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Sökning: WFRF:(Eeg Olofsson Orvar) > (2015) > Oxidative proteome ...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004204naa a2200409 4500
001oai:DiVA.org:uu-269644
003SwePub
008151217s2015 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:132710328
024a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-2696442 URI
024a https://doi.org/10.1016/j.redox.2015.05.0062 DOI
024a http://kipublications.ki.se/Default.aspx?queryparsed=id:1327103282 URI
040 a (SwePub)uud (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Lourenço Dos Santos, Sofiau Sorbonne Universités, UPMC Univ Paris 06, UMR 8256, Biological Adaptation and Ageing-IBPS, Paris, France4 aut
2451 0a Oxidative proteome alterations during skeletal muscle ageing
264 1b Elsevier BV,c 2015
338 a electronic2 rdacarrier
520 a Sarcopenia corresponds to the degenerative loss of skeletal muscle mass, quality, and strength associated with ageing and leads to a progressive impairment of mobility and quality of life. However, the cellular and molecular mechanisms involved in this process are not completely understood. A hallmark of cellular and tissular ageing is the accumulation of oxidatively modified (carbonylated) proteins, leading to a decreased quality of the cellular proteome that could directly impact on normal cellular functions. Although increased oxidative stress has been reported during skeletal muscle ageing, the oxidized protein targets, also referred as to the 'oxi-proteome' or 'carbonylome', have not been characterized yet. To better understand the mechanisms by which these damaged proteins build up and potentially affect muscle function, proteins targeted by these modifications have been identified in human rectus abdominis muscle obtained from young and old healthy donors using a bi-dimensional gel electrophoresis-based proteomic approach coupled with immunodetection of carbonylated proteins. Among evidenced protein spots, 17 were found as increased carbonylated in biopsies from old donors comparing to young counterparts. These proteins are involved in key cellular functions such as cellular morphology and transport, muscle contraction and energy metabolism. Importantly, impairment of these pathways has been described in skeletal muscle during ageing. Functional decline of these proteins due to irreversible oxidation may therefore impact directly on the above-mentioned pathways, hence contributing to the generation of the sarcopenic phenotype.
650 7a MEDICIN OCH HÄLSOVETENSKAPx Medicinsk bioteknologix Medicinsk bioteknologi0 (SwePub)304012 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Medical Biotechnologyx Medical Biotechnology0 (SwePub)304012 hsv//eng
700a Baraibar, Martin Au Sorbonne Universités, UPMC Univ Paris 06, UMR 8256, Biological Adaptation and Ageing-IBPS, Paris, France4 aut
700a Lundberg, Staffan,d 1956-u Uppsala universitet,Institutionen för kvinnors och barns hälsa,Barnneurologisk forskning/Ahlsten4 aut0 (Swepub:uu)staflund
700a Eeg-Olofsson, Orvar,d 1932-u Uppsala universitet,Institutionen för kvinnors och barns hälsa,Barnneurologisk forskning/Ahlsten4 aut0 (Swepub:uu)orvareo
700a Larsson, Larsu Karolinska Institutet4 aut
700a Friguet, Bertrandu Sorbonne Universités, UPMC Univ Paris 06, UMR 8256, Biological Adaptation and Ageing-IBPS, Paris, France4 aut
710a Sorbonne Universités, UPMC Univ Paris 06, UMR 8256, Biological Adaptation and Ageing-IBPS, Paris, Franceb Institutionen för kvinnors och barns hälsa4 org
773t Redox Biologyd : Elsevier BVg 5, s. 267-274q 5<267-274x 2213-2317
856u https://doi.org/10.1016/j.redox.2015.05.006y Fulltext
856u https://uu.diva-portal.org/smash/get/diva2:883569/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print
856u https://doi.org/10.1016/j.redox.2015.05.006
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-269644
8564 8u https://doi.org/10.1016/j.redox.2015.05.006
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:132710328

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