Post-transcriptional regulation of the pro alpha 1(I) collagen gene in pro alpha 1(I)-deficient, chemically transformed Syrian hamster embryo fibroblasts.
4-Nitroquinoline-1-oxide-transformed Syrian hamster embryo fibroblasts (NQT-SHE) synthesize the pro alpha 2 chain but not the pro alpha 1 subunit of type I procollagen, and they contain little pro alpha 1(I)mRNA. This study shows that there was no accumulation of pro alpha 1(I) poly(A)+ mRNA in NQT-SHE fibroblasts. BHK cells, a normal established line of hamster fibroblasts that synthesized collagen at approximately the same rate as NQT-SHE fibroblasts, nevertheless produced both subunits of type I collagen and contained pro alpha 1(I)mRNA. Run-off transcription assays with isolated nuclei showed that both the pro alpha 1(I) and pro alpha 2(I) genes were transcribed at about the same rate in NQT-SHE cells as well as in the normal BHK cells. These results suggest that a post-transcriptional defect, probably resulting from transformation, prevents the accumulation of pro alpha 1(I)mRNA in NQT-SHE cells.
D000818:Animals; D015152:Blotting, Northern; D002461:Cell Line, Transformed; D002467:Cell Nucleus / Q000378:metabolism; D006224:Cricetinae; D004591:Electrophoresis, Polyacrylamide Gel; D004622:Embryo, Mammalian; D005347:Fibroblasts / Q000378:metabolism; D007668:Kidney; D008647:Mesocricetus; D008970:Molecular Weight; D011061:Poly A / Q000302:isolation & purification / Q000378:metabolism; D011347:Procollagen / Q000096:biosynthesis* / Q000235:genetics* / Q000302:isolation & purification; D012313:RNA / Q000302:isolation & purification / Q000378:metabolism; D012323:RNA Processing, Post-Transcriptional; D012333:RNA, Messenger / Q000378:metabolism; D014158:Transcription, Genetic
D011347:Procollagen; D012333:RNA, Messenger; D011061:Poly A; D012313:RNA