| Project/Area Number |
08680911
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Laboratory animal science
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| Research Institution | KITASATO UNIVERSITY |
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Principal Investigator |
FURUDATE Sen-ichi Kitasato Univ.Sch.of Med., Asso ciate Prof., 医学部, 助教授 (80095512)
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| Co-Investigator(Kenkyū-buntansha) |
SAKAI Yasuhiro Kitasato Univ.Sch.of Med.Associate Prof., 医学部, 助教授 (00050625)
KOJIMA Hisako Kitasato Univ.Sch.of Associate Prof., 医学部, 助教授 (90118810)
ONO Masao Rikkyo Univ.Sch, of Science, Prof., 理学部, 教授 (40050645)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 1997: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1996: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | dwarfism / hypothyhoidism / rdw / thyroglobulin / endoplasmic reticulum / chaperone / stress protein / ERSD / 原発性甲状腺機能低下症 / hsp70 / Bip / エンドプラスミン / 分子シャペロン / 小胞体蓄積病(ERSD) / 遺伝性侏儒症 / 卵巣移植 / CNPase / サイクログロブリン |
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| Research Abstract |
The rdw rat was initially reported as an animal model for fereditary dwarfism, but the rat has been shown as primary hypothyroidism by much accumulated evidence. We examined the thyroid gland of the rdw rat morphologically and proteins of the gland related to the hereditary dwarfism and/or primary hypothyroidism. The thyroid gland of rdw seems very poor in the general development. The average size of the follicle was very small. The follicle lumen was not stained with hematoxylin and eosin. In electron microscope observation, a huge vacuole was seen in the infra-nuclear region and the nucleus was shifted to the lamina side in the follicular epithelial cells of rdw. Secretory granules could not be detected in follicular epithelial cells. The cytoplasm of follicular cells had markedly distended rough endoplasmic reticulum. Proteins having relations to hereditary dwarfism of the rdw rat were searched for in various tissues of the rat with an improved two-dimensional gel electrophoresis technique followed by immunoblotting and microsequencing. Only pituitary and thyroid glands among those tissues showed abnormalities in protein contents. GH and PRL contents in the rdw pituitary were much less than in the normal one, but the abnormalities in the rdw thyroid were far more serious than in the pituitary. At least 18 protein levels in the rdw thyroid were above, and 17 were below the normal. Those identified among the increased proteins were endoplasmin, immunoglobulin heavy chain binding protein (Bip), and heat shock protein 70 (hsp70), the contents of which respectively were a40 times, 10 times and more than 50 times as much in the rdw thyroid as in the normal tissue. Because Bip and endoplasmin are known to be ER resident proteins, and because all three belong to a chaperone protein family, accumulation of these proteins in the rdw, thyroid suggests that protein folding and secreting disorders underlie the hypothyroidism of the rdw rat.
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