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Zoolog Sci. 2016 Oct;33(5):497-504.

Molecular Cloning of Ghrelin and Characteristics of Ghrelin-Producing Cells in the Gastrointestinal Tract of the Common Marmoset (Callithrix jacchus).

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1 Area of Regulatory Biology, Division of Life Science, Graduate School of Science and Engineering,Saitama University, 255 Shimo-okubo, Sakura-ku, Saitama 338-8570, Japan.
2 Area of Life-NanoBio, Division of Strategy Research, Graduate School of Science and Engineering,Saitama University, 255 Shimo-okubo, Sakura-ku, Saitama 338-8570, Japan.
3 Drug Safety Research Laboratories, Shin Nippon Biomedical Laboratories, Ltd. (SNBL DSR),2438 Miyanoura, Kagoshima 891-1394, Japan.
4 Graduate School of Medical and Dental Sciences, Kagoshima University,Kagoshima 890-8544, Japan.


Ghrelin was first isolated from human and rat as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R). In the present study, we determined the ghrelin cDNA sequence of the common marmoset (Callithrix jacchus), a small-bodied New World monkey, and investigated the distribution of ghrelin-producing cells in the gastrointestinal tract and localization profiles with somatostatin-producing cells. The marmoset ghrelin cDNA coding region was 354 base pairs, and showed high homology to that in human, rhesus monkey, and mouse. Marmoset ghrelin consists of 28 amino acids, and the N-terminal region is highly conserved as found in other mammalian species. Marmoset preproghrelin and mature ghrelin have 86.3% and 92.9% homology, respectively, to their human counterparts. Quantitative RT-PCR analysis showed that marmoset ghrelin mRNA is highly expressed in the stomach, but it is not detected in other tissues of the gastrointestinal tract. In addition, a large number of ghrelin mRNA-expressing cells and ghrelin-immunopositive cells were detected in the mucosal layer of the stomach, but not in the myenteric plexus. Moreover, all the ghrelin cells examined in the stomach were observed to be closed-type. Double staining showed that somatostatin-immunopositive cells were not co-localized with ghrelin-producing cells; however, a subset of somatostatin-immunopositive cells is directly adjacent to ghrelin-immunopositive cells. These findings suggest that the distribution of ghrelin cells in marmoset differs from that in rodents, and thus the marmoset may be a more useful model for the translational study of ghrelin in primates. In conclusion, we have clarified the expression and cell distribution of ghrelin in marmoset, which may represent a useful model in translational study.


ghrelin; immunohistochemistry; in situ hybridization; somatostatin; stomach

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