PMID- 16365096 OWN - NLM STAT- MEDLINE DCOM- 20060302 LR - 20230216 IS - 0022-3166 (Print) IS - 0022-3166 (Linking) VI - 136 IP - 1 Suppl DP - 2006 Jan TI - Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise. PG - 269S-73S LID - 10.1093/jn/136.1.269S [doi] AB - BCAAs (leucine, isoleucine, and valine), particularly leucine, have anabolic effects on protein metabolism by increasing the rate of protein synthesis and decreasing the rate of protein degradation in resting human muscle. Also, during recovery from endurance exercise, BCAAs were found to have anabolic effects in human muscle. These effects are likely to be mediated through changes in signaling pathways controlling protein synthesis. This involves phosphorylation of the mammalian target of rapamycin (mTOR) and sequential activation of 70-kD S6 protein kinase (p70 S6 kinase) and the eukaryotic initiation factor 4E-binding protein 1. Activation of p70 S6 kinase, and subsequent phopsphorylation of the ribosomal protein S6, is associated with enhanced translation of specific mRNAs. When BCAAs were supplied to subjects during and after one session of quadriceps muscle resistance exercise, an increase in mTOR, p70 S6 kinase, and S6 phosphorylation was found in the recovery period after the exercise with no effect of BCAAs on Akt or glycogen synthase kinase 3 (GSK-3) phosphorylation. Exercise without BCAA intake led to a partial phosphorylation of p70 S6 kinase without activating the enzyme, a decrease in Akt phosphorylation, and no change in GSK-3. It has previously been shown that leucine infusion increases p70 S6 kinase phosphorylation in an Akt-independent manner in resting subjects; however, a relation between mTOR and p70 S6 kinase has not been reported previously. The results suggest that BCAAs activate mTOR and p70 S6 kinase in human muscle in the recovery period after exercise and that GSK-3 is not involved in the anabolic action of BCAAs on human muscle. FAU - Blomstrand, Eva AU - Blomstrand E AD - Department of Surgical Science, Karolinska Institutet, Stockholm, Sweden. eva.blomstrand@gih.se FAU - Eliasson, Jorgen AU - Eliasson J FAU - Karlsson, Hakan K R AU - Karlsson HK FAU - Kohnke, Rickard AU - Kohnke R LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PT - Review PL - United States TA - J Nutr JT - The Journal of nutrition JID - 0404243 RN - 0 (Amino Acids, Branched-Chain) RN - EC 2.7.- (Protein Kinases) RN - EC 2.7.1.1 (MTOR protein, human) RN - EC 2.7.11.1 (Proto-Oncogene Proteins c-akt) RN - EC 2.7.11.1 (Ribosomal Protein S6 Kinases, 70-kDa) RN - EC 2.7.11.1 (TOR Serine-Threonine Kinases) RN - EC 2.7.11.26 (Glycogen Synthase Kinase 3) RN - EC 2.7.11.26 (glycogen synthase kinase 3 alpha) SB - IM MH - Amino Acids, Branched-Chain/*pharmacology MH - *Exercise MH - Glycogen Synthase Kinase 3/metabolism MH - Humans MH - Muscle, Skeletal/metabolism MH - Phosphorylation MH - *Protein Biosynthesis MH - Protein Kinases/metabolism MH - Proto-Oncogene Proteins c-akt/metabolism MH - Ribosomal Protein S6 Kinases, 70-kDa/metabolism MH - Signal Transduction MH - TOR Serine-Threonine Kinases RF - 48 EDAT- 2005/12/21 09:00 MHDA- 2006/03/03 09:00 CRDT- 2005/12/21 09:00 PHST- 2005/12/21 09:00 [pubmed] PHST- 2006/03/03 09:00 [medline] PHST- 2005/12/21 09:00 [entrez] AID - S0022-3166(22)08047-6 [pii] AID - 10.1093/jn/136.1.269S [doi] PST - ppublish SO - J Nutr. 2006 Jan;136(1 Suppl):269S-73S. doi: 10.1093/jn/136.1.269S.