Muscle Atrophy

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The originating physiological occurrence resulting in muscle atrophy appears to be the loss of muscle tension. Today, a good amount of the physiology of muscle atrophy has been categorized. Still, not much is understood about the causes or the molecular signaling events motivating this occurrence. The rise in protein degradation and reduction in protein synthesis have been found to be responsible for leading to muscle protein loss because of disuse. Modern research has explained components of both the synthetic and proteolytic activities leading atrophy of muscle in humans. Also, it is now determined that certain connections between acknowledged proteolytic pathways including ubiquitin-proteasome, lysosomal, and calpain are a part of the muscle …show more content…
One such mechanism is hypertrophy, which is an increase in the size of myofibers. A second mechanism is hyperplasia, which is the increase in the number of myofibers. In the scientific community, it is largely established that during the perinatal period the number of fibers in a muscle is set. Still, it has been proposed that myofiber splitting happens if the myofiber size becomes too big. This proposition has not been conveyed in human beings. It has also been seen that new myofibers could develop due to the fusion of satellite cells and small myotubes. Also, it is found that myofibers conveying myogenic markers may be seen in human muscle after periods of training. Though, the general agreement is that an upsurge in cross-sectional area is mainly a result of an escalation of myofiber cross-sectional area and not the number of …show more content…
AKT1 seems to be central for regulation of the growth of muscle. On the other hand, AKT2 seems to be related to metabolism. It has been discovered that the downstream of AKT is mTOR. It creates two complexes with additional molecules known as mTORC1 and mTORC2. It has been determined that mTORC1 is related to the regulation of protein synthesis and it is sensitive to rapamycin. The name mTOR, which stands for mammalian target of rapamycin, helps show this. It has been seen that mTORC2 is related to regulating the actin cytoskeleton and it is not sensitive to rapamycin. The mTORC2 complex activates the translational regulators p70S6-K and 4E-BP1. Phosphorylation of 4E-BP1 leads to the discharge of eIF4E, which is needed for attachment of mRNA to the ribosome. This process starts translation. Phosphorylation of p70S6-K leads to an increase in translation of ribosomal and other mRNAs, which have a 5′ tract of oligopyrimidines. Consequently, mTORC1 may control the biogenesis of ribosomes and the start of translation. Also, it can be stimulated by essential amino acids like
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