Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2011-1-3
pubmed:abstractText
The marked increase in skeletal muscle mass during the neonatal period is largely due to a high rate of postprandial protein synthesis that is modulated by an enhanced sensitivity to insulin and amino acids. The amino acid signaling pathway leading to the stimulation of protein synthesis has not been fully elucidated. Among the amino acids, leucine is considered to be a principal anabolic agent that regulates protein synthesis. mTORC1, which controls protein synthesis, has been implicated as a target for leucine. Until recently, there have been few studies exploring the role of amino acids in enhancing muscle protein synthesis in vivo. In this review, we discuss amino acid-induced protein synthesis in muscle in the neonate, focusing on current knowledge of the role of amino acids in the activation of mTORC1 leading to mRNA translation. The role of the amino acid transporters, SNAT2, LAT1, and PAT, in the modulation of mTORC1 activation and the role of amino acids in the activation of putative regulators of mTORC1, i.e., raptor, Rheb, MAP4K3, Vps34, and Rag GTPases, are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport System A, http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport Systems, http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids, http://linkedlifedata.com/resource/pubmed/chemical/Class III Phosphatidylinositol..., http://linkedlifedata.com/resource/pubmed/chemical/Large Neutral Amino..., http://linkedlifedata.com/resource/pubmed/chemical/Leucine, http://linkedlifedata.com/resource/pubmed/chemical/MAP4K3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Monomeric GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RHEB protein, human, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RPTOR protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SLC36A1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SLC38A2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Symporters, http://linkedlifedata.com/resource/pubmed/chemical/mTORC1 complex, human, http://linkedlifedata.com/resource/pubmed/chemical/ras Guanine Nucleotide Exchange...
pubmed:status
MEDLINE
pubmed:issn
1093-4715
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1445-60
pubmed:dateRevised
2011-8-1
pubmed:meshHeading
pubmed-meshheading:21196241-Adaptor Proteins, Signal Transducing, pubmed-meshheading:21196241-Amino Acid Transport System A, pubmed-meshheading:21196241-Amino Acid Transport Systems, pubmed-meshheading:21196241-Amino Acids, pubmed-meshheading:21196241-Animals, pubmed-meshheading:21196241-Animals, Newborn, pubmed-meshheading:21196241-Class III Phosphatidylinositol 3-Kinases, pubmed-meshheading:21196241-Humans, pubmed-meshheading:21196241-Infant, Newborn, pubmed-meshheading:21196241-Large Neutral Amino Acid-Transporter 1, pubmed-meshheading:21196241-Leucine, pubmed-meshheading:21196241-Monomeric GTP-Binding Proteins, pubmed-meshheading:21196241-Muscle, Skeletal, pubmed-meshheading:21196241-Muscle Proteins, pubmed-meshheading:21196241-Neuropeptides, pubmed-meshheading:21196241-Protein Biosynthesis, pubmed-meshheading:21196241-Protein-Serine-Threonine Kinases, pubmed-meshheading:21196241-Proteins, pubmed-meshheading:21196241-RNA, Messenger, pubmed-meshheading:21196241-Signal Transduction, pubmed-meshheading:21196241-Swine, pubmed-meshheading:21196241-Symporters, pubmed-meshheading:21196241-ras Guanine Nucleotide Exchange Factors
pubmed:year
2011
pubmed:articleTitle
Regulation of protein synthesis by amino acids in muscle of neonates.
pubmed:affiliation
United States Department Of Agriculture/Agriculture Research Service, Children's Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, Texas 77030, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, N.I.H., Extramural