Poly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain.

Proteostasis is critical for the maintenance of life. In neuronal cells an imbalance between protein synthesis and degradation is thought to be involved in the pathogenesis of neurodegenerative diseases during aging. Partly, this seems to be due to a decrease in the activity of the ubiquitin-proteas...

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Autores principales:	Carolin Giannini, Alexander Kloß, Sabrina Gohlke, Michele Mishto, Thomas P Nicholson, Paul W Sheppard, Peter-Michael Kloetzel, Burkhardt Dahlmann
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a35a41333648407d91fdc5a9b6e666b6
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spelling	oai:doaj.org-article:a35a41333648407d91fdc5a9b6e666b62021-11-18T07:46:25ZPoly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain.1932-620310.1371/journal.pone.0064042https://doaj.org/article/a35a41333648407d91fdc5a9b6e666b62013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23667697/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Proteostasis is critical for the maintenance of life. In neuronal cells an imbalance between protein synthesis and degradation is thought to be involved in the pathogenesis of neurodegenerative diseases during aging. Partly, this seems to be due to a decrease in the activity of the ubiquitin-proteasome system, wherein the 20S/26S proteasome complexes catalyse the proteolytic step. We have characterised 20S and 26S proteasomes from cerebrum, cerebellum and hippocampus of 3 weeks old (young) and 24 month old (aged) rats. Our data reveal that the absolute amount of the proteasome is not dfferent between both age groups. Within the majority of standard proteasomes in brain the minute amounts of immuno-subunits are slightly increased in aged rat brain. While this goes along with a decrease in the activities of 20S and 26S proteasomes to hydrolyse synthetic fluorogenic tripeptide substrates from young to aged rats, the capacity of 26S proteasomes for degradation of poly-Ub-model substrates and its activation by poly-Ub-substrates is not impaired or even slightly increased in brain of aged rats. We conclude that these alterations in proteasome properties are important for maintaining proteostasis in the brain during an uncomplicated aging process.Carolin GianniniAlexander KloßSabrina GohlkeMichele MishtoThomas P NicholsonPaul W SheppardPeter-Michael KloetzelBurkhardt DahlmannPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 5, p e64042 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Carolin Giannini Alexander Kloß Sabrina Gohlke Michele Mishto Thomas P Nicholson Paul W Sheppard Peter-Michael Kloetzel Burkhardt Dahlmann Poly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain.
description	Proteostasis is critical for the maintenance of life. In neuronal cells an imbalance between protein synthesis and degradation is thought to be involved in the pathogenesis of neurodegenerative diseases during aging. Partly, this seems to be due to a decrease in the activity of the ubiquitin-proteasome system, wherein the 20S/26S proteasome complexes catalyse the proteolytic step. We have characterised 20S and 26S proteasomes from cerebrum, cerebellum and hippocampus of 3 weeks old (young) and 24 month old (aged) rats. Our data reveal that the absolute amount of the proteasome is not dfferent between both age groups. Within the majority of standard proteasomes in brain the minute amounts of immuno-subunits are slightly increased in aged rat brain. While this goes along with a decrease in the activities of 20S and 26S proteasomes to hydrolyse synthetic fluorogenic tripeptide substrates from young to aged rats, the capacity of 26S proteasomes for degradation of poly-Ub-model substrates and its activation by poly-Ub-substrates is not impaired or even slightly increased in brain of aged rats. We conclude that these alterations in proteasome properties are important for maintaining proteostasis in the brain during an uncomplicated aging process.
format	article
author	Carolin Giannini Alexander Kloß Sabrina Gohlke Michele Mishto Thomas P Nicholson Paul W Sheppard Peter-Michael Kloetzel Burkhardt Dahlmann
author_facet	Carolin Giannini Alexander Kloß Sabrina Gohlke Michele Mishto Thomas P Nicholson Paul W Sheppard Peter-Michael Kloetzel Burkhardt Dahlmann
author_sort	Carolin Giannini
title	Poly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain.
title_short	Poly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain.
title_full	Poly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain.
title_fullStr	Poly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain.
title_full_unstemmed	Poly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain.
title_sort	poly-ub-substrate-degradative activity of 26s proteasome is not impaired in the aging rat brain.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/a35a41333648407d91fdc5a9b6e666b6
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Poly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain.

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