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Phytochemicals in Spanish black radish induce detoxification enzymes
Author(s) -
Hanlon Paul Robert,
Webber David M,
Metzger Brandon T,
Barnes David M
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a565-d
Subject(s) - glucosinolate , enzyme , chemistry , detoxification (alternative medicine) , reductase , biochemistry , myrosinase , enzyme assay , food science , botany , biology , brassica , medicine , alternative medicine , pathology
For 25 years Standard Process has organically grown, dried, and concentrated Spanish Black Radish (SBR) into nutritional supplement form. To better understand the physiological effect of SBR, a rich source of glucosinolates and their metabolites, the prevalence and effectiveness of these constituents contained in SBR were examined. SBR glucosinolates were putatively identified and the effects of SBR extracts on detoxification enzyme activity were determined. HPLC analysis of lyophilized whole, halved, quartered, and sliced SBR confirmed a high abundance of the glucosinolate 4‐methylthiobut‐3‐enyl (4‐MTB‐3‐E), whereas lyophilized ground or high temperature dried SBR demonstrated very little 4‐MTB‐3‐E. SBR aqueous extracts induced three detoxification enzymes in the Hepa‐1c1c7 immortalized mouse hepatoma cell line: glutathione S‐transferase, quinone reductase (QR), and thioredoxin reductase. The data demonstrate that the aqueous extract of SBR is a more potent inducer of QR activity than the aqueous extract of other crucifers (kale and Brussels sprouts). Moreover, following induction by SBR QR activity remained elevated for seven days even after SBR extract had been removed from the cells. However, certain active biological constituents of SBR remain unknown. It is now recognized that SBR contains high levels of one major glucosinolate, multiple breakdown products of this glucosinolate confirmed by GC‐MS, and the capacity to induce detoxification enzymes in liver cells. Work supported by Standard Process, Inc.