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


     

A more recent version of this article appeared on December 1, 2004

Papers In Press, published online ahead of print September 1, 2004
J. Lipid Res., doi:10.1194/jlr.M400213-JLR200
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
M400213-JLR200v1
45/12/2260    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 Teiber, J. F.
Right arrow Articles by La Du, B. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Teiber, J. F.
Right arrow Articles by La Du, B. N.
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 June 8, 2004
Revised on August 23, 2004
Accepted on August 24, 2004

Purified human serum PON1 does not protect LDL against oxidation in the in vitro assays initiated with copper or AAPH

John F. Teiber, Dragomir I. Draganov, and Bert N. La Du

Pharmacology Dept., The University of Michigan, Ann Arbor, MI 48109-0632

Corresponding Author: bladu{at}umich.edu

Purified serum PON1 had been shown to attenuate the oxidation of LDL in vitro. We critically re-evaluated the antioxidant properties of serum PON1 in the in vitro assays initiated with copper or the free radical generator 2, 2’-azobis-2-amidinopropane hydrochloride. The antioxidant activity of different purified PON1 preparations did not correlate with their arylesterase, lactonase or phopholipase A-2 activities, or with the amounts of detergent or protein. Dialysis of three of these preparations resulted in a 30-40 % loss of their arylesterase activities but in a complete loss of their antioxidant activities. We also followed the distribution of the antioxidant activity during human serum PON1 purification by two purification methods. The antioxidant activity of the anion exchange chromatography fractions did not co-purify with PON1 using either method and could largely be accounted for by the “antioxidant” activity of the detergent present. In conclusion, using the copper or AAPH in vitro assays no PON1-mediated antioxidant activity was detected suggesting that the removal of PON1 from its natural environment may impair its antioxidative activity and that this assay with highly purified PON1 may be an inappropriate method to study the antioxidative properties of the enzyme.


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
 J. Biol. Chem.Home page
T. Kriska, G. K. Marathe, J. C. Schmidt, T. M. McIntyre, and A. W. Girotti
Phospholipase Action of Platelet-activating Factor Acetylhydrolase, but Not Paraoxonase-1, on Long Fatty Acyl Chain Phospholipid Hydroperoxides
J. Biol. Chem., January 5, 2007; 282(1): 100 - 108.
[Abstract] [Full Text] [PDF]

Home page
 J. Lipid Res.Home page
L. Gaidukov, M. Rosenblat, M. Aviram, and D. S. Tawfik
The 192R/Q polymorphs of serum paraoxonase PON1 differ in HDL binding, lipolactonase stimulation, and cholesterol efflux
J. Lipid Res., November 1, 2006; 47(11): 2492 - 2502.
[Abstract] [Full Text] [PDF]

Home page
 Pharmacol. Rev.Home page
A. Kontush and M. J. Chapman
Functionally Defective High-Density Lipoprotein: A New Therapeutic Target at the Crossroads of Dyslipidemia, Inflammation, and Atherosclerosis
Pharmacol. Rev., September 1, 2006; 58(3): 342 - 374.
[Abstract] [Full Text] [PDF]

Home page
 J. Lipid Res.Home page
C. S. Carlson, P. J. Heagerty, T. S. Hatsukami, R. J. Richter, J. Ranchalis, J. Lewis, T. J. Bacus, L. A. McKinstry, G. D. Schellenberg, M. Rieder, et al.
TagSNP analyses of the PON gene cluster: effects on PON1 activity, LDL oxidative susceptibility, and vascular disease
J. Lipid Res., May 1, 2006; 47(5): 1014 - 1024.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Rosenblat, L. Gaidukov, O. Khersonsky, J. Vaya, R. Oren, D. S. Tawfik, and M. Aviram
The Catalytic Histidine Dyad of High Density Lipoprotein-associated Serum Paraoxonase-1 (PON1) Is Essential for PON1-mediated Inhibition of Low Density Lipoprotein Oxidation and Stimulation of Macrophage Cholesterol Efflux
J. Biol. Chem., March 17, 2006; 281(11): 7657 - 7665.
[Abstract] [Full Text] [PDF]

Home page
 J. Lipid Res.Home page
D. I. Draganov, J. F. Teiber, A. Speelman, Y. Osawa, R. Sunahara, and B. N. La Du
Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities
J. Lipid Res., June 1, 2005; 46(6): 1239 - 1247.
[Abstract] [Full Text] [PDF]

Home page
 J. Lipid Res.Home page
A. Chait, C. Y. Han, J. F. Oram, and J. W. Heinecke
Thematic review series: The Immune System and Atherogenesis. Lipoprotein-associated inflammatory proteins: markers or mediators of cardiovascular disease?
J. Lipid Res., March 1, 2005; 46(3): 389 - 403.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.