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Ghrelin and des-acyl ghrelin both inhibit isoproterenol-induced lipolysis in rat adipocytes via a non-type 1a growth hormone secretagogue receptor.
Eur J Pharmacol. 2004 Sep 13; 498(1-3):27-35.EJ

Abstract

Besides possessing a strong growth hormone (GH)-releasing activity, the gastrointestinal octanoylated peptide ghrelin has been reported to antagonize lipolysis in rat adipocytes. It is not yet clear whether this inhibitory activity on lipolysis is also shared by the major circulating isoform, des-acyl ghrelin, that does not activate the ghrelin receptor, namely the type 1a GH secretagogue-receptor (GHS-R1a) and lacks the endocrine effects of the acylated form. Here we show that des-acyl ghrelin, like ghrelin and some synthetic GHS (hexarelin and MK0677) and carboxy-terminally ghrelin fragments such as ghrelin-(1-5) and ghrelin-(1-10), all significantly reduced, over concentrations ranging from 1 to 1000 nM, the stimulation of glycerol release caused in rat epididymal adipocytes by the nonselective beta-adrenoceptor agonist isoproterenol in vitro. The order of potency on stimulated-lipolysis was: des-acyl ghrelin=ghrelin>MK0677=hexarelin>ghrelin-(1-5)=ghrelin-(1-10). This ranking was consistent with the binding experiments performed on membranes of epididymal adipose tissue or isolated adipocytes that did not express mRNA for GHS-R1a. A common high-affinity binding site was recognized in these cells by both acylated and des-acylated ghrelin and also by hexarelin, MK0677, ghrelin-(1-5) and ghrelin-(1-10). In conclusion, these findings provide the first evidence that des-acyl ghrelin, as well as ghrelin, short ghrelin fragments and synthetic GHS, may act directly as antilipolytic factors on the adipose tissue through binding to a specific receptor which is distinct from GHS-R1a.

Authors+Show Affiliations

Division of Pharmacology, Department of Anatomy, Pharmacology and Forensic Medicine, Via Pietro Giuria 13, I-10125, Turin, Italy. giampiero.muccioli@unito.itNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15363972

Citation

Muccioli, Giampiero, et al. "Ghrelin and Des-acyl Ghrelin Both Inhibit Isoproterenol-induced Lipolysis in Rat Adipocytes Via a Non-type 1a Growth Hormone Secretagogue Receptor." European Journal of Pharmacology, vol. 498, no. 1-3, 2004, pp. 27-35.
Muccioli G, Pons N, Ghè C, et al. Ghrelin and des-acyl ghrelin both inhibit isoproterenol-induced lipolysis in rat adipocytes via a non-type 1a growth hormone secretagogue receptor. Eur J Pharmacol. 2004;498(1-3):27-35.
Muccioli, G., Pons, N., Ghè, C., Catapano, F., Granata, R., & Ghigo, E. (2004). Ghrelin and des-acyl ghrelin both inhibit isoproterenol-induced lipolysis in rat adipocytes via a non-type 1a growth hormone secretagogue receptor. European Journal of Pharmacology, 498(1-3), 27-35.
Muccioli G, et al. Ghrelin and Des-acyl Ghrelin Both Inhibit Isoproterenol-induced Lipolysis in Rat Adipocytes Via a Non-type 1a Growth Hormone Secretagogue Receptor. Eur J Pharmacol. 2004 Sep 13;498(1-3):27-35. PubMed PMID: 15363972.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Ghrelin and des-acyl ghrelin both inhibit isoproterenol-induced lipolysis in rat adipocytes via a non-type 1a growth hormone secretagogue receptor. AU - Muccioli,Giampiero, AU - Pons,Nicoletta, AU - Ghè,Corrado, AU - Catapano,Filomena, AU - Granata,Riccarda, AU - Ghigo,Ezio, PY - 2004/02/05/received PY - 2004/07/02/revised PY - 2004/07/08/accepted PY - 2004/9/15/pubmed PY - 2005/3/1/medline PY - 2004/9/15/entrez SP - 27 EP - 35 JF - European journal of pharmacology JO - Eur J Pharmacol VL - 498 IS - 1-3 N2 - Besides possessing a strong growth hormone (GH)-releasing activity, the gastrointestinal octanoylated peptide ghrelin has been reported to antagonize lipolysis in rat adipocytes. It is not yet clear whether this inhibitory activity on lipolysis is also shared by the major circulating isoform, des-acyl ghrelin, that does not activate the ghrelin receptor, namely the type 1a GH secretagogue-receptor (GHS-R1a) and lacks the endocrine effects of the acylated form. Here we show that des-acyl ghrelin, like ghrelin and some synthetic GHS (hexarelin and MK0677) and carboxy-terminally ghrelin fragments such as ghrelin-(1-5) and ghrelin-(1-10), all significantly reduced, over concentrations ranging from 1 to 1000 nM, the stimulation of glycerol release caused in rat epididymal adipocytes by the nonselective beta-adrenoceptor agonist isoproterenol in vitro. The order of potency on stimulated-lipolysis was: des-acyl ghrelin=ghrelin>MK0677=hexarelin>ghrelin-(1-5)=ghrelin-(1-10). This ranking was consistent with the binding experiments performed on membranes of epididymal adipose tissue or isolated adipocytes that did not express mRNA for GHS-R1a. A common high-affinity binding site was recognized in these cells by both acylated and des-acylated ghrelin and also by hexarelin, MK0677, ghrelin-(1-5) and ghrelin-(1-10). In conclusion, these findings provide the first evidence that des-acyl ghrelin, as well as ghrelin, short ghrelin fragments and synthetic GHS, may act directly as antilipolytic factors on the adipose tissue through binding to a specific receptor which is distinct from GHS-R1a. SN - 0014-2999 UR - https://www.unboundmedicine.com/medline/citation/15363972/Ghrelin_and_des_acyl_ghrelin_both_inhibit_isoproterenol_induced_lipolysis_in_rat_adipocytes_via_a_non_type_1a_growth_hormone_secretagogue_receptor_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0014-2999(04)00799-X DB - PRIME DP - Unbound Medicine ER -