| Increased proteasome-dependent degradation of estrogen receptor-alpha by TGF-beta1 in breast cancer cell lines. | |
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MedLine Citation:
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PMID: 12461787 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Normal mammary epithelial cells are rapidly induced to G(1) arrest by the widely expressed cytokine, transforming growth factor beta (TGF-beta1). Studies in established breast cancer cell lines that express the estrogen receptor alpha (ERalpha) have demonstrated loss of this responsiveness. This inverse correlation suggests interpathway signaling important to cell growth and regulation. The adenocarcinoma breast cell line BT474, which was not growth arrested by TGF-beta1, was used as a model of estrogen-inducible growth to explore interpathway crosstalk. Although BT474 cells were not growth-arrested by TGF-beta1 as determined by flow cytometry analysis and 5'-bromo-3'-deoxyuridine incorporation into DNA, estrogen receptor protein levels were attenuated by 100 pM TGF-beta1 after 6 h. This decrease in ERalpha reached 50% of untreated control levels by 24 h of treatment and was further supported by a 50% decrease in estrogen-inducible DNA synthesis. Inspection of ERalpha transcripts suggested that this decrease was primarily the result of altered ERalpha protein stability or availability. Use of the proteasome inhibitor, MG132, abolished all effects on ERalpha by TGF-beta1. Collectively, this data supports a role for TGF-beta1 in regulating the growth of otherwise insensitive breast cancer cells through modulation of ERalpha stability. |
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Authors:
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Trevor A Petrel; Robert W Brueggemeier |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Journal of cellular biochemistry Volume: 88 ISSN: 0730-2312 ISO Abbreviation: J. Cell. Biochem. Publication Date: 2003 Jan |
Date Detail:
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Created Date: 2002-12-03 Completed Date: 2003-06-13 Revised Date: 2011-09-26 |
Medline Journal Info:
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Nlm Unique ID: 8205768 Medline TA: J Cell Biochem Country: United States |
Other Details:
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Languages: eng Pagination: 181-90 Citation Subset: IM |
Copyright Information:
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Copyright 2002 Wiley-Liss, Inc. |
Affiliation:
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The Ohio State Biochemistry Program, College of Medicine and Public Health, and OSU Comprehensive Cancer Center, The Ohio State University, Columbus, Ohio 43210, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Blotting, Northern Blotting, Western Breast Neoplasms / metabolism, pathology* Bromodeoxyuridine / pharmacology Cell Division Cysteine Endopeptidases / metabolism* Estradiol / pharmacology Estrogen Receptor alpha Flow Cytometry Humans Leupeptins / pharmacology Multienzyme Complexes / metabolism* Proteasome Endopeptidase Complex Receptors, Estrogen / metabolism* Reverse Transcriptase Polymerase Chain Reaction Time Factors Transforming Growth Factor beta / metabolism* Transforming Growth Factor beta1 Tumor Cells, Cultured Ubiquitin / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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P30 CA16058/CA/NCI NIH HHS; R01 CA073698-04A1/CA/NCI NIH HHS; R01 CA73698/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Estrogen Receptor alpha; 0/Leupeptins; 0/Multienzyme Complexes; 0/Receptors, Estrogen; 0/TGFB1 protein, human; 0/Transforming Growth Factor beta; 0/Transforming Growth Factor beta1; 0/Ubiquitin; 133407-82-6/benzyloxycarbonylleucyl-leucyl-leucine aldehyde; 50-28-2/Estradiol; 59-14-3/Bromodeoxyuridine; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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