioscler Thromb Vasc Biol, September 1, 2000; 20(9): 2156 - 2161.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
N. H. van Tilburg, F. R. Rosendaal, and R. M. Bertina
Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis
Blood, May 1, 2000; 95(9): 2855 - 2859.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1999 by the American Association for Clinical Chemistry.