@inbook{571fcd8114b847c4aa87653c7d5f5f3c,
title = "Ghrelin O-Acyltransferase Assays and Inhibition",
abstract = "Ghrelin O-acyltransferase (GOAT) is responsible for catalyzing the attachment of the eight-carbon fatty acid octanoyl to the Ser3 side chain of the peptide ghrelin to generate the active form of this metabolic hormone. As such, GOAT is viewed as a potential therapeutic target for the treatment of obesity and diabetes mellitus. Here, we review recent progress in the development of cell and in vitro assays to measure GOAT action and the identification of several synthetic GOAT inhibitors. In particular, we discuss the design, synthesis, and characterization of the bisubstrate analog GO-CoA-Tat and its ability to modulate weight and blood glucose in mice. We also highlight current challenges and future research directions in our biomedical understanding of this fascinating ghrelin processing enzyme.",
keywords = "ELISA, bisubstrate, design, inhibitor, mechanism, metabolism, octanoyl-CoA, peptide, synthetic compound, weight",
author = "Taylor, {Martin S.} and Yousang Hwang and Hsiao, {Po Yuan} and Boeke, {Jef D.} and Cole, {Philip A.}",
note = "Funding Information: We thank Brad Barnett, Dan Leahy, Jun Liu, Paul Pfluger, Henriette Kirchner, Matthias Tsch?p, and Mehboob Hussain for contributions to these studies and for a critical reading of this chapter. We also thank Don Steiner for helpful discussion. Further, we thank the NIH and Pfeiffer Foundation, Kaufman Foundation, and Keck Foundation for financial support. Funding Information: We thank Brad Barnett, Dan Leahy, Jun Liu, Paul Pfluger, Henriette Kirchner, Matthias Tsch{\"o}p, and Mehboob Hussain for contributions to these studies and for a critical reading of this chapter. We also thank Don Steiner for helpful discussion. Further, we thank the NIH and Pfeiffer Foundation, Kaufman Foundation, and Keck Foundation for financial support. Publisher Copyright: {\textcopyright} 2012 Elsevier Inc.",
year = "2012",
month = jan,
doi = "10.1016/B978-0-12-381272-8.00013-1",
language = "English (US)",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "205--228",
booktitle = "Methods in Enzymology",
}