J. Lipid Res.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on July 1, 2007

Papers In Press, published online ahead of print April 13, 2007
J. Lipid Res., doi:10.1194/jlr.D600045-JLR200
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
D600045-JLR200v1
48/7/1637    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
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 Google Scholar
Google Scholar
Right arrow Articles by Gaidukov, L.
Right arrow Articles by Tawfik, D. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gaidukov, L.
Right arrow Articles by Tawfik, D. S.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Submitted on November 14, 2006
Revised on April 13, 2007
Accepted on April 13, 2007

The development of human sera tests for HDL-bound serum paraoxonase PON1 and its lipo-lactonase activity

Leonid Gaidukov and Dan S. Tawfik

Department of Biochemistry, Weizmann Institute of Science, Rehovot 76100

Corresponding Author: leonid.gaydukov{at}weizmann.ac.il

Serum paraoxonase (PON1) is a lipo-lactonase that associates with HDL-apoA-I and thereby plays a role in the prevention of atherosclerosis. Current sera tests make use of promiscuous substrates and provide no indications regarding HDL-PON1 complex formation. We developed new enzymatic tests that detect the total PON1 levels, irrespective of its HDL status and R/Q polymorphism, as well as the degree of catalytic stimulation and increased stability that follow PON1’s tight binding to HDL-apoA-I. The tests are based on measuring total PON1 levels with a fluorogenic phosphotriester; measuring the lipo-lactonase activity with a chromogenic lactone; and assaying the enzyme’s chelator-mediated inactivation rate. The latter two are affected by tight HDL binding, and thereby derive the levels of the serum PON1-HDL complex. We demonstrate these new tests with a group of healthy individuals (n=54), and show that the levels of PON1-HDL vary by a factor of 12. Whereas the traditionally applied paraoxonase and aryl esterase tests weakly reflected the PON1-HDL levels (R=0.64), the lipo-lactonase test provided better correlation (R=0.80). These new tests indicate the levels and activity of PON1 in a physiologically relevant context, and the levels and quality of the HDL particles with which the enzyme is associated.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Nephrol Dial TransplantHome page
P. W. Connelly
Increased serum advanced glycation end products are associated with impairment in HDL antioxidative capacity in diabetic nephropathy
Nephrol. Dial. Transplant., August 1, 2008; 23(8): 2699 - 2700.
[Full Text] [PDF]

Home page
 Clin. Chem.Home page
B. Thyagarajan, D. R. Jacobs Jr., J. J. Carr, O. Alozie, M. W. Steffes, P. Kailash, J. H. Hayes, and M. D. Gross
Factors Associated with Paraoxonase Genotypes and Activity in a Diverse, Young, Healthy Population: The Coronary Artery Risk Development in Young Adults (CARDIA) Study
Clin. Chem., April 1, 2008; 54(4): 738 - 746.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.