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Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase.
- M. Aviram, M. Rosenblat, C. Bisgaier, R. Newton, S. Primo-Parmo, B. La Du
- BiologyThe Journal of clinical investigation
- 15 April 1998
It is concluded that HDL-associated PON possesses peroxidase-like activity that can contribute to the protective effect of PON against lipoprotein oxidation, and may be a major contributor to the antiatherogenicity of this lipop Protein.
Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificitiess⃞s⃞ The online version of this article (available at http://www.jlr.org) contains…
- D. Draganov, J. Teiber, A. Speelman, Y. Osawa, R. Sunahara, B. La Du
- BiologyJournal of Lipid Research
- 1 June 2005
A baculovirus-mediated expression system is developed, suitable for all three human PONs, and optimized procedures for their purification, which revealed them to be lactonases/lactonizing enzymes, with some overlapping substrates, but also to have distinctive substrate specificities.
The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family.
Evidence that the human genome contains two PON1-like genes, designated PON2 and PON3, is presented here and will have important implications for future experiments designed to discover the individual functions, catalytic properties, and physiological roles of the paraoxonases.
Protective effect of high density lipoprotein associated paraoxonase. Inhibition of the biological activity of minimally oxidized low density lipoprotein.
The results suggest that PON in HDL may protect against the induction of inflammatory responses in artery wall cells by destroying biologically active lipids in mildly oxidized LDL.
The human serum paraoxonase/arylesterase polymorphism.
It is postulate that a single serum enzyme, with both paraox onase and arylesterase activity, exists in two different isozymic forms with qualitatively different properties, and that paraoxon is a "discriminating" substrate (having a polymorphic distribution of activity) and phenylacetate is a 'nondiscriminating' substrate for the two isozymes.
Anti-inflammatory HDL becomes pro-inflammatory during the acute phase response. Loss of protective effect of HDL against LDL oxidation in aortic wall cell cocultures.
- B. V. Van Lenten, S. Hama, M. Navab
- Biology, MedicineThe Journal of clinical investigation
- 1 December 1995
Under basal conditions HDL serves an anti-inflammatory role but during APR displacement and/or exchange of proteins associated with HDL results in a pro-inflammatory molecule.
Current progress on esterases: from molecular structure to function.
- T. Satoh, P. Taylor, W. Bosron, S. Sanghani, M. Hosokawa, B. La Du
- BiologyDrug metabolism and disposition: the biological…
- 1 May 2002
Mechanisms of regulation of gene expression of the various esterases by developmental factors and xenobiotics, as well as the interplay between physiological and chemical regulation of enzyme activity are covered.
Rabbit Serum Paraoxonase 3 (PON3) Is a High Density Lipoprotein-associated Lactonase and Protects Low Density Lipoprotein against Oxidation*
- D. Draganov, P. Stetson, C. Watson, S. Billecke, B. La Du
- BiologyThe Journal of Biological Chemistry
- 27 October 2000
Rabbit serum PON3 is more efficient than rabbit PON1 in protecting low density lipoprotein from copper-induced oxidation and is the first report that identifies a second PON enzyme in mammalian serum and the first to describe an enzymatic activity for Pon3.
Human serum paraoxonase (PON 1) is inactivated by oxidized low density lipoprotein and preserved by antioxidants.
Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: glutamine or arginine at position 191, for the respective A or B allozymes.
Pedigree analysis showed both polymorphisms to be inherited in the expected Mendelian manner and confirmed that only the 191 polymorphism showed concordance with the serum paraoxonase/arylesterase phenotypes.