Skip to main content
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1980 Jun 25;8(12):2823–2833. doi: 10.1093/nar/8.12.2823

Procollagen mRNA metabolism during the fibroblast cell cycle and its synthesis in transformed cells.

I Parker, W Fitschen
PMCID: PMC324123  PMID: 6253892

Abstract

Procollagen mRNA was isolated from mouse embryos and used for the synthesis of a highly labelled cDNA probe complementary to collagen mRNA. This probe was used for the investigation of procollagen mRNA metabolism during the cell cycle of 3T6 mouse embryo fibroblasts in culture. Titration hybridization experiments revealed that procollagen mRNA was present throughout the cell cycle following stumulation of confluent monolayers. Procollagen mRNA levels of sparse cultures appeared similar to those of unstimulated monolayers. The fluctuating levels of collagen synthesis during the cell cycle can be ascribed to changes in the amount of collagen mRNA present. In mouse sarcoma virus transformed 3T3 cells only 20--30% of the amount of procollagen mRNA in 3T3 cells is present indicating that the decline in collagen synthesis is due to mRNA availability.

Full text

PDF
2823

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adams S. L., Sobel M. E., Howard B. H., Olden K., Yamada K. M., de Crombrugghe B., Pastan I. Levels of translatable mRNAs for cell surface protein, collagen precursors, and two membrane proteins are altered in Rous sarcoma virus-transformed chick embryo fibroblasts. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3399–3403. doi: 10.1073/pnas.74.8.3399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Boedtker H., Crkvenjakov R. B., Last J. A., Doty P. The identification of collagen messenger RNA. Proc Natl Acad Sci U S A. 1974 Oct;71(10):4208–4212. doi: 10.1073/pnas.71.10.4208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Detke S., Lichtler A., Phillips I., Stein J., Stein G. Reassessment of histone gene expression during cell cycle in human cells by using homologous H4 histone cDNA. Proc Natl Acad Sci U S A. 1979 Oct;76(10):4995–4999. doi: 10.1073/pnas.76.10.4995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Frischauf A. M., Lehrach H., Rosner C., Boedtker H. Procollagen complementary DNA, a probe for messenger RNA purification and the number of type I collagen genes. Biochemistry. 1978 Aug 8;17(16):3243–3249. doi: 10.1021/bi00609a011. [DOI] [PubMed] [Google Scholar]
  5. Getz M. J., Birnie G. D., Young B. D., MacPhail E., Paul J. A kinetic estimation of base sequence complexity of nuclear poly(A)-containing RNA in mouse Friend cells. Cell. 1975 Feb;4(2):121–129. doi: 10.1016/0092-8674(75)90118-x. [DOI] [PubMed] [Google Scholar]
  6. Haralson M. A., Sonneborn J. H., Mitchell W. M. Chinese hamster lung cell polysomes direct the synthesis of a single molecular weight species of procollagen alpha chains. J Biol Chem. 1978 Aug 10;253(15):5536–5542. [PubMed] [Google Scholar]
  7. Harrison P. R., Birnie G. D., Hell A., Humphries S., Young B. D., Paul J. Kinetic studies of gene frequency. I. Use of a DNA copy of reticulocyte 9 S RNA to estimate globin gene dosage in mouse tissues. J Mol Biol. 1974 Apr 25;84(4):539–554. doi: 10.1016/0022-2836(74)90115-6. [DOI] [PubMed] [Google Scholar]
  8. Howard B. H., Adams S. L., Sobel M. E., Pastan I., de Crombrugghe B. Decreased levels of collagen mRNA in rous sarcoma virus-transformed chick embryo fibroblasts. J Biol Chem. 1978 Aug 25;253(16):5869–5874. [PubMed] [Google Scholar]
  9. Humphries S., Windass J., Williamson R. Mouse globin gene expression in erythroid and non-erythroid tissues. Cell. 1976 Feb;7(2):267–277. doi: 10.1016/0092-8674(76)90026-x. [DOI] [PubMed] [Google Scholar]
