Tanaka Minoru, Miyazaki Takashi, Yamamoto Ichiro, Nakai Naoya, Ohta Yoshiyuki, Tsushima Nobumichi, Wakita Masaaki, Shimada Kiyoshi
Department of Animal Science, Faculty of Applied Life Science, Nippon Veterinary and Animal Science University, Musashino, Tokyo 180-8602, Japan.
Gen Comp Endocrinol. 2003 Nov;134(2):198-202. doi: 10.1016/s0016-6480(03)00247-8.
Synthetic growth hormone secretagogues stimulate growth hormone secretion by binding to a specific receptor, growth hormone secretagogue receptor (GHS-R). In this study, we investigated the cDNA and the genomic structure of chicken GHS-R. Chicken GHS-R gene is composed of two exons separated by an intron. Two GHS-R mRNA species, cGHS-R1a and cGHS-R1a-variant (cGHS-R1aV) are generated by alternative splicing of a primary transcript. cGHS-R1a protein is predicted to have seven transmembrane domains by a high degree of amino acid sequence identity with mammalian and teleost homologs. cGHS-R1aV lacks the transmembrane-6 domain due to a 48 bp deletion. RT-PCR analysis showed widespread tissue distributions of cGHS-R1a and cGHS-R1aV mRNAs with much higher amounts of cGHS-R1a in all the tissues.
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