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    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


    Staunton, Lisa and Zweyer, Margit and Swandulla, Dieter and Ohlendieck, Kay (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 (4). pp. 723-733. ISSN 1107-3756

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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.

    Item Type: Article
    Additional Information: This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited: 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. http://dx.doi.org/10.3892/ijmm.2012.1056
    Keywords: aging; carbonic anhydrase isoform 3; difference in-gel electrophoresis; sarcopenia; vastus lateralis;
    Academic Unit: Faculty of Science and Engineering > Biology
    Item ID: 6907
    Identification Number: https://doi.org/10.3892/ijmm.2012.1056
    Depositing User: Prof. Kay Ohlendieck
    Date Deposited: 21 Jan 2016 14:41
    Journal or Publication Title: International Journal of Molecular Medicine
    Publisher: Spandidos Publications
    Refereed: Yes
    Funders: Science Foundation Ireland (SFI), Health Research Board (HRB), Higher Education Authority (HEA)
    URI:

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