An alternative splice site in ghrelin is missing in ruminants

Dickin, J. C.; Thue, T. D.; Buchanan, Fiona

doi:10.1111/j.1365-2052.2004.01175.x

Cited by 18 publications

(15 citation statements)

References 4 publications

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“…It has been predicted that all studied ruminant species have only the 27 amino acid form of the mature ghrelin peptide. The first splicing acceptor site within intron 2 has been lost as a result of a transition event (adenine to thymine) (DICKIN et al 2004), and the present study supports this finding. By BLAST searching the GenBank database, another cDNA (acc.…”

Section: Resultssupporting

confidence: 86%

Molecular characterization of the bovine <i>GHRL</i> gene (Short Communication)

2009

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Bovine ghrelin, a 27 amino acid peptide, has been identified in oxyntic glands of the abomasum. It is an endogenous ligand for growth hormone secretagogue receptor and stimulates food intake and growth hormone secretion. The bovine GHRL gene was completely sequenced and consists of five exons and four introns. Like mouse and human GHRL genes, we found that the bovine GHRL gene also contains a first non-coding exon of 21 bp. The bovine GHRL gene codes for 116 amino acid peptide named preproghrelin which contains the ghrelin peptide and another peptide similar to obestatin. Sequence analysis revealed eight polymorphisms, which are located in the non-coding sequence of the gene.

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Section: Resultssupporting

confidence: 86%

Molecular characterization of the bovine <i>GHRL</i> gene (Short Communication)

2009

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“…In contrast, truncated peptides of octanoylated ghrelin, such as EP-01037 (Gly-Ser-Ser(Ooctanoyl)-Phe-NH 2 ) and EP-00775 (Gly-Ser-Ser(Ooctanoyl)-Phe-Leu-Ser-Pro-Glu-NH 2 ) neither stimulate GH secretion in vivo nor replace radiolabeled ghrelin from binding sites (Torsello et al 2002). Moreover, bovine ghrelin is a 27 amino acid peptide and 8 amino acids of the C-terminal region (11-27) are heterologous to those of monogastric animals (Dickin et al 2004). Based on these facts, it is preferable to use a specific peptide to investigate the physiological effect of ghrelin on the mechanism of GH secretion in ruminants.…”

Section: Discussionmentioning

confidence: 99%

“…ghrelin and des-Gln 14 -ghrelin, have been purified and characterized from rat stomach and both peptides can bind to GHS-R1a (Hosada et al 2000b). Monogastric animals have both forms of peptide, while ruminants only possess des-Gln 14 -ghrelin because the first splicing acceptor site within intron 1 has been lost (Dickin et al 2004). Moreover, although the N-terminal region of ghrelin is homologous among species, 7 or 8 amino acids of the C-terminal region of ruminant ghrelin are different from those of monogastric animals (Dickin et al 2004).…”

Section: Introductionmentioning

confidence: 99%

Dose-dependent response of plasma ghrelin and growth hormone concentrations to bovine ghrelin in Holstein heifers

ThidarMyint¹,

Yoshida²,

Ito³

et al. 2006

Journal of Endocrinology

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The stimulatory effect of the novel gastric-derived hormone, ghrelin, on growth hormone (GH) secretion has been reported in domestic animals as well as in humans and rats. The octanoyl modification on the Ser3 residue of ghrelin appears to be essential for its endocrine activity. A major portion of circulatory ghrelin lacks acylation but possesses some biological activities other than GH stimulation; therefore, both types of acylated and des-acyl ghrelin are supposed to be important for energy homeostasis. The effects of pharmacological doses of rat and/or human ghrelin on GH secretion have been reported recently in ruminants; however, the physiological effect of exogenous bovine ghrelin on its own plasma level and on GH secretion is still unknown. Moreover, the RIA systems for the measurement of bovine active ghrelin and for bovine total ghrelin including acylated ghrelin, des-acyl ghrelin and all ghrelin peptides with an intact bovine C-terminal have not yet been validated. In this study, we established the RIA system for bovine ghrelin, and the dose-dependent effects of synthesized acylated bovine ghrelin(1-27) on plasma active and total ghrelin, GH, insulin and metabolites were measured in Holstein heifers. Six animals were intravenously injected with synthesized acylated bovine ghrelin (0, 0·1, 0·5, 1·0, 5·0, 10·0 µg/kg body weight (BW)) and plasma hormone concentrations were measured from serially collected samples. Bovine ghrelin RIA showed that the basal level of total ghrelin is approximately 16 times higher than that of active ghrelin in bovine plasma. Both forms of ghrelin were increased in a dose-dependent manner in response to bovine ghrelin injections, peak values were reached at 5 min after administration and returned to pre-injected values within 15 min. Plasma GH was responsive to all doses of bovine ghrelin in a dose-dependent manner, peaked as early as at 5-10 min after injection and returned to the basal value within 60 min. The GH area under curve 1 h after injection of the smallest dose of ghrelin used in this experiment (0·1 µg/kg BW) was significantly higher than that of the vehicle (0·1% BSA saline)-injected control group (P<0·05). The GH response to the highest dose of ghrelin (10·0 µg/kg BW) was greater than the response to 5·0 µg/kg BW ghrelin (P<0·001). Plasma glucose concentrations were not significantly altered by the administration of bovine ghrelin while plasma insulin levels were transiently stimulated by the higher doses of ghrelin (1·0, 5·0, 10·0 µg/kg BW). Plasma non-esterified fatty acid levels also increased following ghrelin administration. Our study indicates that a considerable quantity of both acylated and des-acyl ghrelin is circulating in the bloodstream, and also confirms that ghrelin is not only a potent stimulator of GH secretion but also plays a considerable role in energy homeostasis in Holstein heifers.

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“…Ghrelin is a 28 amino acid peptide in monogastric species and a 27 amino acid peptide in ruminants (Dickin et al 2004). It is primarily produced by oxyntic cells in the stomach or abomasum respectively with smaller amounts produced by the intestine and pancreas (Hayashida et al 2001, Hosoda et al 2006.…”

Section: Introductionmentioning

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

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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.

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An alternative splice site in ghrelin is missing in ruminants

Cited by 18 publications

References 4 publications

Molecular characterization of the bovine <i>GHRL</i> gene (Short Communication)

Molecular characterization of the bovine <i>GHRL</i> gene (Short Communication)

Dose-dependent response of plasma ghrelin and growth hormone concentrations to bovine ghrelin in Holstein heifers

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

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An alternative splice site in ghrelin is missing in ruminants

Cited by 18 publications

References 4 publications

Molecular characterization of the bovine &lt;i&gt;GHRL&lt;/i&gt; gene (Short Communication)

Molecular characterization of the bovine &lt;i&gt;GHRL&lt;/i&gt; gene (Short Communication)

Dose-dependent response of plasma ghrelin and growth hormone concentrations to bovine ghrelin in Holstein heifers

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

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Molecular characterization of the bovine <i>GHRL</i> gene (Short Communication)

Molecular characterization of the bovine <i>GHRL</i> gene (Short Communication)