Is desacyl ghrelin a modulator of food intake?

Inhoff, Tobias; Wiedenmann, Bertram; Klapp, Burghard F.; Mönnikes, Hubert; Kobelt, Peter

doi:10.1016/j.peptides.2009.01.019

Cited by 48 publications

(39 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…To the best of our knowledge, there are no data on the effect of desacyl ghrelin on feed intake in ruminants. However, in rats, it has been suggested to be involved in the regulation of energy homeostasis because of its ability to cross the blood-brain barrier and to induce increased neuronal activity in the hypothalamic arcuate nucleus (Inhoff et al 2009). …”

Section: Figurementioning

confidence: 99%

Plasma ghrelin is positively associated with body fat, liver fat and milk fat content but not with feed intake of dairy cows after parturition

Börner¹,

Derno²,

Hacke³

et al. 2012

Journal of Endocrinology

View full text Add to dashboard Cite

Ghrelin is a gastrointestinal peptide hormone that is present in blood mostly in a non-posttranslationally modified form, with a minor proportion acylated at Ser 3 . Both ghrelin forms were initially assigned a role in the control of food intake but there is accumulating evidence for their involvement in fat allocation and utilization. We investigated changes in the ghrelin system in dairy cows, exhibiting differences in body fat mobilization and fatty liver, from late pregnancy to early lactation. Sixteen dairy cows underwent liver biopsy and were retrospectively grouped based on high (H) or low (L) liver fat content post-partum. Both groups had a comparable feed intake in week K6 (before parturition) and week 2 (after parturition). Only before parturition was preprandial total ghrelin concentration higher in L than in H cows and only after parturition was the basal plasma concentration of non-esterified fatty acids higher in H than in L cows. Both before and after parturition, H cows had higher preprandial plasma concentrations of acyl ghrelin, a higher acyl:total ghrelin ratio, lower plasma triacylglyceride concentrations and a lower respiratory quotient compared with L cows. These group differences could not be attributed to an allelic variant of the acyl ghrelin receptor. Rather, the ratio of acyl:total ghrelin correlated with several aspects of fat metabolism and with respiratory quotient but not with feed intake. These results show that endogenous ghrelin forms are associated with fat allocation, fatty liver, and utilization of fat during the periparturient period.

show abstract

Section: Figurementioning

confidence: 99%

Plasma ghrelin is positively associated with body fat, liver fat and milk fat content but not with feed intake of dairy cows after parturition

Börner¹,

Derno²,

Hacke³

et al. 2012

Journal of Endocrinology

View full text Add to dashboard Cite

show abstract

“…Interestingly, AG and UAG recognize common binding sites, and exert functions in cells and tissues that do not express the GHS-R1a, implying the existence of an as yet unidentified receptor for the ghrelin isoforms ( Fig. 1; Soares & Leite-Moreira 2008, Inhoff et al 2009, van der Lely 2009). …”

Section: Introductionmentioning

confidence: 99%

Unraveling the role of the ghrelin gene peptides in the endocrine pancreas

Granata

Baragli²,

Settanni³

et al. 2010

Journal of Molecular Endocrinology

View full text Add to dashboard Cite

The ghrelin gene peptides include acylated ghrelin (AG), unacylated ghrelin (UAG), and obestatin (Ob). AG, mainly produced by the stomach, exerts its central and peripheral effects through the GH secretagogue receptor type 1a (GHS-R1a). UAG, although devoid of GHS-R1a-binding affinity, is an active peptide, sharing with AG many effects through an unknown receptor. Ob was discovered as the G-protein-coupled receptor 39 (GPR39) ligand; however, its physiological actions remain unclear. The endocrine pancreas is necessary for glucose homeostasis maintenance. AG, UAG, and Ob are expressed in both human and rodent pancreatic islets from fetal to adult life, and the pancreas is the major source of ghrelin in the perinatal period. GHS-R1a and GPR39 expression has been shown in b-cells and islets, as well as specific binding sites for AG, UAG, and Ob. Ghrelin colocalizes with glucagon in a-islet cells, but is also uniquely expressed in 3-islet cells, suggesting a role in islet function and development. Indeed, AG, UAG, and Ob regulate insulin secretion in b-cells and isolated islets, promote b-cell proliferation and survival, inhibit b-cell and human islet cell apoptosis, and modulate the expression of genes that are essential in pancreatic islet cell biology. They even induce b-cell regeneration and prevent diabetes in streptozotocin-treated neonatal rats. The receptor(s) mediating their effects are not fully characterized, and a signaling crosstalk has been suggested. The present review summarizes the newest findings on AG, UAG, and Ob expression in pancreatic islets and the role of these peptides on b-cell development, survival, and function.

show abstract

“…Unacylated ghrelin is also present in circulating blood and the stomach, and the quantity is much greater than that of ghrelin (Kojima et al 1999, Hosoda et al 2000. Unacylated ghrelin exerts some biological actions, e.g., regulate feeding (Asakawa et al 2005, Toshinai et al 2006, Inhoff et al 2009) and gut motility (Fujimiya et al 2012), a GHS-R1a-independent antagonistic effect on ghrelin-induced insulin secretion and glucose metabolism, a trophic and protective effect on b-cells, as well as a role in muscle regeneration and in decreasing fat mass (Delhanty et al 2012, Delhanty & van der Lely 2013. How does unacylated ghrelin act?…”

mentioning

confidence: 99%

MOLECULAR EVOLUTION OF GPCRS: Ghrelin/ghrelin receptors

Kaiya

Kangawa

Miyazato

2013

Journal of Molecular Endocrinology

View full text Add to dashboard Cite

After the discovery in 1996 of the GH secretagogue-receptor type-1a (GHS-R1a) as an orphan G-protein coupled receptor, many research groups attempted to identify the endogenous ligand. Finally, Kojima and colleagues successfully isolated the peptide ligand from rat stomach extracts, determined its structure, and named it ghrelin. The GHS-R1a is now accepted to be the ghrelin receptor. The existence of the ghrelin system has been demonstrated in many animal classes through biochemical and molecular biological strategies as well as through genome projects. Our work, focused on identifying the ghrelin receptor and its ligand ghrelin in laboratory animals, particularly nonmammalian vertebrates, has provided new insights into the molecular evolution of the ghrelin receptor. In mammals, it is assumed that the ghrelin receptor evolution is in line with the plate tectonics theory. In contrast, the evolution of the ghrelin receptor in nonmammalian vertebrates differs from that of mammals: multiplicity of the ghrelin receptor isoforms is observed in nonmammalian vertebrates only. This multiplicity is due to genome duplication and polyploidization events that particularly occurred in Teleostei. Furthermore, it is likely that the evolution of the ghrelin receptor is distinct from that of its ligand, ghrelin, because only one ghrelin isoform has been detected in all species examined so far. In this review, we summarize current knowledge related to the molecular evolution of the ghrelin receptor in mammalian and nonmammalian vertebrates.

show abstract

Is desacyl ghrelin a modulator of food intake?

Cited by 48 publications

References 45 publications

Plasma ghrelin is positively associated with body fat, liver fat and milk fat content but not with feed intake of dairy cows after parturition

Plasma ghrelin is positively associated with body fat, liver fat and milk fat content but not with feed intake of dairy cows after parturition

Unraveling the role of the ghrelin gene peptides in the endocrine pancreas

MOLECULAR EVOLUTION OF GPCRS: Ghrelin/ghrelin receptors

Contact Info

Product

Resources

About