Novel pathways associated with quinone-induced stress in breast cancer cells.

Abstract:

:Hormone-dependent breast cancers that overexpress the ligand-binding nuclear transcription factor, estrogen receptor (ER), represent the most common form of breast epithelial malignancy. Exposure of breast epithelial cells to a redox-cycling and arylating quinone induces mitogen-activated protein kinase phosphorylation of the cytoskeletal filament protein, cytokeratin-8, along with thiol arylation of H3 nuclear histones. Exogenous or endogenous quinones can also induce ligand-independent nuclear translocation and phosphorylation of ER; with excess exposure, these quinones can arylate ER zinc fingers, impairing ER DNA-binding and altering ER-inducible gene expression. Immunoaffinity enrichment for low abundance proteins such as ER, coupled with modern mass spectrometry techniques, promises to improve understanding of the protein-modifications produced by endogenous and exogenous quinone exposure and their role in the development or progression of epithelial malignancies such as breast cancer.

journal_name

Drug Metab Rev

journal_title

Drug metabolism reviews

authors

Benz CC,Atsriku C,Yau C,Britton D,Schilling B,Gibson BW,Baldwin MA,Scott GK

doi

10.1080/03602530600959391

subject

Has Abstract

pub_date

2006-01-01 00:00:00

pages

601-13

issue

4

eissn

0360-2532

issn

1097-9883

pii

G3J6606H75783N18

journal_volume

38

pub_type

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