Tissue specificity of type I collagen gene expression is determined at both transcriptional and post-transcriptional levels.
We analyzed the control of type I collagen synthesis in four kinds of differentiated cells from chicken embryos which synthesize very different amounts of the protein. Tendon, skin, and smooth muscle cells were found to have identical amounts of type I collagen RNAs; however, the RNAs had inherently different translatabilities, which were observed both in vivo and in vitro. Chondrocytes also had substantial amounts of type I collagen RNAs, even though they directed no detectable synthesis of the protein either in vivo or in vitro. Type I collagen RNAs in chondrocytes display altered electrophoretic mobilities, suggesting that in these cells the reduction in translational efficiency may be mediated in part by changes in the RNA structure. These data indicate that control of type I collagen gene expression is a complex process which is exerted at both transcriptional and post-transcriptional levels.
D000818:Animals; D001482:Base Composition; D001483:Base Sequence; D002356:Cartilage / Q000378:metabolism; D002454:Cell Differentiation; D002478:Cells, Cultured; D002642:Chick Embryo; D003094:Collagen / Q000235:genetics*; D005347:Fibroblasts / Q000166:cytology; D005796:Genes; D007700:Kinetics; D009693:Nucleic Acid Hybridization; D014176:Protein Biosynthesis; D012867:Skin / Q000166:cytology; D013710:Tendons / Q000166:cytology; D014158:Transcription, Genetic
D003094:Collagen