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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Elsevier
2015-09-01
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Series: | Data in Brief |
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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. |
first_indexed | 2024-12-22T01:02:58Z |
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issn | 2352-3409 |
language | English |
last_indexed | 2024-12-22T01:02:58Z |
publishDate | 2015-09-01 |
publisher | Elsevier |
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series | Data in Brief |
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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