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Proteomic features of skeletal muscle adaptation to resistance exercise training as a function of age

Proteomic features of skeletal muscle adaptation to resistance exercise training as a function of age
Proteomic features of skeletal muscle adaptation to resistance exercise training as a function of age
Resistance exercise training (RET) can counteract negative features of muscle ageing but older age associates with reduced adaptive capacity to RET. Altered muscle protein networks likely contribute to ageing RET adaptation; therefore, associated proteome-wide responses warrant exploration. We employed quantitative sarcoplasmic proteomics to compare age-related proteome and phosphoproteome responses to RET. Thigh muscle biopsies were collected from eight young (25 ± 1.1 years) and eight older (67.5 ± 2.6 years) adults before and after 20 weeks supervised RET. Muscle sarcoplasmic fractions were pooled for each condition and analysed using Isobaric Tags for Relative and Absolute Quantification (iTRAQ) labelling, tandem mass spectrometry and network-based hub protein identification. Older adults displayed impaired RET-induced adaptations in whole-body lean mass, body fat percentage and thigh lean mass (P > 0.05). iTRAQ identified 73 differentially expressed proteins with age and/or RET. Despite possible proteomic stochasticity, RET improved ageing profiles for mitochondrial function and glucose metabolism (top hub; PYK (pyruvate kinase)) but failed to correct altered ageing expression of cytoskeletal proteins (top hub; YWHAZ (14-3-3 protein zeta/delta)). These ageing RET proteomic profiles were generally unchanged or oppositely regulated post-RET in younger muscle. Similarly, RET corrected expression of 10 phosphoproteins altered in ageing, but these responses were again different vs. younger adults. Older muscle is characterised by RET-induced metabolic protein profiles that, whilst not present in younger muscle, improve untrained age-related proteomic deficits. Combined with impaired cytoskeletal adhesion responses, these results provide a proteomic framework for understanding and optimising ageing muscle RET adaptation.
Deane, Colleen S
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Deane, Colleen S
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Phillips, BE
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Willis, CRG
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Wilkinson, DJ
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Smith, K
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Higashitani, N
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Williams, JP
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Szewczyk, NJ
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Atherton, PJ
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Higashitani, A
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Etheridge, T
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Deane, Colleen S
3320532e-f411-4ea8-9a14-4a9f248da898
Deane, Colleen S
3320532e-f411-4ea8-9a14-4a9f248da898
Phillips, BE
610a353f-5782-44b8-95b9-b2ad8354fc9c
Willis, CRG
52567102-755b-42ac-9f61-e7cd392f7b35
Wilkinson, DJ
c690a110-b3ff-4281-9588-b619c4f16904
Smith, K
b91c1242-9722-4644-afc9-adfa516437de
Higashitani, N
aa966bdc-1040-48f5-964f-792273e0dadf
Williams, JP
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Szewczyk, NJ
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Atherton, PJ
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Higashitani, A
b69569b0-5699-41d1-adde-d55980414a5c
Etheridge, T
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Deane, Colleen S, Deane, Colleen S, Phillips, BE, Willis, CRG, Wilkinson, DJ, Smith, K, Higashitani, N, Williams, JP, Szewczyk, NJ, Atherton, PJ, Higashitani, A and Etheridge, T (2022) Proteomic features of skeletal muscle adaptation to resistance exercise training as a function of age. GeroScience. (doi:10.1007/s11357-022-00658-5).

Record type: Article

Abstract

Resistance exercise training (RET) can counteract negative features of muscle ageing but older age associates with reduced adaptive capacity to RET. Altered muscle protein networks likely contribute to ageing RET adaptation; therefore, associated proteome-wide responses warrant exploration. We employed quantitative sarcoplasmic proteomics to compare age-related proteome and phosphoproteome responses to RET. Thigh muscle biopsies were collected from eight young (25 ± 1.1 years) and eight older (67.5 ± 2.6 years) adults before and after 20 weeks supervised RET. Muscle sarcoplasmic fractions were pooled for each condition and analysed using Isobaric Tags for Relative and Absolute Quantification (iTRAQ) labelling, tandem mass spectrometry and network-based hub protein identification. Older adults displayed impaired RET-induced adaptations in whole-body lean mass, body fat percentage and thigh lean mass (P > 0.05). iTRAQ identified 73 differentially expressed proteins with age and/or RET. Despite possible proteomic stochasticity, RET improved ageing profiles for mitochondrial function and glucose metabolism (top hub; PYK (pyruvate kinase)) but failed to correct altered ageing expression of cytoskeletal proteins (top hub; YWHAZ (14-3-3 protein zeta/delta)). These ageing RET proteomic profiles were generally unchanged or oppositely regulated post-RET in younger muscle. Similarly, RET corrected expression of 10 phosphoproteins altered in ageing, but these responses were again different vs. younger adults. Older muscle is characterised by RET-induced metabolic protein profiles that, whilst not present in younger muscle, improve untrained age-related proteomic deficits. Combined with impaired cytoskeletal adhesion responses, these results provide a proteomic framework for understanding and optimising ageing muscle RET adaptation.

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Accepted/In Press date: 3 September 2022
Published date: 26 September 2022
Additional Information: Funding: TE was supported by a postdoctoral fellowship from the Japan Society for the Promotion of Science and the Royal Society (JSPS/FF1/435). This work was supported by grants from the Medical Research Council (MR/T026014/1 and G0801271) and the Biotechnology and Biological Sciences Research Council (BB/X510697/1 and BB/C516779/1).

Identifiers

Local EPrints ID: 477920
URI: http://eprints.soton.ac.uk/id/eprint/477920
PURE UUID: ad4731e9-f6ac-4c40-823d-404e876d34e2
ORCID for Colleen S Deane: ORCID iD orcid.org/0000-0002-2281-6479
ORCID for Colleen S Deane: ORCID iD orcid.org/0000-0002-2281-6479

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Date deposited: 16 Jun 2023 16:38
Last modified: 17 Mar 2024 04:15

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Contributors

Author: Colleen S Deane ORCID iD
Author: Colleen S Deane ORCID iD
Author: BE Phillips
Author: CRG Willis
Author: DJ Wilkinson
Author: K Smith
Author: N Higashitani
Author: JP Williams
Author: NJ Szewczyk
Author: PJ Atherton
Author: A Higashitani
Author: T Etheridge

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