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Regular Article |
a Laboratory of Animal Physiology,
b School of Agricultural Sciences, Nagoya University, Chikusa, Nagoya, Japan 464-860
c Center for Molecular Biology and Genetics, Mie University, Tsu, Mie, Japan 514-850
d Laboratory of Animal Genetics, School of Agricultural Sciences, Nagoya University, Chikusa, Nagoya, Japan 464-860
e Department of Animal Science, McGill University, Ste Anne de Bellevue, Quebec, Canada H9X 3V
ABSTRACT
Chicken vasoactive intestinal polypeptide receptor (VIPR) cDNA was cloned by the reverse transcription-polymerase chain reaction method using primers designed on the basis of other species of VIPR cDNA. The cDNA obtained was sequenced by the dideoxy-mediated chain-termination method. Of the 2227 nucleotides that were sequenced, 84, 855, and 1338 bases represent the 5'-untranslated region (UTR), the 3'-UTR, and the open reading frame that predicts a peptide of 446 amino acids. The cDNA of the chicken VIPR shows 65% and 60% homologies to human cDNA of VIP1 and VIP2 receptors, respectively. The clone had the expected similarity to highly conserved features of the other G protein-coupled receptors (GPCRs) such as six cysteine residues that are functionally important in the VIPR subfamily. In addition, the seven potential membrane-spanning domains characteristic of the family B group III GPCR superfamily and highly conserved motif within the third cellular loop between transmembrane regions 5 and 6. Northern blot hybridization analysis in this study indicated mRNA expression of VIPRs in the various tissues of the chicken. Strong signal was detected in the brain and anterior pituitary gland. High levels of VIPR mRNA in the brain was consistent with VIP-binding experiments and with the function of VIP in the brain as a neuroendocrine factor or neurotransmitter. Expression of VIPR was detected in the anterior pituitary gland of chick embryos. The expression of VIPR mRNA in the chick anterior pituitary gland may indicate a regulatory function of VIP on prolactin (PRL) production or PRL cell proliferation during embryogenesis. Chicken VIPR shows high homology with mammalian type I VIPR but, in some part, possesses similarity of amino acid sequence. Expression of VIPR in various tissues supports diverse functions for VIP in the chicken.
1 This research was supported by grants from the Monbusho International Scientific Research Program (Joint Research; 07044190) to K.S. and by a JSPS Research Fellowship for Young Scientists awarded to N.K. (80003425). The nucleotide sequence report in this paper has been submitted to GenBank/EMBL/DDBJ Bank with the accession number AB029895.
2 Correspondence. FAX: 81 52 789 4065; g44500a{at}nucc.cc.nagoya-u.ac.jp
3 Current address: Chromosome Research Unit, Faculty of Science, Hokkaido University, Kita 10, Nishi 8, Kita-ku, Sapporo, Japan 060-0810.
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