Molecular characterization of chicken growth hormone secretagogue receptor gene

Tanaka, Minoru; Miyazaki, Takashi; Yamamoto, Ichiro; Nakai, Norihiro; Ohta, Yoshiyuki; Tsushima, Nobumichi; Wakita, Masaaki; Shimada, Kiyoshi

doi:10.1016/s0016-6480(03)00247-8

Cited by 69 publications

(41 citation statements)

References 24 publications

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“…This gene organization and the insert position of the intron are identical to those of the mammalian GHS-R gene (McKee et al, 1997;Petersenn, 2002), indicating that the GHSR gene has been evolutionary conserved from fish to mammals. Seven TMD were predicted in grass carp GHS-R1a and this organization was identical to that reported for other GHS-R1 genes including those of human (Petersenn et al, 2001), chicken (Tanaka et al, 2003) and other fishes (Palyha et al, 2000;Chan and Cheng, 2004;Olsson et al, 2008;Kaiya et al, 2009a,b).…”

Section: Discussionsupporting

confidence: 76%

“…Amino acid sequences of GHS-R1a of seabream, pufferfish and chicken GHS-R1a have 56, 55 and 72% identity to human GHS-R1a, respectively (Palyha et al, 2000;Kaiya et al, 2008;Zhang et al, 2008). It has been reported that the GHS-R gene has two exons and one intron in chicken (Tanaka et al, 2003), seabream (Chan and Cheng, 2004) and pufferfish (Palyha et al, 2000). This gene organization and the insert position of the intron are identical to those of the mammalian GHS-R gene (McKee et al, 1997;Petersenn, 2002), indicating that the GHSR gene has been evolutionary conserved from fish to mammals.…”

Section: Discussionmentioning

confidence: 99%

“…Mammalian GHS-R gene is composed of two exons, and two types of GHS-R mRNAs, GHS-R1a and 1b, are generated by alternative transcription process of the gene (Howard et al, 1996). So far, GHS-Rs have been identified in mammals (Howard et al, 1996;Katayama et al, 2000;Kitazawa et al, 2011;Suzuki et al, 2012), avians (Geelissen et al, 2003;Tanaka et al, 2003) and several fish species (Palyha et al, 2000;Chan and Cheng, 2004;Olsson et al, 2008;Kaiya et al, 2009a,b;Small et al, 2009;Eom et al, 2014). In fish, GHS-R1a was first identified by Palyha et al (2000) in pufferfish Takifugu rubripes.…”

Section: Introductionmentioning

confidence: 99%

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Sequence, genomic organization and expression of ghrelin receptor in grass carp, Ctenopharyngodon idellus

Cai

Yuan

et al. 2015

Comparative Biochemistry and Physiology Part A: Molecular &

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Section: Discussionsupporting

confidence: 76%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Sequence, genomic organization and expression of ghrelin receptor in grass carp, Ctenopharyngodon idellus

Cai

Yuan

et al. 2015

Comparative Biochemistry and Physiology Part A: Molecular &

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“…In zebrafish, a novel GHSR paralogous sequence that has 74% homology with the former reported GHSR1a has also been discovered in the genomic database and is named zebrafish GHSR2a (Kaiya et al 2008). Moreover, another variant form of GHSR, designated GHSR1c or GHSR1aV, which lacks TM-6 when compared with GHSR1a due to a 48 bp deletion, has been detected in chicken and turkey (Geelissen et al 2003, Tanaka et al 2003, Richards et al 2006. Our study provides new evidence for the existence of GHSR1b in teleostean fishes.…”

Section: Discussionsupporting

confidence: 60%

Molecular cloning and mRNA expression analysis of two GH secretagogue receptor transcripts in orange-spotted grouper (Epinephelus coioides)

