Regulation of Type I Collagen Genes Expression
- 1 January 1995
- journal article
- review article
- Published by Informa UK Limited in International Reviews of Immunology
- Vol. 12 (2-4), 177-185
- https://doi.org/10.3109/08830189509056711
Abstract
Type I collagen, the most abundant protein of the body, is preferentially synthesized in bone, dermis, and tendons by two cell types, the osteoblast and the fibroblast. The expression of type I collagen is increased in the various forms of fibrosis such as lung, liver, bone marrow fibrosis and scleroderma. Type I collagen is a heterotrimer molecule consisting of two alpha 1(I) chains and one alpha 2(I) chain. The two polypeptide chains are synthesized in a 2:1 stoichiometry. The same 2:1 ratio is observed for the rate of synthesis of the corresponding mRNAs. One hypothesis that would explain how this coregulation occurs at the transcriptional level is that common cis-acting elements are present on both genes. These common regulatory elements would bind identical transcription factors displaying the same function. The characterization of the various regulatory elements present in these genes would foster our understanding of the molecular mechanisms controlling type I collagen gene expression in normal and in pathological situations. Over the past few years, several laboratories have identified cis-acting elements in the promoters of the COL1A1 and COL1A2 genes. At least, two of these cis-acting elements are common to both promoters. One is centered by a pentanucleotide CCAAT and binds a ubiquitously expressed heteromeric CCAAT binding factor. A second one is centered by a G-rich region and it binds a new transcription factor called C-Krox.(ABSTRACT TRUNCATED AT 250 WORDS)Keywords
This publication has 31 references indexed in Scilit:
- The zinc finger transcription factor Egr-1 is essential for and restricts differentiation along the macrophage lineageCell, 1993
- Minimal DNA sequences that control the cell lineage-specific expression of the pro alpha 2(I) collagen promoter in transgenic mice.The Journal of cell biology, 1992
- Differential utilization of regulatory domains within the alpha 1(I) collagen promoter in osseous and fibroblastic cells.The Journal of cell biology, 1992
- Tumor necrosis factor-alpha and interferon-gamma suppress the activation of human type I collagen gene expression by transforming growth factor-beta 1. Evidence for two distinct mechanisms of inhibition at the transcriptional and posttranscriptional levels.JCI Insight, 1990
- Segment-specific expression of a zinc-finger gene in the developing nervous system of the mouseNature, 1989
- Selective Activation of Transcription by a Novel CCAAT Binding FactorScience, 1988
- A nuclear factor 1 binding site mediates the transcriptional activation of a type I collagen promoter by transforming growth factor-βCell, 1988
- Gamma-interferon inhibits collagen synthesis in vivo in the mouse.JCI Insight, 1987
- Influences of gamma interferon on synovial fibroblast-like cells. Ia induction and inhibition of collagen synthesis.JCI Insight, 1985
- Selective inhibition of human diploid fibroblast collagen synthesis by interferons.JCI Insight, 1984