gluconasturtiin has been researched along with allyl-isothiocyanate* in 2 studies
2 other study(ies) available for gluconasturtiin and allyl-isothiocyanate
| Article | Year |
|---|---|
Correlation of quinone reductase activity and allyl isothiocyanate formation among different genotypes and grades of horseradish roots.
Horseradish (Armoracia rusticana) is a perennial crop and its ground root tissue is used in condiments because of the pungency of the glucosinolate (GS)-hydrolysis products allyl isothiocyanate (AITC) and phenethyl isothiocyanate (PEITC) derived from sinigrin and gluconasturtiin, respectively. Horseradish roots are sold in three grades: U.S. Fancy, U.S. No. 1, and U.S. No. 2 according to the USDA standards. These grading standards are primarily based on root diameter and length. There is little information on whether root grades vary in their phytochemical content or potential health promoting properties. This study measured GS, GS-hydrolysis products, potential anticancer activity (as quinone reductase inducing activity), total phenolic content, and antioxidant activities from different grades of horseradish accessions. U.S. Fancy showed significantly higher sinigrin and AITC concentrations than U.S. No. 1 ,whereas U.S. No. 1 showed significantly higher concentrations of 1-cyano 2,3-epithiopropane, the epithionitrile hydrolysis product of sinigrin, and significantly higher total phenolic concentrations than U.S. Fancy. Topics: Armoracia; Genotype; Glucosinolates; Isothiocyanates; Plant Proteins; Plant Roots; Quinone Reductases | 2015 |
Myrosinase-treated glucoerucin is a potent inducer of the Nrf2 target gene heme oxygenase 1--studies in cultured HT-29 cells and mice.
In this study, the effect of myrosinase-treated glucoerucin (GER+MYR), which releases the isothiocyanate (ITC) erucin, on heme oxygenase 1 (HO-1) gene expression and Nrf2 signaling was investigated in vitro in cultured cells and in vivo in mice. Treatment of HT-29 cells with GER+MYR resulted in a significant increase in the mRNA and protein levels of nuclear Nrf2 and HO-1. GER+MYR was more potent at enhancing the nuclear Nrf2 levels than were the following myrosinase-treated glucosinolates: sinigrin, glucoraphanin and gluconasturtiin, which are the precursors of allyl-ITC, R-sulforaphane and 2-phenylethyl ITC, respectively. GER+MYR also significantly induced HO-1 gene expression in the mouse intestinal mucosae and liver but not in the brain. Mechanistic studies suggest that GER+MYR induces Nrf2 via ERK1/2-, p38- and JNK-dependent signal transduction pathways. The GER+MYR-mediated increase in HO-1 expression is primarily attributable to p38 signaling. Topics: Animals; Brain; Diet, High-Fat; Female; Glucose; Glucosinolates; Glycoside Hydrolases; Heme Oxygenase-1; HT29 Cells; Humans; Imidoesters; Intestinal Mucosa; Intestines; Isothiocyanates; Liver; Membrane Proteins; Mice; Mice, Inbred C57BL; Mitogen-Activated Protein Kinase 3; Mustard Plant; NF-E2-Related Factor 2; Oximes; p38 Mitogen-Activated Protein Kinases; Plant Extracts; RNA, Messenger; Signal Transduction; Sulfoxides; Up-Regulation | 2015 |