Analysis of transcriptional control mechanism for the expression of type I collagen gene in fibrotic skin disorders

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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.