| Project/Area Number |
60480249
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Dermatology
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| Research Institution | Meiidical College of Oita |
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Principal Investigator |
SHINKAI Hiroshi Medical College of Oita Dept. Dermatology, 医学部, 助教授 (90030957)
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| Co-Investigator(Kenkyū-buntansha) |
HONDA Tomohito Medical College of Oita Dept. Dermatology, 医学部, 助手 (80173665)
FUJIWARA Sakuhei Medical College of Oita Dept. Dermatology, 医学部, 助手 (90181411)
MATSUNAGA Etsuji Medical College of Oita Dept. Dermatology, 医学部, 講師 (00145400)
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| Project Period (FY) |
1985 – 1987
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| Project Status |
Completed (Fiscal Year 1987)
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| Budget Amount *help |
¥5,500,000 (Direct Cost: ¥5,500,000)
Fiscal Year 1987: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1986: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 1985: ¥3,500,000 (Direct Cost: ¥3,500,000)
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| Keywords | Collagen / Hereditary connective tissue disease / reverse-phase HPLC Proteoglycan / プロテオグリカン / デルマタン硫酸 / デルマタン硫酸プロテオグリカン / コンドロイチン硫酸プロテオグリカン / エーラス・ダンロス症候群 |
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| Research Abstract |
Molecular defects of collagen or proteoglycans including the replacement of amino acid in poly-peptide chains, were found in hereditary connective tissue diseases. Northern and southern blot analyses using cDNA of collagen <alpha>1(I)- and <alpha>2(I)-chain, showed depression of <alpha>2(I) gene expression from a variant form of Ehlers -Danlos syndrome. The study of collagen structure, in health and disease, frequently requires fractionation and peptide analysis of the collagen chains. In order to micro-analysis of the heterogenity of newly synthesized collagen from hereditary connective tissue diseases, revers-phase HPLC system was more useful for the rapid separation and the recovery of polypeptide chains than the ordinary CM cellulose chromatography. Two dimensinal electrophoresis uwing iso-electrophocasing as first dimension and DDS- polyacrylamide gel electrophoeresis as second from CNBr peptides of <alpha>-chains which were separated by reverse-phase HPLC, could be detected the molecular heterogenity of collagen. Dermatan sulfate proteoglycans which associate collagen fibril, were found several forms in interstitial connective tissues. The defect of dermatan sulfate proteoglycans were occured in a case of Ehlers- Danlos syndrome. In order to more clarify the cause of the proteoglycan deficiency, we attempt to cDNA cloning from guinea pig skin fibroblast culture.
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