Format

Send to

Choose Destination
Biochem Biophys Res Commun. 2004 Jan 9;313(2):417-22.

Regulation of protein synthesis by branched-chain amino acids in vivo.

Author information

1
Department of Animal Science, Utsunomiya University, Utsunomiya, Tochigi 321-8505, Japan. fumiaki@cc.utsunomiya-u.ac.jp

Abstract

Recent advances in the understanding of mRNA translation have facilitated molecular studies on the regulation of protein synthesis by nutrients and the interplay between nutrients and hormonal signals. Numerous reports have established that, in skeletal muscle, the branched-chain amino acids (BCAAs) have the unique ability to initiate signal transduction pathways that modulate translation initiation. Of the BCAAs, leucine is the most potent. Oral administration of leucine to food-deprived rats enhances muscle protein synthesis, in part, through activation of the mRNA binding step of translation initiation. Interestingly, leucine signaling in skeletal muscle differs from that in liver, suggesting that the responses may be tissue specific. The purpose of this paper was to briefly review the current knowledge of how BCAAs act as regulators of protein synthesis in physiologically important tissues, with particular focus on the mechanisms by which BCAAs regulate translation initiation.

PMID:
14684178
DOI:
10.1016/j.bbrc.2003.07.013
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center