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Ghrelin regulation of glucose metabolism.

Peptides 100, 236-242 (2018)
Postprint DOI PMC
Open Access Green
The a 28-amino acid peptide ghrelin was discovered in 1999 as a growth hormone (GH) releasing peptide. Soon after its discovery, ghrelin was found to increase body weight and adiposity by acting on the hypothalamic melanocortinergic system. Subsequently, ghrelin was found to exert a series of metabolic effects, overall testifying ghrelin a pleiotropic nature of broad pharmacological interest. Ghrelin acts through the growth hormone secretagogue-receptor (GHS-R), a seven transmembrane G protein-coupled receptor with high expression in the anterior pituitary, pancreatic islets, thyroid gland, heart and various regions of the brain. Among ghrelins numerous metabolic effects are the most prominent the stimulation of appetite via activation of orexigenic hypothalamic neurocircuits and the food-intake independent stimulation of lipogenesis, which both together lead to an increase in body weight and adiposity. Ghrelin effects beyond the regulation of appetite and GH secretion include the regulation of gut motility, sleep-wake rhythm, taste sensation, reward seeking behaviour, and the regulation of glucose metabolism. The latter received recently increasing recognition because pharmacological inhibition of ghrelin signaling might be of therapeutic value to improve insuin resistance and type 2 diabetes. In this review we highlight the multifaceted nature of ghrelin and summarize its glucoregulatory action and discuss the pharmacological value of ghrelin pathway inhibition for the treatment of glucose intolerance and type 2 diabetes.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Ghrelin ; Glucose Metabolism ; Insulin Sensitivity ; Diabetes ; Diet-induced Obesity; Des-acyl Ghrelin; Hormone Secretagogue Receptor; Pancreatic Beta-cells; Brown Adipose-tissue; International Diabetes Organizations; Stimulated Insulin-secretion; Polycystic-ovary-syndrome; O-acyltransferase Goat; Prader-willi-syndrome; Treated Newborn Rats
ISSN (print) / ISBN 0196-9781
e-ISSN 1873-5169
Zeitschrift Peptides
Quellenangaben Band: 100, Heft: , Seiten: 236-242 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort New York, NY
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed