Source:http://linkedlifedata.com/resource/pubmed/id/19361568
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2009-5-25
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pubmed:abstractText |
Ghrelin, a GH-releasing and appetite-regulating peptide that is released from the stomach is an endogenous ligand for growth hormone secretagogue-receptor (GHS-R). Two types of GHS-R are accepted to be present, a functional GHS-R1a and GHS-R1b with unknown function. In this study, we identified cDNA that encodes protein with close sequence similarity to GHS-R and exon-intron organization of the GHS-R genes in rainbow trout, Oncorhynchus mykiss. Two variants of GHS-R1a proteins with 387-amino acids, namely DQTA/LN-type and ERAT/IS-type, were identified. In 3'-RACE PCR and genomic PCR, we also identified three GHS-R1b orthologs that are consisted of 297- or 300-amino acids with different amino acid sequence at the C-terminus, in addition to the DQTA/LN-type and ERAT/IS-type variations. Genomic PCR revealed that the genes are composed of two exons separated by an intron, and that two GHS-R1a and three GHS-R1b variants are generated by three distinct genes. GHS-R1a and GHSR-1b mRNA were predominantly expressed in the pituitary, followed by the brain. Identified DQTA/LN-type or ERAT/IS-type GHS-R1a cDNA was transfected into mammalian cells, and intracellular calcium ion mobilization assay was carried out. However, we did not find any response to rat ghrelin and a homologous ligand, des-VRQ trout ghrelin, of either receptor in vitro. We found that unexpected mRNA splicing had occurred in the transfected cells, suggesting that the full-length, functional receptor protein might not be generated in the cells. Gene structure and characterization of protein sequence identified in this study were closely similar to other GHS-R, but to conclude that it is a GHS-R for rainbow trout, further study is required to confirm activation of GHS-R1a by ghrelin or GHS. Thus we designated the identified receptor proteins in this study as GHS-R-like receptor (GHSR-LR).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1531-4332
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
153
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
438-50
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pubmed:meshHeading |
pubmed-meshheading:19361568-Amino Acid Sequence,
pubmed-meshheading:19361568-Animals,
pubmed-meshheading:19361568-Base Sequence,
pubmed-meshheading:19361568-Cloning, Molecular,
pubmed-meshheading:19361568-DNA, Complementary,
pubmed-meshheading:19361568-DNA Primers,
pubmed-meshheading:19361568-Exons,
pubmed-meshheading:19361568-Genome,
pubmed-meshheading:19361568-Introns,
pubmed-meshheading:19361568-Oncorhynchus mykiss,
pubmed-meshheading:19361568-Phylogeny,
pubmed-meshheading:19361568-Polymerase Chain Reaction,
pubmed-meshheading:19361568-RNA, Messenger,
pubmed-meshheading:19361568-Receptors, Ghrelin,
pubmed-meshheading:19361568-Sequence Homology, Amino Acid
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pubmed:year |
2009
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pubmed:articleTitle |
Ghrelin receptor (GHS-R)-like receptor and its genomic organisation in rainbow trout, Oncorhynchus mykiss.
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pubmed:affiliation |
Department of Biochemistry, National Cardiovascular Center Research Institute, 5-7-1 Fujishirodai, Suita, Osaka 565-8565, Japan. kaiya@ri.ncvc.go.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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