Abstract
Ghrelin is a gastric hormone that acts on pituitary and hypothalamus to stimulate growth hormone release regulating adiposity and appetite. Its activity is thought to be dependent on acylation. Ghrelin is O-octanoylated at Ser3 (acylated ghrelin [AG]) by ghrelin O-acyltransferase (GOAT), a posttranslational modification required for mediating its action through growth hormone secretagogue receptor 1a (GHS-R1a). However, as only 5–20% of circulating ghrelin is acylated, unacylated ghrelin (UnAG, also called des-acyl ghrelin) remains the major circulating form (1). UnAG has long been considered as a degradation product of ghrelin. Hence, UnAG has not received much attention regarding its biological significance and possible therapeutic effects. In recent years however, there has been increasing interest in deciphering the biological actions of UnAG in an attempt to use it as a therapeutic tool (2). A few years ago in a very well-performed study, Delhanty et al. (2) showed rapid effects of UnAG on genome-wide expression patterns in the adipose tissues, muscles, and livers of GHSR1a knockout mice. These studies established the notion that UnAG has GHS-R1a–independent …
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