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
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: |
|
| Use Licence: |
This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available
here |
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