The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation.

The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation. Research Abstract Details 

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The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation. Abstract Text:

Ashraf Said Al-Madhoun,Yong-Xiang Chen,Leila Haidari,Katey Rayner,William Gerthoffer,Heidi McBride,Edward R O'Brien,

Recently, we identified heat shock protein 27 (HSP27) as an estrogen receptor-beta (ERbeta) associated protein that acts as a co-repressor of estrogen signaling and serves as a biomarker of atherosclerosis. In this study, we sought to further characterize the subcellular interaction of HSP27 and ERbeta, as well as explore the factors that may modulate this interaction. In vitro we determined that phosphorylated HSP27 is retained in the cytoplasm after treatment with 17beta-estradiol and to a lesser extent with heat shock. Under all experimental conditions ERbeta was found to be slightly more abundant in the cytoplasm compared to the nucleus. HSP27 and ERbeta associate in both the cytoplasm and nucleus, however, co-localization studies reveal that in the presence of 17beta-estradiol, a significant portion of this interaction occurs outside of the nucleus. These data highlight an extranuclear interaction between ERbeta and HSP27 that may be of potential importance in modulating estrogen signaling.

The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation. Publishing Authors By Initials

AS Al-Madhoun,YX Chen,L Haidari,K Rayner,W Gerthoffer,H McBride,ER O'Brien,

For similar cells: cellular structures: subcellular fractions research abstracts see: cells: cellular structures: subcellular fractions research

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The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Molecular and cellular endocrinology

VOLUME: 270

Page Numbers: 33-42

Journal Abbreviation:

ISSN: 0303-7207

DAY: 13

MONTH: 02

YEAR: 2007

The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7500844

The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation. Keywords Mesh Terms:

KEYWORDS: Subcellular Fractions

MESH TERMS: drug effects

Chemical & Substance for Abstract: The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation. Information

Substance Name: Estradiol

Registry Number: 50-28-2

Grant and Affiliation Information for The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation.

AFFILIATION: University of Ottawa Heart Institute, 40 Ruskin St., Ottawa, Ontario K1Y 4W7, Canada.

Country: Ireland

AGENCY: United States NHLBI

GRANT: HL077726

ACRONYM: HL

MEDLINETA: Mol Cell Endocrinol

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