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Antioxidant activity of secoisolariciresinol diglucoside-derived metabolites, secoisolariciresinol, Enterodiol, and enterolactone
Abstract
Secoisolariciresinol diglucoside (SDG), an antioxidant isolated from flaxseed, is metabolized to secoisolariciresinol (SECO), enterodiol (ED), and enterolactone (EL) in the body. The effectiveness of SDG in hypercholesterolemic atherosclerosis, diabetes, and endotoxic shock could be due to these metabolites. These metabolites may have antioxidant activity. However, the antioxidant activity of these metabolites is not known. The antioxidant activity of SECO, ED, and EL was investigated using chemiluminescence (CL) of zymosan-activated polymorphonuclear leukocytes (PMNLs) [PMNL-CL]. Other antioxidants (SDG and vitamin E) were also used for comparison. SDG, SECO, ED, EL, and vitamin E, each in the concentration of 0.5, 1.0, 2.5, 5.0 and 10.0 mg/ml, produced a concentration-dependent reduction in zymosan-activated PMNL-CL. SDG, SECO, ED, EL, and vitamin E, in the concentration of 2.5 mg/ml, produced a reduction of zymosan-activated PMNL-CL by 23.8%, 91.2%, 94.2%, 81.6% and 18.7%, respectively. Activated PMNLs produce reactive oxygen species and luminol-dependent CL reflects the amount of oxygen species generated from activated PMNLs. The reduction of PMNL-CL, therefore, reflects the antioxidant activity of the compounds studied. These results suggest that the metabolites of SDG have antioxidant activity. The antioxidant activity was highest with SECO and ED and lowest with vitamin E. The antioxidant potency of SECO, ED, EL, and SDG was 4.86, 5.02, 4.35, and 1.27 respectively, as compared to vitamin E. SECO, ED and EL are respectively 3.82, 3.95, and 3.43 more potent than SDG.
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Metadata
- Authors
- Prasad, K.
- Venue
- International Journal of Angiology
- Publisher
- Georg Thieme Verlag KG
- Published
- 2011-04-24
- Volume
- 9
- Issue
- 04
- Pages
- 220-225
- ISSN
- 1061-1711 (ISSN-L)
- 1615-5939
- OpenAlex
- W2087880867
- Cited by
- 266
- References
- 0
- FWCI
- 7.92
- Type
- journal article
- Language
- en
- Open access
- closed
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