z-logo
open-access-imgOpen Access
The Level of Circulating Octanoate Does Not Predict GhrelinO-Acyl Transferase (GOAT)-Mediated Acylation of Ghrelin During Fasting
Author(s) -
Ralf Nass,
Alexander Nikolayev,
Jianhua Liu,
Suzan S. Pezzoli,
Leon S. Farhy,
James T. Patrie,
Bruce D. Gaylinn,
Mark L. Heiman,
Michael O. Thorner
Publication year - 2014
Publication title -
the journal of clinical endocrinology and metabolism
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.206
H-Index - 353
eISSN - 1945-7197
pISSN - 0021-972X
DOI - 10.1210/jc.2014-1318
Subject(s) - ghrelin , acylation , medicine , endocrinology , chemistry , biochemistry , hormone , biology , catalysis
Acyl-ghrelin is a 28-amino acid peptide released from the stomach. Ghrelin O-acyl transferase (GOAT) attaches an 8-carbon medium-chain fatty acid (MCFA) (octanoate) to serine 3 of ghrelin. This acylation is necessary for the activity of ghrelin. Animal data suggest that MCFAs provide substrate for GOAT and an increase in nutritional octanoate increases acyl-ghrelin.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom