Conjugated linoleic acid is an activator and ligand for peroxisome proliferator-activated receptor-gamma (PPARγ)
| Autor: | Lisa M. Leesnitzer, Martha A. Belury, Silvia Y. Moya-Camarena, Ming Lu, Lingling Shi, Steven G. Blanchard |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
chemistry.chemical_classification
Nutrition and Dietetics integumentary system Activator (genetics) Endocrinology Diabetes and Metabolism Linoleic acid Conjugated linoleic acid food and beverages Fatty acid Peroxisome proliferator-activated receptor Biology Ligand (biochemistry) chemistry.chemical_compound Endocrinology chemistry Biochemistry Nuclear receptor lipids (amino acids peptides and proteins) Polyunsaturated fatty acid |
| Zdroj: | Nutrition Research. 22:817-824 |
| ISSN: | 0271-5317 |
| Popis: | The goal of the present study was to elucidate the extent that CLA binds to and activates PPARγ. All of the isomers of CLA tested activated PPARγ in a manner similar to the polyunsaturated fatty acid, linoleic acid (18:2n6). When the binding affinity of CLA to PPARγ was determined using a scintillation proximity assay (SPA), isomers of CLA were ligands for PPARγ with micromolar affinity. To determine the extent that metabolism of CLA via Δ6 desaturase could alter activation of PPARγ, we used a Δ6 desaturase inhibitor, SC-26,196, to block Δ6 desaturase metabolism. Blocking Δ6 desaturase significantly reduced activation of PPARγ by c9t11-CLA. These data suggest that the ability of CLA to induce PPAR-responsive genes may be via both direct binding of CLA to the nuclear hormone receptor, PPARγ, as well as active metabolites of CLA via Δ6 desaturase. Further work is needed to determine the ability of Δ6 desaturase metabolites of CLA to bind and activate PPARγ. |
| Databáze: | OpenAIRE |
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