Relation between glutamine, branched-chain amino acids, and protein metabolism
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem, přehledy
PubMed
11844643
DOI
10.1016/s0899-9007(01)00767-5
PII: S0899900701007675
Knihovny.cz E-zdroje
- MeSH
- alanin biosyntéza metabolismus MeSH
- glutamin biosyntéza metabolismus MeSH
- játra metabolismus MeSH
- kosterní svaly metabolismus MeSH
- kritický stav MeSH
- krysa rodu Rattus MeSH
- lidé MeSH
- proteiny metabolismus MeSH
- větvené aminokyseliny metabolismus MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
- Názvy látek
- alanin MeSH
- glutamin MeSH
- proteiny MeSH
- větvené aminokyseliny MeSH
The branched-chain amino acids (BCAAs; valine, isoleucine, and leucine) are the major nitrogen source for glutamine and alanine synthesis in muscle. Synthesis of glutamine, alanine, and BCAA use is activated in critical illnesses such as in sepsis, cancer, and trauma. The use of glutamine often exceeds its synthesis, resulting in the lack of glutamine in plasma and tissues. In critical illness, resynthesis of BCAA from branched-chain keto acids is activated, particularly in hepatic tissue. The BCAA released to circulation may be used for protein synthesis or synthesis of alanine and glutamine. Glutamine and/or alanine infusion has an inhibitory effect on the breakdown of body proteins and decreases BCAA catabolism in postabsorptive control, endotoxemic, and irradiated rats. Decreased protein breakdown also was observed when glutamine synthesis was activated by ammonia infusion. In conclusion some favorable effects of BCAA supply can be explained by its role in the synthesis of glutamine and some positive effects of glutamine exogenous supply can be explained by its effect on metabolism of BCAA.
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