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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Main Authors: Brian McDonagh, Giorgos K. Sakellariou, Neil T. Smith, Philip Brownridge, Malcolm J. Jackson
Format: Article
Language:English
Published: Elsevier 2015-09-01
Series:Data in Brief
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2352340915001079
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author Brian McDonagh
Giorgos K. Sakellariou
Neil T. Smith
Philip Brownridge
Malcolm J. Jackson
author_facet Brian McDonagh
Giorgos K. Sakellariou
Neil T. Smith
Philip Brownridge
Malcolm J. Jackson
author_sort Brian McDonagh
collection DOAJ
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 doaj.art-2a6d01308a6048ce93cdfd8f25b76bba2022-12-21T18:44:09ZengElsevierData in Brief2352-34092015-09-014C34434810.1016/j.dib.2015.06.012Redox proteomic analysis of the gastrocnemius muscle from adult and old miceBrian McDonagh0Giorgos K. Sakellariou1Neil T. Smith2Philip Brownridge3Malcolm J. Jackson4Skeletal Muscle Pathophysiology Group, MRC-Arthritis Research UK Centre for Integrated Research into Musculoskeletal Aging (CIMA), Institute of Ageing and Chronic Disease, University of Liverpool, United KingdomSkeletal Muscle Pathophysiology Group, MRC-Arthritis Research UK Centre for Integrated Research into Musculoskeletal Aging (CIMA), Institute of Ageing and Chronic Disease, University of Liverpool, United KingdomSkeletal Muscle Pathophysiology Group, MRC-Arthritis Research UK Centre for Integrated Research into Musculoskeletal Aging (CIMA), Institute of Ageing and Chronic Disease, University of Liverpool, United KingdomCentre for Proteome Research, Institute of Integrative Biology, University of Liverpool, United KingdomSkeletal Muscle Pathophysiology Group, MRC-Arthritis Research UK Centre for Integrated Research into Musculoskeletal Aging (CIMA), Institute of Ageing and Chronic Disease, University of Liverpool, United KingdomThe 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.http://www.sciencedirect.com/science/article/pii/S2352340915001079Redox proteomicsSkeletal muscleAgingOxidative stress
spellingShingle Brian McDonagh
Giorgos K. Sakellariou
Neil T. Smith
Philip Brownridge
Malcolm J. Jackson
Redox proteomic analysis of the gastrocnemius muscle from adult and old mice
Data in Brief
Redox proteomics
Skeletal muscle
Aging
Oxidative stress
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 Redox proteomics
Skeletal muscle
Aging
Oxidative stress
url http://www.sciencedirect.com/science/article/pii/S2352340915001079
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