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Redox proteomic analysis of the gastrocnemius muscle from adult and old mice

The data provides information in support of the research article, “Differential Cysteine Labeling and Global Label-Free Proteomics Reveals an Altered Metabolic State in Skeletal Muscle Aging”, Journal of Proteome Research, 2014, 13 (11), 2008–21 [1]. Raw data is available from ProteomeXchange [2] wi...

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Autores principales: McDonagh, Brian, Sakellariou, Giorgos K., Smith, Neil T., Brownridge, Philip, Jackson, Malcolm J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4510572/
https://www.ncbi.nlm.nih.gov/pubmed/26217813
http://dx.doi.org/10.1016/j.dib.2015.06.012
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author McDonagh, Brian
Sakellariou, Giorgos K.
Smith, Neil T.
Brownridge, Philip
Jackson, Malcolm J.
author_facet McDonagh, Brian
Sakellariou, Giorgos K.
Smith, Neil T.
Brownridge, Philip
Jackson, Malcolm J.
author_sort McDonagh, Brian
collection PubMed
description The data provides information in support of the research article, “Differential Cysteine Labeling and Global Label-Free Proteomics Reveals an Altered Metabolic State in Skeletal Muscle Aging”, Journal of Proteome Research, 2014, 13 (11), 2008–21 [1]. Raw data is available from ProteomeXchange [2] with identifier PDX001054. The proteome of gastrocnemius muscle from adult and old mice was analyzed by global label-free proteomics and the relative quantification of specific reduced and reversibly oxidized Cysteine (Cys) residues was performed using Skyline [3]. Briefly, reduced Cysteine (Cys) containing peptides was alkylated using N-ethylmalemide (d0-NEM). Samples were desalted and reversibly oxidized Cys residues were reduced using tris(2-carboxyethyl)phosphine (TCEP) and the newly formed reduced Cys residues were labeled with heavy NEM( d5-NEM). Label-free analysis of the global proteome of adult (n=5) and old (n=4) gastrocnemius muscles was performed using Peaks7™ mass spectrometry data analysis software [4]. Relative quantification of Cys containing peptides that were identified as reduced (d(0) NEM labeled) and reversibly oxidized d(5)–NEM labeled was performed using the intensity of their precursor ions in Skyline. Results indicate that muscles from old mice show reduced redox flexibility particularly in proteins involved in the generation of precursor metabolites and energy metabolism, indicating a loss in the flexibility of the redox energy response.
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spelling pubmed-45105722015-07-27 Redox proteomic analysis of the gastrocnemius muscle from adult and old mice McDonagh, Brian Sakellariou, Giorgos K. Smith, Neil T. Brownridge, Philip Jackson, Malcolm J. Data Brief Data Article The data provides information in support of the research article, “Differential Cysteine Labeling and Global Label-Free Proteomics Reveals an Altered Metabolic State in Skeletal Muscle Aging”, Journal of Proteome Research, 2014, 13 (11), 2008–21 [1]. Raw data is available from ProteomeXchange [2] with identifier PDX001054. The proteome of gastrocnemius muscle from adult and old mice was analyzed by global label-free proteomics and the relative quantification of specific reduced and reversibly oxidized Cysteine (Cys) residues was performed using Skyline [3]. Briefly, reduced Cysteine (Cys) containing peptides was alkylated using N-ethylmalemide (d0-NEM). Samples were desalted and reversibly oxidized Cys residues were reduced using tris(2-carboxyethyl)phosphine (TCEP) and the newly formed reduced Cys residues were labeled with heavy NEM( d5-NEM). Label-free analysis of the global proteome of adult (n=5) and old (n=4) gastrocnemius muscles was performed using Peaks7™ mass spectrometry data analysis software [4]. Relative quantification of Cys containing peptides that were identified as reduced (d(0) NEM labeled) and reversibly oxidized d(5)–NEM labeled was performed using the intensity of their precursor ions in Skyline. Results indicate that muscles from old mice show reduced redox flexibility particularly in proteins involved in the generation of precursor metabolites and energy metabolism, indicating a loss in the flexibility of the redox energy response. Elsevier 2015-07-02 /pmc/articles/PMC4510572/ /pubmed/26217813 http://dx.doi.org/10.1016/j.dib.2015.06.012 Text en © 2015 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Data Article
McDonagh, Brian
Sakellariou, Giorgos K.
Smith, Neil T.
Brownridge, Philip
Jackson, Malcolm J.
Redox proteomic analysis of the gastrocnemius muscle from adult and old mice
title Redox proteomic analysis of the gastrocnemius muscle from adult and old mice
title_full Redox proteomic analysis of the gastrocnemius muscle from adult and old mice
title_fullStr Redox proteomic analysis of the gastrocnemius muscle from adult and old mice
title_full_unstemmed Redox proteomic analysis of the gastrocnemius muscle from adult and old mice
title_short Redox proteomic analysis of the gastrocnemius muscle from adult and old mice
title_sort redox proteomic analysis of the gastrocnemius muscle from adult and old mice
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4510572/
https://www.ncbi.nlm.nih.gov/pubmed/26217813
http://dx.doi.org/10.1016/j.dib.2015.06.012
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