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Heat shock proteins in long-lived worms and mice with insulin/insulin-Like signaling mutations

Heat shock proteins (HSPs) have proven to be effective tools for extending invertebrate lifespan, and inC. elegans daf-2 mutants, longevity resulting from loss of insulin / insulin-like signals is at least partly dependent upon elevated HSP expression. In mice, inhibition of the orthologous growth h...

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Detalles Bibliográficos
Autor principal: Swindell, William R.
Formato: Texto
Lenguaje:English
Publicado: Impact Journals LLC 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2806032/
https://www.ncbi.nlm.nih.gov/pubmed/20157538
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author Swindell, William R.
author_facet Swindell, William R.
author_sort Swindell, William R.
collection PubMed
description Heat shock proteins (HSPs) have proven to be effective tools for extending invertebrate lifespan, and inC. elegans daf-2 mutants, longevity resulting from loss of insulin / insulin-like signals is at least partly dependent upon elevated HSP expression. In mice, inhibition of the orthologous growth hormone / insulin-like growth factor I (GH / IGF-I) pathway has similar pro-longevity effects. A recent study, however, suggests that loss of GH / IGF-I signals in long-lived mice does not broadly elevate HSP expression, but in fact decreases HSP expression in many tissue types, such as liver and kidney. The contribution of chaperones to the longevity of long-lived mice with altered GH / IGF-I signals may therefore differ from that described in C. elegans daf-2 mutants. This result, in combination with other recent findings, underscores the possibility that systemic overexpression of chaperones will have dissimilar effects on longevity in vertebrate and invertebrate systems.
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spelling pubmed-28060322010-02-12 Heat shock proteins in long-lived worms and mice with insulin/insulin-Like signaling mutations Swindell, William R. Aging (Albany NY) Research Perspective Heat shock proteins (HSPs) have proven to be effective tools for extending invertebrate lifespan, and inC. elegans daf-2 mutants, longevity resulting from loss of insulin / insulin-like signals is at least partly dependent upon elevated HSP expression. In mice, inhibition of the orthologous growth hormone / insulin-like growth factor I (GH / IGF-I) pathway has similar pro-longevity effects. A recent study, however, suggests that loss of GH / IGF-I signals in long-lived mice does not broadly elevate HSP expression, but in fact decreases HSP expression in many tissue types, such as liver and kidney. The contribution of chaperones to the longevity of long-lived mice with altered GH / IGF-I signals may therefore differ from that described in C. elegans daf-2 mutants. This result, in combination with other recent findings, underscores the possibility that systemic overexpression of chaperones will have dissimilar effects on longevity in vertebrate and invertebrate systems. Impact Journals LLC 2009-06-15 /pmc/articles/PMC2806032/ /pubmed/20157538 Text en Copyright: ©2009 Swindell. http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Perspective
Swindell, William R.
Heat shock proteins in long-lived worms and mice with insulin/insulin-Like signaling mutations
title Heat shock proteins in long-lived worms and mice with insulin/insulin-Like signaling mutations
title_full Heat shock proteins in long-lived worms and mice with insulin/insulin-Like signaling mutations
title_fullStr Heat shock proteins in long-lived worms and mice with insulin/insulin-Like signaling mutations
title_full_unstemmed Heat shock proteins in long-lived worms and mice with insulin/insulin-Like signaling mutations
title_short Heat shock proteins in long-lived worms and mice with insulin/insulin-Like signaling mutations
title_sort heat shock proteins in long-lived worms and mice with insulin/insulin-like signaling mutations
topic Research Perspective
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2806032/
https://www.ncbi.nlm.nih.gov/pubmed/20157538
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