Chen

Tang²,

Yan³

et al. 2008

Journal of Endocrinology

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GH secretagogue receptor (GHSR) is the receptor of ghrelin, a circulating GH-releasing and appetite-inducing hormone. In this paper, two Ghsr cDNAs, gpGhsr1a and gpGhsr1b, were identified and characterized in a teleost, the orange-spotted grouper (Epinephelus coioides). The gpGHSR1a is 1512 bp in length with an open reading frame (ORF) that encodes a protein of 383 amino acids with seven transmembrane (TM) domains, while the 1703 bp gpGHSR1b contains an ORF encoding for 303 amino acids with five TM domains. Comparison between cDNA and gene sequences showed that the two transcripts are two alternative splicing forms of a single gpGhsr gene. Tissue distribution and ontogeny of two gpGhsr mRNAs were examined by RT-PCR. The gpGHSR1a is mainly expressed in brain and pituitary gland, when compared with a more widespread expression of gpGHSR1b. During embryonic and larval development, the gpGhsr1b mRNA appears before the gpGhsr1a mRNA. Furthermore, quantitative real-time PCR performed on brain showed that both transcripts have the highest expression level in the pituitary gland. The expression level of gpGHSR1a was generally higher than that of gpGHSR1b. GHSR expressing cells were also detected widely in grouper brain by in situ hybridization, with a broader distribution than previous reports in mammals. Finally, an in vitro study showed that expression of both gpGHSR transcripts in pituitary and hypothalamus is downregulated by GH and ghrelin but not by des-acyl ghrelin, and this suggests that feedback regulation of GHSR also exists in teleostean fishes.

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“…Wada et al (2003) observed ghrelin mRNA expression only in the proventriculus of newly hatched Leghorn chicks, whereas in adult chickens, mRNA expression was also detected in proventriculus and duodenum. This is similar to the tissue expression patterns reported previously for 8-week-old White Leghorn chickens (Tanaka et al, 2003) and 10 day-old broiler chicks (Geelissen et al, 2003).…”

Section: Ghrelin Mrna Expressionsupporting

confidence: 90%

Ghrelin Gene Expression in Broiler Proventriculus Tissue are Changed by Feed Restriction, Different Dietary Energy and Protein Levels

Ghazanfari¹,

Nassiry²,

Tahmoorespur³

et al. 2010

American J. of Animal and Veterinary Sciences

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Problem statement:The aim of this study was to investigate the effects of feed restriction and different energy and protein contents of diet on ghrelin gene expression in broiler chicken. Approach: Feeding programs consisted of ad libitum and feed restriction, two energy levels (3100 and 2800 kcal ME kg −1 ) and three protein levels (22.3, 19.3 and 16.3% CP). Feed restriction was applied during 22-32 days of age. Proventriculus samples were collected at 21, 32 and 49 days of age. Ghrelin mRNA expression in proventriculus tissue was quantitate using Real Time quantitative PCR. Results: We found that ghrelin gene expression was increased in restricted chicks compared with those fed ad libitum at 32 days of age (p = 0.09) but feed restriction had no effect on ghrelin gene expression at 49 days of age. A positive response in ghrelin gene expression was achieved by decreasing energy level in the diet at 21 days of age (p<0.07) and at 32 days of age (p<0.05). Also, we showed that dietary protein had no effect on ghrelin gene expression, whereas there was a tendency for an increase in ghrelin gene expression as protein decreased at total period. Conclusion: The present study, we investigated the effects of feed restriction and different energy and protein contents of the diet on ghrelin gene expression in broiler chicken. We have characterized chicken ghrelin cDNA in proventriculus tissue in broiler chicken. We also found that ghrelin gene expression is differently suppressed by diet manipulations. Additional studies are necessary to investigate the role of nutrition on ghrelin gene expression in proventriculus tissue in broiler chicken.

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Molecular characterization of chicken growth hormone secretagogue receptor gene

Cited by 69 publications

References 24 publications

Sequence, genomic organization and expression of ghrelin receptor in grass carp, Ctenopharyngodon idellus

Sequence, genomic organization and expression of ghrelin receptor in grass carp, Ctenopharyngodon idellus

Molecular cloning and mRNA expression analysis of two GH secretagogue receptor transcripts in orange-spotted grouper (Epinephelus coioides)

Ghrelin Gene Expression in Broiler Proventriculus Tissue are Changed by Feed Restriction, Different Dietary Energy and Protein Levels

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