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Abstract

Ghrelin is a novel growth-hormone-releasing acylated peptide, which has been purified and identified in rat stomach. In the present study, the full-length sequence of bovine ghrelin cDNA was cloned by RT-PCR. The bovine ghrelin cDNA sequence derived in the present study included a 348 bp open reading frame and a 137 bp 3'UTR. The putative amino acid sequence of bovine prepro-ghrelin consisted of 116 amino acids, which contained the 27-amino acid ghrelin. The sequence analysis of the bovine ghrelin gene revealed that an intron existed between Gln$^{13}$ and Arg$^{14}$ of ghrelin. This exon-intron boundary matched the GT-AG rule of the splicing mechanism. Compared with rats, which have two tandem CAG sequences in the 3'end of intron, bovine ghrelin genome has only one CAG sequence. Therefore, although rats can produce 28 amino acid-ghrelin and 27 amino acid-des-Gln$^{14}$-ghrelin by alternative splicing, ruminant species, including bovines, might be able to produce only one type of ghrelin peptide, des-Gln$^{14}$-ghrelin. The influence of aging on plasma ghrelin concentration was also examined. Plasma ghrelin concentration increased after birth to approximately 600 days of age, and then remained constant.

참고문헌 (13)

  1. Kojima, M., H. Hosoda and K. Kangawa. 2001. Purification and distribution of ghrelin: The natural endogenous ligand for the growth hormone secretagogue receptor. Horm. Res. 56 (Suppl. 1):93-97. 
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  3. Nakazato, M., N. Murakam, Y. Date, M. Kojima, H. Matsuo, K. Kangawa and S. Matsukura. 2001. A role for ghrelin in the central regulation of feeding. Nature 409:194-198. 
  4. Rigamonti, A. E., A. I. Pincelli, B. Corra, R. Viarengo, S. M. Bonomo, D. Galimberti, M. Scacchi, E. Scarpini, F Cavagnini and E. E. Muller. 2002. Plasma ghrelin concentrations in elderly subjects: comparison with anorexic and obese patients. J. Endocrinol. 175:R1-5. 
  5. Sugino, T., Y. Hasegawa, Y. Kikkawa, J. Yamaura, M. Yamagishi, Y. Kurose, M. Kojima, K. Kangawa and Y. Terashima. 2002a. A transient ghrelin surge occurs just before feeding in a scheduled meal-fed sheep. Biochem. Biophys. Res. Commun. 295:255-260. 
  6. Sugino, T., J. Yamaura, M. Yamagishi, A. Ogura, R. Hayashi, Y. Kurose, M. Kojima, K. Kangawa, Y. Hasegawa and Y. Terashima. 2002b. A transient surge of ghrelin secretion before feeding in modified by different feeding regimens in sheep.Biochem. Biophys. Res. Commun. 298:785-788. 
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  9. Sugino, T., J. Yamaura, M. Yamagishi, Y. Kurose, M. Kojima, K. Kangawa, Y. Hasegawa and Y. Terashima. 2003. Involvement of cholinergic neurons in the regulation of the ghrelin secretory response to feeding in sheep. Biochem. Biophys. Res. Commun. 304:308-312. 
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  12. Hashizume, T., M. Horiuchi, N. Tate, S. Kojima, H. Hosoda and K. Kangawa. 2003. Effects of ghrelin on growth hormone secretion from cultured adenohypophysical cells in cattle. Endocrine J. 50:289-295. 
  13. Sakata, I., T. Tanaka, M. Matsubara, M. Yamazaki, S. Tani, Y. Hayashi, K. Kangawa and T. Sakai. 2002. Postnatal changes in ghrelin mRNA expression and in ghrelin-producing cells in the rat stomach. J. Endocrinol. 174:463-471. 

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