The Department of Genetic Medicine at Weill Cornell leads a dynamic and innovative translational research program, advancing diverse fields such as Genetic Therapy and Personalized Medicine.
Our translational research program aims to leverage our expertise in genetic therapies and personalized medicine to develop clinical solutions that target the molecular causes of human diseases.
The Department of Genetic Medicine advances treatments and diagnostics through diverse clinical trials, including drug testing and research to better understand diseases.
The Department of Genetic Medicine at Weill Cornell leads a dynamic and innovative translational research program, advancing diverse fields such as Genetic Therapy and Personalized Medicine.
Our translational research program aims to leverage our expertise in genetic therapies and personalized medicine to develop clinical solutions that target the molecular causes of human diseases.
The Department of Genetic Medicine advances treatments and diagnostics through diverse clinical trials, including drug testing and research to better understand diseases.
Miskulin M, Dalgleish R, Kluve-Beckerman B, Rennard S, Tolstoshev P, Brantly M, Crystal R
Journal
Biochemistry
Volume
25
Issue
6
Pagination
1408-13
Date Published
03/25/1986
ISSN
0006-2960
Keywords
Cloning, Molecular, Collagen, Genes
Abstract
Type III collagen is one of the major interstitial collagens and, as such, plays an important role in modulating the structure and function of most tissues. To compare the expression of the type III collagen gene to that of the type I collagen alpha 1(I) and alpha 2(I) genes, cDNAs encoding the 3' one-third of the human alpha 1(III) collagen mRNA were obtained by screening a human fetal lung fibroblast cDNA library with a cloned segment of the chicken alpha 1(III) gene. Northern blot analysis of human fetal lung fibroblast RNA demonstrated two alpha 1(III)-specific mRNAs of sizes 6.6 and 5.8 kilobases, sizes clearly different from those of the type I collagen mRNAs. Analyses of populations of dividing and nondividing human lung fibroblasts revealed that, on a per cell basis, the nondividing population contained twice as much alpha 1(III) mRNA than did the dividing population. The same was true for the type I collagen alpha 1(I) and alpha 2(I) mRNA transcripts. Similar results were obtained when alpha 1(III), alpha 1(I), and alpha 2(I) mRNA transcripts were quantified by using dot blot evaluation of total RNA, Northern analysis of total RNA, and dot blot evaluation of cytoplasmic RNA. Thus, despite the fact that the alpha 1(III) collagen gene is located on a chromosome different from the alpha 1(I) and alpha 2(I) genes, the expression of these three collagen chains appears to be coordinately controlled during periods of rapid and slow fibroblast growth.