Abstract
Most muscle pathologies are characterized by the progressive loss of muscle tissue due to chronic degeneration combined with the inability of regeneration machinery to replace the damaged muscle. These pathological changes, known as muscle wasting, can be attributed to the activation of several proteolytic systems, such as calpain, ubiquitin-proteasome and caspases, and to the alteration in muscle growth factors. Among them, insulin-like growth factor-1 (IGF-1) has been implicated in the control of skeletal muscle growth, differentiation, survival, and regeneration and has been considered a promising therapeutic agent in staving off the advance of muscle weakness. Here we review the molecular basis of muscle wasting associated with diseases, such as sarcopenia, muscular dystrophy and Amyotrophic Lateral Sclerosis, and discuss the potential therapeutic role of local IGF-1 isoforms in muscle aging and diseases.
Highlights
It is generally accepted that the primary cause of functional impairment in muscle is a cumulative failure to repair damage related to an overall decrease in anabolic processes
Despite numerous theories and intensive research, the principal molecular mechanisms underlying the process of muscle wasting are still unknown
insulin-like growth factor-1 (IGF-1), involved in muscle growth and hypertrophy, decline during postnatal life, raising the prospect that this decline contributes to the progress of muscle atrophy in senescence, and limits the ability of skeletal muscle tissue to effect repair or to regenerate
Summary
It is generally accepted that the primary cause of functional impairment in muscle is a cumulative failure to repair damage related to an overall decrease in anabolic processes. One of the potential candidates is the insulin-like growth factor-1 (IGF-1), involved in several anabolic process in skeletal muscle [7]. The analysis of the amino acid structure of both E-peptides has revealed the presence of two N-linked glycosylation sites only in the Ea peptide, but not in the Eb peptide, suggesting that this post-translational modification is involved in a biological action of the IGF-1 isoform [11].
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