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Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress

Stress induces the synthesis of several large and small heat shock proteins (hsp's). Two related small hsp's, hsp25 and alpha B crystallin exist in mice. alpha B crystallin is an abundant protein in several tissues even in the absence of stress. Particularly high amounts accumulate in the...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1993
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119529/
https://www.ncbi.nlm.nih.gov/pubmed/8425893
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collection PubMed
description Stress induces the synthesis of several large and small heat shock proteins (hsp's). Two related small hsp's, hsp25 and alpha B crystallin exist in mice. alpha B crystallin is an abundant protein in several tissues even in the absence of stress. Particularly high amounts accumulate in the eye lens. Here we show that hsp25 is likewise constitutively expressed in many normal adult tissues. In the absence of stress the protein is most abundant in the eye lens, heart, stomach, colon, lung, and bladder. The stress-independent expression pattern of the two small hsp's is distinct. In several tissues the amount of hsp25 exceeds that accumulating in NIH 3T3 fibroblasts in response to heat stress. hsp25, like alpha B crystallin, exists in a highly aggregated form in the eye lens. The expression of hsp25 and alpha B crystallin in normal tissues suggests an essential, but distinct function of the two related proteins under standard physiological conditions.
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spelling pubmed-21195292008-05-01 Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress J Cell Biol Articles Stress induces the synthesis of several large and small heat shock proteins (hsp's). Two related small hsp's, hsp25 and alpha B crystallin exist in mice. alpha B crystallin is an abundant protein in several tissues even in the absence of stress. Particularly high amounts accumulate in the eye lens. Here we show that hsp25 is likewise constitutively expressed in many normal adult tissues. In the absence of stress the protein is most abundant in the eye lens, heart, stomach, colon, lung, and bladder. The stress-independent expression pattern of the two small hsp's is distinct. In several tissues the amount of hsp25 exceeds that accumulating in NIH 3T3 fibroblasts in response to heat stress. hsp25, like alpha B crystallin, exists in a highly aggregated form in the eye lens. The expression of hsp25 and alpha B crystallin in normal tissues suggests an essential, but distinct function of the two related proteins under standard physiological conditions. The Rockefeller University Press 1993-02-01 /pmc/articles/PMC2119529/ /pubmed/8425893 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress
title Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress
title_full Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress
title_fullStr Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress
title_full_unstemmed Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress
title_short Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress
title_sort expression of the murine small heat shock proteins hsp 25 and alpha b crystallin in the absence of stress
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119529/
https://www.ncbi.nlm.nih.gov/pubmed/8425893