NDLI: Protective action of CLA against oxidative inactivation of paraoxonase 1, an antioxidant enzyme

Content Provider	Springer Nature Link
Author	Su, Nguyen Duy Liu, Xi Wen Kim, Mee Ree Jeong, Tae Sook Sok, Dai Eun
Copyright Year	2003
Abstract	The effect of CLA on paraoxonase 1 (PON1), one of the antioxidant proteins associated with HDL, was investigated for its protective action against oxidative inactivation as well as its stabilization activity. When cis-9 (c9),trans-11 (t11)-CLA and t10,c12-CLA were examined for their protective activity against ascorbate/Cu$^{2−}$-induced inactivation of PON1 in the presence of Ca$^{2+}$, two CLA isomers exhibited a remarkable protection (E $_{max}$, 71–74%) in a concentration-dependent manner (50% effective concentration, 3–4 μM), characterized by a saturation pattern. Such a protective action was also reproduced with oleic acid, but not linoleic acid. Rather, linoleic acid antagonized the protective action of CLA isomers in a noncompetitive fashion. Additionally, the two CLA isomers also protected PON1 from oxidative inactivation by H$_{2}$O$_{2}$ or cumene hydroperoxide. The concentration-dependent protective action of CLA against various oxidative inactivation systems suggests that the protective action of CLA isomers may be mediated through their selective binding to a specific binding site in a PON1 molecule. Separately, the inactivation of PON1 by p-hydroxymercuribenzoate (PHMB), a modifier of the cysteine residue, was also prevented by CLA isomers, suggesting the possible existence of the cysteine residue in the binding site of CLA. The c9,t11-CLA isomer seems to be somewhat more effective than t10,c12-CLA in protecting against the inactivation of PON1 by either peroxides or PHMB, in contrast to the similar efficacy of these two CLA isomers in preventing ascorbate/Cu$^{2+}$-induced inactivation of PON1. Separately, CLA isomers successfully stabilized PON1, but not linoleic acid. These data suggest that the two CLA isomers may play a beneficial role in protecting PON1 from oxidative inactivation as well as in its stabilization.
Starting Page	615
Ending Page	622
Page Count	8
File Format	PDF
ISSN	00244201
Journal	Lipids
Volume Number	38
Issue Number	6
e-ISSN	15589307
Language	English
Publisher	Springer-Verlag
Publisher Date	2003-01-01
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Nutrition Bioorganic Chemistry Medicinal Chemistry Medical Biochemistry Biochemistry Microbial Genetics and Genomics
Content Type	Text
Resource Type	Article
Subject	Cell Biology Organic Chemistry Biochemistry

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