Myrosinase-treated glucoerucin is a potent inducer of the Nrf2 target gene heme oxygenase 1 - studies in cultured HT-29 cells and mice

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

  • A.E. Wagner
  • C. Sturm
  • S. Piegholdt
  • I.M.A. Wolf
  • T. Esatbeyoglu
  • G.R. De Nicola
  • R. Iori
  • G. Rimbach
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Details

OriginalspracheEnglisch
Seiten (von - bis)661-666
Seitenumfang6
FachzeitschriftJournal of Nutritional Biochemistry
Jahrgang26
Ausgabenummer6
PublikationsstatusVeröffentlicht - 1 Juni 2015

Abstract

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.

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Myrosinase-treated glucoerucin is a potent inducer of the Nrf2 target gene heme oxygenase 1 - studies in cultured HT-29 cells and mice. / Wagner, A.E.; Sturm, C.; Piegholdt, S. et al.
in: Journal of Nutritional Biochemistry, Jahrgang 26, Nr. 6, 01.06.2015, S. 661-666.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Wagner AE, Sturm C, Piegholdt S, Wolf IMA, Esatbeyoglu T, De Nicola GR et al. Myrosinase-treated glucoerucin is a potent inducer of the Nrf2 target gene heme oxygenase 1 - studies in cultured HT-29 cells and mice. Journal of Nutritional Biochemistry. 2015 Jun 1;26(6):661-666. doi: 10.1016/j.jnutbio.2015.01.004
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title = "Myrosinase-treated glucoerucin is a potent inducer of the Nrf2 target gene heme oxygenase 1 - studies in cultured HT-29 cells and mice",
abstract = "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.",
keywords = "Glucoerucin, Glucosinolates, Heme oxygenase 1, MAPK, Myrosinase, Nrf2",
author = "A.E. Wagner and C. Sturm and S. Piegholdt and I.M.A. Wolf and T. Esatbeyoglu and {De Nicola}, G.R. and R. Iori and G. Rimbach",
note = "Funding information: This work was supported by a grant from the “Deutsche Forschungsgemeinschaft (DFG)” to A.E.W. (WA 3370/1-1) and by the DFG cluster of excellence “Inflammation at Interfaces”.",
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T1 - Myrosinase-treated glucoerucin is a potent inducer of the Nrf2 target gene heme oxygenase 1 - studies in cultured HT-29 cells and mice

AU - Wagner, A.E.

AU - Sturm, C.

AU - Piegholdt, S.

AU - Wolf, I.M.A.

AU - Esatbeyoglu, T.

AU - De Nicola, G.R.

AU - Iori, R.

AU - Rimbach, G.

N1 - Funding information: This work was supported by a grant from the “Deutsche Forschungsgemeinschaft (DFG)” to A.E.W. (WA 3370/1-1) and by the DFG cluster of excellence “Inflammation at Interfaces”.

PY - 2015/6/1

Y1 - 2015/6/1

N2 - 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.

AB - 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.

KW - Glucoerucin

KW - Glucosinolates

KW - Heme oxygenase 1

KW - MAPK

KW - Myrosinase

KW - Nrf2

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DO - 10.1016/j.jnutbio.2015.01.004

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EP - 666

JO - Journal of Nutritional Biochemistry

JF - Journal of Nutritional Biochemistry

SN - 0955-2863

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