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• W1978991257 abstract "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." @default.
• W1978991257 created "2016-06-24" @default.
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• W1978991257 date "2009-07-23" @default.
• W1978991257 modified "2023-10-03" @default.
• W1978991257 title "Production of n-octanoyl-modified Ghrelin in Cultured Cells Requires Prohormone Processing Protease and Ghrelin O-acyltransferase, as well as n-octanoic Acid" @default.
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• W1978991257 doi "https://doi.org/10.1093/jb/mvp112" @default.
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