PMC:7601109 / 48533-50159 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7601109","sourcedb":"PMC","sourceid":"7601109","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7601109","text":"Research indicates that age-related skeletal muscle wasting results mainly from insufficient delivery of amino acids to skeletal muscle due to dysregulations in the activity of mTORC1- and activating transcription factor-4 (ATF4)-mediated amino acid sensing pathways. Meanwhile, interventions that ameliorate age-related damages in skeletal muscle operate primarily by reversing alterations in the delivery of amino acids to skeletal muscle via upregulation of mTORC1 and/or ATF4 [139]. mTORC1 is a nutrient sensing protein that acts as a core regulator of protein metabolism. It is sensitive to amino acids, energy status (ATP), stress (e.g., oxidative stress), and growth factors (e.g., insulin), which all can regulate its signaling [2,136]. Nevertheless, bioavailability of amino acids is necessary for growth factors to effectively activate mTORC1. Even more, amino acids on their own can adequately activate mTORC1 [136]. Evidence from preclinical and human studies confirms that ingestion of essential amino acids (similar to those found in royal jelly and bee pollen such as valine) increases cellular bioavailability of amino acids, which is associated with activation of the endothelial nitric oxide synthase (eNOs) pathway. eNOs further upregulates mTORC1 kinase. Translocation of mTORC1 from the cytosol to the surface of lysosomes is associated with improved mitochondrial biogenesis and cellular oxidative capacity in skeletal muscle due to activation of its substrates: P70 ribosomal proteins S6 kinase (S6K) and eukaryotic translation initiation 4E-binding protein 1 (eIF4E, also known as 4eBP1) 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