Open Access

Mass spectrometry-based proteomic analysis of middle-aged vs. aged vastus lateralis reveals increased levels of carbonic anhydrase isoform 3 in senescent human skeletal muscle

  • Authors:
    • Lisa Staunton
    • Margit Zweyer
    • Dieter Swandulla
    • Kay Ohlendieck
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  • Published online on: July 6, 2012     https://doi.org/10.3892/ijmm.2012.1056
  • Pages: 723-733
  • Copyright: © Staunton et al. This is an open access article distributed under the terms of Creative Commons Attribution License [CC BY_NC 3.0].

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Abstract

The age-related loss of skeletal muscle mass and associated progressive decline in contractile strength is a serious pathophysiological issue in the elderly. In order to investigate global changes in the skeletal muscle proteome after the fifth decade of life, this study analysed total extracts from human vastus lateralis muscle by fluorescence difference in-gel electrophoresis. Tissue specimens were derived from middle-aged (47-62 years) vs. aged (76-82 years) individuals and potential changes in the protein expression profiles were compared between these two age groups by a comprehensive gel electrophoresis-based survey. Age-dependent alterations in the concentration of 19 protein spots were revealed and mass spectrometry identified these components as being involved in the excitation-contraction-relaxation cycle, muscle metabolism, ion handling and the cellular stress response. This indicates a generally perturbed protein expression pattern in senescent human muscle. Increased levels of mitochondrial enzymes and isoform switching of the key contractile protein, actin, support the idea of glycolytic-to-oxidative and fast-to-slow transition processes during muscle aging. Importantly, the carbonic anhydrase (CA)3 isoform displayed an increased abundance during muscle aging, which was independently verified by immunoblotting of differently aged human skeletal muscle samples. Since the CA3 isoform is relatively muscle-specific and exhibits a fibre type-specific expression pattern, this enzyme may represent an interesting new biomarker of sarcopenia. Increased levels of CA are indicative of an increased demand of CO2-removal in senescent muscle, and also suggest age-related fibre type shifting to slower-contracting muscles during human aging.
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October 2012
Volume 30 Issue 4

Print ISSN: 1107-3756
Online ISSN:1791-244X

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Spandidos Publications style
Staunton L, Zweyer M, Swandulla D and Ohlendieck K: Mass spectrometry-based proteomic analysis of middle-aged vs. aged vastus lateralis reveals increased levels of carbonic anhydrase isoform 3 in senescent human skeletal muscle. Int J Mol Med 30: 723-733, 2012.
APA
Staunton, L., Zweyer, M., Swandulla, D., & Ohlendieck, K. (2012). Mass spectrometry-based proteomic analysis of middle-aged vs. aged vastus lateralis reveals increased levels of carbonic anhydrase isoform 3 in senescent human skeletal muscle. International Journal of Molecular Medicine, 30, 723-733. https://doi.org/10.3892/ijmm.2012.1056
MLA
Staunton, L., Zweyer, M., Swandulla, D., Ohlendieck, K."Mass spectrometry-based proteomic analysis of middle-aged vs. aged vastus lateralis reveals increased levels of carbonic anhydrase isoform 3 in senescent human skeletal muscle". International Journal of Molecular Medicine 30.4 (2012): 723-733.
Chicago
Staunton, L., Zweyer, M., Swandulla, D., Ohlendieck, K."Mass spectrometry-based proteomic analysis of middle-aged vs. aged vastus lateralis reveals increased levels of carbonic anhydrase isoform 3 in senescent human skeletal muscle". International Journal of Molecular Medicine 30, no. 4 (2012): 723-733. https://doi.org/10.3892/ijmm.2012.1056