Characterization of the binding of MSH-B, HP-228, GHRP-6 and 153N-6 to the human melanocortin receptor subtypes
References (36)
- et al.
Molecular cloning and expression of the human melanocyte stimulating hormone receptor cDNA
FEBS Lett
(1992) - et al.
Molecular cloning of a novel human melanocortin receptor
Biochem Biophys Res Commun
(1993) - et al.
Molecular cloning of a novel melanocortin receptor
J Biol Chem
(1993) - et al.
Molecular cloning, expression, and gene localization of a fourth melanocortin receptor
J Biol Chem
(1993) - et al.
Characterisation of melanocortin receptor subtypes by radioligand binding analysis
Eur J Pharmacol
(1995) - et al.
Major pharmacological distinction of the ACTH receptor from the other melanocortic receptors
Life Sci
(1996) - et al.
Targeted disruption of the melanocortin-4 receptor results in obesity in mice
Cell
(1997) - et al.
Identification of antagonists for melanocortin MC3, MC4 and MC5 receptors
Eur J Pharmacol
(1994) - et al.
Discovery and structure-function analysis of α-melanocyte stimulating hormone antagonists
J Biol Chem
(1994) - et al.
A modification of a protein-binding method for rapid quantification of cAMP in cell-culture supernatants and body fluid
Anal Chem
(1990)
Binding of cyclic and linear MSH core peptides to the melanocortin receptor subtypes
Eur J Pharmacol
Characterization of a putative α-MSH antagonist 153N-6 at melanocortin receptor subtypes by radioligand binding
Peptides
Synthesis and biological evaluation of α-MSH analogues substituted with alanine
Peptides
The melanocortin (MC3) receptor from rat hypothalamus: photoaffinity labelling and binding of alanine-substituted α-MSH analogues
FEBS Lett
Molecular cloning, expression, and characterization of fifth melanocortin receptor
Biochem Biophys Res Commun
Molecular cloning and characterization of the fifth melanocortin receptor
Biochem Biophys Res Commun
Molecular cloning of a bovine MSH receptor which is highly expressed in the testis
FEBS Lett
The melanotropins
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Ghrelin receptor antagonism and satiety attenuate Pavlovian-instrumental transfer
2024, Neurobiology of Learning and MemoryLiver-expressed antimicrobial peptide 2 functions independently of growth hormone secretagogue receptor in calorie-restricted mice
2022, PeptidesCitation Excerpt :These findings strongly suggest that inhibition of feeding by [D-Lys3]-GHRP-6 is mediated not only by blocking GHSR activity but also by binding with other receptors. Previous studies showed that [D-Lys3]-GHRP-6 also binds with chemokines and melanocortin receptors [27,28]. A more recent experiment showed that both male and female Leap2-KO mice exhibited normal physiological changes including feeding, body weight, and hepatic fat accumulation when maintained on regular chow-diet, but only female Leap2-KO mice were hyperphagic, gained more body weight and hepatic fat accumulation compared to their littermate when maintained on a long-term high-fat diet [29].
Hypothalamic regulation of body growth and appetite by ghrelin-derived peptides during balanced nutrition or undernutrition
2016, Molecular and Cellular EndocrinologyCitation Excerpt :In contrast, [D-Lys3]-GHRP6 has no action on spontaneous ultradian GH secretion (Okimura et al., 2003). Results are biased by the fact that [D-Lys3]-GHRP6 also binds to all melanocortin receptors (Schioth et al., 1997) and [D-Arg-1, D-Phe-5, D-Trp-7,9,Leu-11]-substance P also antagonizes many peptide receptors (Woll and Rozengurt, 1988) and has full inverse agonist action in vitro and in vivo (Holst et al., 2003; Petersen et al., 2009b). Another recently developed molecule, JMV2810, antagonized the effects of hexarelin (a synthetic ghrelin agonist) on food intake but not on GH secretion after acute injection but its effects on spontaneous GH secretion or food intake have not been reported (Demange et al., 2007).
Physiological roles of preproghrelin-derived peptides in GH secretion and feeding
2011, PeptidesCitation Excerpt :Repeated injections of [d-Lys3]-GHRP6, however, did not modify ultradian GH secretion [53]. However, results with both of these compounds are difficult to interpret because the first one also binds to four of the melanocortin receptors [65] and the second one antagonizes many peptide receptors [87] and has been shown to display a full inverse agonist activity both in vitro [30] and in vivo [61]. Another recently developed molecule, JMV2810, antagonized the effects of hexarelin (a synthetic ghrelin agonist) on food intake but not on GH secretion after acute injection [15] but its effects per se on spontaneous GH secretion or food intake were not investigated.
Co-operative regulation of ligand binding to melanocortin receptor subtypes: Evidence for interacting binding sites
2005, European Journal of PharmacologyGhrelin stimulates motility in the small intestine of rats through intrinsic cholinergic neurons
2004, Regulatory Peptides