| First Author | Yamane T | Year | 2018 |
| Journal | Biosci Biotechnol Biochem | Volume | 82 |
| Issue | 4 | Pages | 611-615 |
| PubMed ID | 29191093 | Mgi Jnum | J:341807 |
| Mgi Id | MGI:6740754 | Doi | 10.1080/09168451.2017.1386084 |
| Citation | Yamane T, et al. (2018) Branched-chain amino acids regulate type I tropocollagen and type III tropocollagen syntheses via modulation of mTOR in the skin. Biosci Biotechnol Biochem 82(4):611-615 |
| abstractText | Branched-chain amino acids (BCAAs) exhibit many physiological functions. However, the potential link and mechanism between BCAA and skin function are unknown. We examined the effects of deletion of branched-chain alpha-keto acid dehydrogenase kinase (BDK), a key enzyme in BCAA catabolism, on type I and III tropocollagen syntheses in mice. Leucine and isoleucine levels were significantly lower in the skin of BDK-KO mice compared with wild-type mice. No changes in valine concentrations were observed. The levels of type I and III tropocollagen proteins and mRNAs (COL1A1 and COL3A1) were significantly lower in the skin of BDK-KO mice compared with wild-type mice. The phosphorylation of p70 S6 kinase, which indicates mammalian target of rapamycin (mTOR) activation, was reduced in the skin of BDK-KO mice compared with wild-type mice. These findings suggest that deficiencies of leucine and isoleucine reduce type I and III tropocollagen syntheses in skin by suppressing the action of mTOR. |
