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.

Capitanio, D., Vasso, M., De Palma, S., Fania, C., Torretta, E., Cammarata, F., et al. (2016). Specific protein changes contribute to the differential muscle mass loss during ageing. PROTEOMICS, 16(4), 645-656 [10.1002/pmic.201500395].

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

Fania, Chiara;
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.
Articolo in rivista - Articolo scientifico
2D-DIGE; Animal proteomics; Intermediate metabolism; Mass spectrometry; Muscle ageing; Muscle proteome;
2D-DIGE; Animal proteomics; Intermediate metabolism; Mass spectrometry; Muscle ageing; Muscle proteome; Animals; Autophagy; Male; Mitochondria; Muscle Proteins; Muscle, Skeletal; Muscular Diseases; Myosin Heavy Chains; Proteomics; Rats, Sprague-Dawley; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Two-Dimensional Difference Gel Electrophoresis; Aging
English
2016
16
4
645
656
none
Capitanio, D., Vasso, M., De Palma, S., Fania, C., Torretta, E., Cammarata, F., et al. (2016). Specific protein changes contribute to the differential muscle mass loss during ageing. PROTEOMICS, 16(4), 645-656 [10.1002/pmic.201500395].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/215249
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