ArticleInternational journal of molecular medicine2012
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.
Article in International journal of molecular medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.
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Who cites it
45 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Gene Ontology (GO)-Driven Inference of Candidate Proteomic Markers Associated with Muscle Atrophy Conditions.Molecules (Basel, Switzerland) · 2022Pooled it
- Aging concomitantly reduces skeletal muscle proteome plasticity and hypertrophic responses to resistance training in male adults.Physiological reports · 2026Article
- Proteomic Age Acceleration in Multiple Sclerosis Precedes Symptom Onset and Associates with Severity.medRxiv : the preprint server for health sciences · 2026Article
- The skeletal muscle proteomic determinants of neuromuscular function in young and older women following 8 weeks of resistance training.Experimental physiology · 2025Article
- Plasma-derived protein and imaging biomarkers distinguish disease severity in oculopharyngeal muscular dystrophy.Journal of neuromuscular diseases · 2025Article
- Molecular composition of skeletal muscle in infants and adults: a comparative proteomic and transcriptomic study.Scientific reports · 2024Article
- Proteomic reference map for sarcopenia research: mass spectrometric identification of key muscle proteins located in the sarcomere, cytoskeleton and the extracellular matrix.European journal of translational myology · 2024Article
- Proteomic reference map for sarcopenia research: mass spectrometric identification of key muscle proteins of organelles, cellular signaling, bioenergetic metabolism and molecular chaperoning.European journal of translational myology · 2024Article
- Nitrosative Stress in Astronaut Skeletal Muscle in Spaceflight.Antioxidants (Basel, Switzerland) · 2024Article
- Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology.Cells · 2023Review
- Proteomic features of skeletal muscle adaptation to resistance exercise training as a function of age.GeroScience · 2023Article
- Biomarkers of aging.Science China. Life sciences · 2023Review
- Article
- Fiber-Type Shifting in Sarcopenia of Old Age: Proteomic Profiling of the Contractile Apparatus of Skeletal Muscles.International journal of molecular sciences · 2023Review
- Two-CyDye-Based 2D-DIGE Analysis of Aged Human Muscle Biopsy Specimens.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Comparative 3-Sample 2D-DIGE Analysis of Skeletal Muscles.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Article
- Carbonic Anhydrase III Attenuates Hypoxia-Induced Apoptosis and Activates PI3K/Akt/mTOR Pathway in H9c2 Cardiomyocyte Cell Line.Cardiovascular toxicology · 2021Article
- Muscle Proteomic and Transcriptomic Profiling of Healthy Aging and Metabolic Syndrome in Men.International journal of molecular sciences · 2021Article
- Proteomics and Epidemiological Models of Human Aging.Frontiers in physiology · 2021Review
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4 authors.
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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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