In the skeletal muscle, the ageing process is characterized by a loss of muscle mass and strength, coupled with a decline of mitochondrial function and a decrease of satellite cells. This profile is more pronounced in hindlimb than in forelimb muscles, both in humans and in rodents. Utilizing light and electron microscopy, myosin heavy chain isoform distribution, proteomic analysis by 2D-DIGE, MALDI-TOF MS and quantitative immunoblotting, this study analyzes the protein levels and the nuclear localization of specific molecules, which can contribute to a preferential muscle loss. Our results identify the molecular changes in the hindlimb (gastrocnemius) and forelimb (triceps) muscles during ageing in rats (3- and 22-month-old). Specifically, the oxidative metabolism contributes to tissue homeostasis in triceps, whereas respiratory chain disruption and oxidative-stress-induced damage imbalance the homeostasis in gastrocnemius muscle. High levels of dihydrolipoyllysine-residue acetyltransferase (Dlat) and ATP synthase subunit alpha (Atp5a1) are detected in triceps and gastrocnemius, respectively. Interestingly, in triceps, both molecules are increased in the nucleus in aged rats and are associated to an increased protein acetylation and myoglobin availability. Furthermore, autophagy is retained in triceps whereas an enhanced fusion, decrement of mitophagy and of regenerative potential is observed in aged gastrocnemius muscle.

Specific protein changes contribute to the differential muscle mass loss during ageing / D. Capitanio, M. Vasso, S. De Palma, C. Fania, E. Torretta, F.P. Cammarata, V. Magnaghi, P. Procacci, C. Gelfi, D. Capitanio. - In: PROTEOMICS. - ISSN 1615-9853. - 16:4(2016 Feb), pp. 645-656. [10.1002/pmic.201500395]

Specific protein changes contribute to the differential muscle mass loss during ageing

D. Capitanio
Primo
;
M. Vasso
Secondo
;
S. De Palma;C. Fania;E. Torretta;F.P. Cammarata;V. Magnaghi;P. Procacci
Penultimo
;
C. Gelfi
Ultimo
;
D. Capitanio
2016

Abstract

In the skeletal muscle, the ageing process is characterized by a loss of muscle mass and strength, coupled with a decline of mitochondrial function and a decrease of satellite cells. This profile is more pronounced in hindlimb than in forelimb muscles, both in humans and in rodents. Utilizing light and electron microscopy, myosin heavy chain isoform distribution, proteomic analysis by 2D-DIGE, MALDI-TOF MS and quantitative immunoblotting, this study analyzes the protein levels and the nuclear localization of specific molecules, which can contribute to a preferential muscle loss. Our results identify the molecular changes in the hindlimb (gastrocnemius) and forelimb (triceps) muscles during ageing in rats (3- and 22-month-old). Specifically, the oxidative metabolism contributes to tissue homeostasis in triceps, whereas respiratory chain disruption and oxidative-stress-induced damage imbalance the homeostasis in gastrocnemius muscle. High levels of dihydrolipoyllysine-residue acetyltransferase (Dlat) and ATP synthase subunit alpha (Atp5a1) are detected in triceps and gastrocnemius, respectively. Interestingly, in triceps, both molecules are increased in the nucleus in aged rats and are associated to an increased protein acetylation and myoglobin availability. Furthermore, autophagy is retained in triceps whereas an enhanced fusion, decrement of mitophagy and of regenerative potential is observed in aged gastrocnemius muscle.
2D-DIGE; Animal proteomics; Intermediate metabolism; Mass spectrometry; Muscle ageing; Muscle proteome
Settore BIO/12 - Biochimica Clinica e Biologia Molecolare Clinica
Settore BIO/10 - Biochimica
Settore BIO/09 - Fisiologia
Identifying and validating pre-clinical biomarkers for diagnostics and therapeurtics of Neuromuscolar Disorders
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/366734
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