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Modulation of the expression of mult...

Harris, Kristin E.

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Modulation of the expression of multidrug resistance proteins by sulforaphane and erucin.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Modulation of the expression of multidrug resistance proteins by sulforaphane and erucin./
作者:	Harris, Kristin E.
面頁冊數:	116 p.
附註:	Adviser: Elizabeth Jeffery.
Contained By:	Dissertation Abstracts International68-06B.
標題:	Health Sciences, Nutrition. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3269911
ISBN:	9780549102953

Modulation of the expression of multidrug resistance proteins by sulforaphane and erucin.
Harris, Kristin E.

Modulation of the expression of multidrug resistance proteins by sulforaphane and erucin. - 116 p.

Adviser: Elizabeth Jeffery.

Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2007.

Multidrug resistance transporters (MDR) have been termed the phase III detoxification system because they not only export endogenous metabolites, but provide protection from xenobiotic insult by actively secreting foreign compounds and their metabolites from tissues. However, MDR overexpression in tumors can lead to drug resistance, a major obstacle in the treatment of many cancers, including lung cancer. Cruciferous vegetable contain glucosinolates that, upon hydrolysis produce bioactive isothiocyanates, such as sulforaphane (SF) and erucin (ER), known to enhance the expression of phase II detoxification enzymes. We evaluated the ability of SF and ER to modulate MDR mRNA and protein expression, substrate efflux, and chemosensitivity. The expression of P-glycoprotein (P-gp), MRP1, and multidrug resistance protein 2 (MRP2) in human liver (HepG2), colon (Caco2), and lung (A549) cancer cells treated with ER or SF was analyzed by western blotting. Both SF and ER increased the protein level of MRP1 and MRP2 in HepG2 cells, and MRP2 in Caco-2 cells, in a dose-dependent manner, without affecting P-gp. In A549 lung cancer cells, SF increased MRP1 and MRP2 mRNA and protein levels. Erucin caused a similar yet smaller increase in MRP1 and MRP2 mRNA. In addition, both SF and ER increased MRP1-mediated efflux and decreased efficacy of the chemotherapeutics doxorubicin and vinblastine, MRP1 substrates.

ISBN: 9780549102953Subjects--Topical Terms:

1017801
Health Sciences, Nutrition.

Modulation of the expression of multidrug resistance proteins by sulforaphane and erucin.
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520 $a Multidrug resistance transporters (MDR) have been termed the phase III detoxification system because they not only export endogenous metabolites, but provide protection from xenobiotic insult by actively secreting foreign compounds and their metabolites from tissues. However, MDR overexpression in tumors can lead to drug resistance, a major obstacle in the treatment of many cancers, including lung cancer. Cruciferous vegetable contain glucosinolates that, upon hydrolysis produce bioactive isothiocyanates, such as sulforaphane (SF) and erucin (ER), known to enhance the expression of phase II detoxification enzymes. We evaluated the ability of SF and ER to modulate MDR mRNA and protein expression, substrate efflux, and chemosensitivity. The expression of P-glycoprotein (P-gp), MRP1, and multidrug resistance protein 2 (MRP2) in human liver (HepG2), colon (Caco2), and lung (A549) cancer cells treated with ER or SF was analyzed by western blotting. Both SF and ER increased the protein level of MRP1 and MRP2 in HepG2 cells, and MRP2 in Caco-2 cells, in a dose-dependent manner, without affecting P-gp. In A549 lung cancer cells, SF increased MRP1 and MRP2 mRNA and protein levels. Erucin caused a similar yet smaller increase in MRP1 and MRP2 mRNA. In addition, both SF and ER increased MRP1-mediated efflux and decreased efficacy of the chemotherapeutics doxorubicin and vinblastine, MRP1 substrates.
520 $a Sulforaphane increases gene expression through binding of the Nrf2 transcription factor to the antioxidant response element (ARE) in the promoter region of target genes. Because SF and ER increased MRP1 expression at the mRNA level, we investigated the impact of these compounds on MRP1 transcription. Non-small cell lung cancer cells (A549) and human liver carcinoma cells (HepG2) were transfected with an MRP1-luciferase reporter gene and treated with SF or ER. Neither SF nor ER increased luciferase activity in the transfected cells. In addition, overexpression of Nrf2 in A549 cells had no effect on MRP1-luc expression. These results indicate that SF and ER increase MPR1 mRNA and protein levels via a non-transcriptional mechanism and that activation of Nrf2 does not induce transcription of the mrp1 gene.
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