期刊
JOURNAL OF BIOCHEMISTRY
卷 146, 期 5, 页码 675-682出版社
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvp112
关键词
acyl-modification; ghrelin; GOAT; n-octanoic acid; prohormone convertase
资金
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
- Health and Labour Sciences Research Grants
- Program for Promotion of Basic and Applied Researches for Innovations in Bio-oriented Industry
Ghrelin was originally isolated from rat stomach as an endogenous ligand for the GH secretagogue receptor. The major active form of ghrelin is a 28-amino acid peptide modified by an n-octanoic acid on the serine 3 residue, and this lipid modification is essential for the biological activity of ghrelin. However, it is not clear whether prohormone convertase (PC) and ghrelin O-acyltransferase (GOAT) are the minimal requirements for synthesis of acyl-modified ghrelin in cultured cells. By using three cultured cell lines, TT, AtT20 and COS-7, in which the expression levels of processing proteases and GOAT vary, we examined the processing patterns of ghrelin precursor. We found that not only PC1/3 but also both PC2 and furin could process proghrelin to the 28-amino acid ghrelin. Moreover, the presence of PC and GOAT in the cells, as well as n-octanoic acid in the culture medium, was necessary to produce n-octanoyl ghrelin.
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