Analysis of transcriptional control mechanism for the expression of type I collagen gene in fibrotic skin disorders
Project/Area Number |
10670779
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Dermatology
|
Research Institution | Chiba University |
Principal Investigator |
HATAMOCHI Atsushi Chiba University School of Medicine, Associate Professor, 医学部, 助教授 (90172923)
|
Co-Investigator(Kenkyū-buntansha) |
ENDO Hideharu Chiba University School of Medicine, Assistant, 医学部, 助手 (50282489)
SHINKAI Hiroshi Chiba University School of Medicine, Professor, 医学部, 教授 (90030957)
|
Project Period (FY) |
1998 – 2000
|
Project Status |
Completed (Fiscal Year 2000)
|
Budget Amount *help |
¥2,700,000 (Direct Cost: ¥2,700,000)
Fiscal Year 2000: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1999: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1998: ¥1,000,000 (Direct Cost: ¥1,000,000)
|
Keywords | type I collagen / transcription / fibrotic skin diseases / ColF1 / type III collagen / ColF1 / α_2(I)コラーゲン / Ehlers-Danlos症候群 / cutis laxa / acrogeria / Cutis laxa |
Research Abstract |
Type I collagen, a most abundant protein in the dermis, consists of two α1(I) chain and one α 2(I) chain which are coordinately expressed. ColF1, a DNA binding protein which specifically binds to a segment of the α2(I) collagen promoter at -400bp upstream of the start of transcription, activates transcription of the α2(I) collagen gene in vitro, and consists of two polypeptides. We investigated on the the cDNA cloning of this transcriptional factor of the α2(I) collagen gene. We found that 42kDa polypeptide were identical to Pur α, is a nuclear protein which has been reported to binds to a upstream region of human c-mye gene, and 40kDa polypeptide were identical to Pur β, has been partially sequenced and has regions of strong homology to Pur α. Full length of Pur β cDNA were sequenced. We had looked for fibroblasts express abnormal levels of collagen as model systems of transcriptional control mechanisms of type I collagen gene in vivo. We found two strains of Ehlers-Danlos syndrome fibroblasts which produced extremely low levels of type III collagen.
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Report
(4 results)
Research Products
(13 results)