  10. Jansing R. L., Stein J. L., Stein G. S. Activation of histone gene transcription by nonhistone chromosomal proteins in WI-38 human diploid fibroblasts. Proc Natl Acad Sci U S A. 1977 Jan;74(1):173–177. doi: 10.1073/pnas.74.1.173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kamine J., Rubin H. Coordinate control of collagen synthesis and cell growth in chick embryo fibroblasts and the effect of viral transformation on collagen synthesis. J Cell Physiol. 1977 Jul;92(1):1–11. doi: 10.1002/jcp.1040920102. [DOI] [PubMed] [Google Scholar]
  12. Levene C. I., Ockleford C. D., Barber C. L. Scurvy; a comparison between ultrastructural and biochemical changes observed in cultured fibroblasts and the collagen they synthesise. Virchows Arch B Cell Pathol. 1977 Apr 15;23(4):325–338. doi: 10.1007/BF02889141. [DOI] [PubMed] [Google Scholar]
  13. Marcu K., Dudock B. Characterization of a highly efficient protein synthesizing system derived from commercial wheat germ. Nucleic Acids Res. 1974 Nov;1(11):1385–1397. doi: 10.1093/nar/1.11.1385. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Miller E. J. Biochemical characteristics and biological significance of the genetically-distinct collagens. Mol Cell Biochem. 1976 Dec 10;13(3):165–192. doi: 10.1007/BF01731779. [DOI] [PubMed] [Google Scholar]
  15. Narayanan A. S., Page R. C., Kuzan F. Collagens synthesized in vitro by diploid fibroblasts obtained from chronically inflamed human connective tissue. Lab Invest. 1978 Jul;39(1):61–65. [PubMed] [Google Scholar]
  16. Oikarinen A., Anttinen H., Kivirikko K. I. Hydroxylation of lysine and glycosylation of hydroxylysine during collagen biosynthesis in isolated chick-embryo cartilage cells. Biochem J. 1976 Jun 15;156(3):545–551. doi: 10.1042/bj1560545. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Parker I., Fitschen W. Globin gene expression in MSV-transformed fibroblasts. Experientia. 1979 Oct 15;35(10):1312–1313. doi: 10.1007/BF01963978. [DOI] [PubMed] [Google Scholar]
  18. Parker I., Fitschen W. Histone mRNA metabolism during the mouse fibroblast cell cycle. Cell Differ. 1980 Feb;9(1):23–30. doi: 10.1016/0045-6039(80)90004-4. [DOI] [PubMed] [Google Scholar]
  19. Pearson W. R., Davidson E. H., Britten R. J. A program for least squares analysis of reassociation and hybridization data. Nucleic Acids Res. 1977 Jun;4(6):1727–1737. doi: 10.1093/nar/4.6.1727. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Rowe D. W., Moen R. C., Davidson J. M., Byers P. H., Bornstein P., Palmiter R. D. Correlation of procollagen mRNA levels in normal and transformed chick embryo fibroblasts with different rates of procollagen synthesis. Biochemistry. 1978 May 2;17(9):1581–1590. doi: 10.1021/bi00602a001. [DOI] [PubMed] [Google Scholar]
  21. STUDIER F. W. SEDIMENTATION STUDIES OF THE SIZE AND SHAPE OF DNA. J Mol Biol. 1965 Feb;11:373–390. doi: 10.1016/s0022-2836(65)80064-x. [DOI] [PubMed] [Google Scholar]
  22. Stein G., Park W., Thrall C., Mans R., Stein J. Regulation of cell cycle stage-specific transcription of histone genes from chromatin by non-histone chromosomal proteins. Nature. 1975 Oct 30;257(5529):764–767. doi: 10.1038/257764a0. [DOI] [PubMed] [Google Scholar]
  23. Stein J. L., Thrall C. L., Park W. D., Mans R. J., Stein G. S. Hybridization analysis of histone messenger RNA: association with polyribosomes during the cell cycle. Science. 1975 Aug 15;189(4202):557–558. doi: 10.1126/science.1145212. [DOI] [PubMed] [Google Scholar]
  24. Wang L., Simões C. L., Sonohara S., Brentani M., Andrade H. F., Jr, da Silva S. M., Salles J. M., Marques N., Brentani R. Isolation and characterization of collagen messenger RNA*. Nucleic Acids Res. 1975 May;2(5):655–666. doi: 10.1093/nar/2.5.655. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Woods D., Fitschen W. Purification of cDNA complementary to sea urchin histone mRNA. Nucleic Acids Res. 1977 Sep;4(9):3187–3198. doi: 10.1093/nar/4.9.3187. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES