Abstract
In studying the functional role of an extracellular matrix proteo-glycan, decorin, we have made observations that suggest a role for this proteoglycan in the control of cell proliferation. Extracellular matrices are made up of different combinations of collagens, elastin, hyaluronic acid, proteoglycans and various glycoproteins such as fibronectin. Most of these components can interact with cells, and much of the control of cell adhesion, migration and differentiation appears to be mediated by these interactions1. Earlier studies have also attributed growth-regulatory activities to intact extracellular matrices2, but the individual molecules responsible for these effects have not been characterized. We report here that Chinese hamster ovary (CHO) cell lines expressing human decorin3–9 from a stably transfected complementary DNA construct form a more orderly monolayer and grow to a lower saturation density than control cells lacking decorin. The extent of the morphological changes correlates with the level of decorin expression, and the saturation density is inversely proportional to it. The reduction in the saturation densities of the cell lines with the highest expression of decorin is more than 50%. These results reveal a novel growth inhibitory mechanism which may be related to contact inhibition of cell proliferation.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Ruoslahti, E. & Pierschbacher, M. D. Science 238, 491–497 (1987).
Gospodarowicz, D., Ferrara, N., Schweigerer, L. & Neufeld, G. Endocr. Rev. 8, 95–114 (1987).
Ruoslahti, E. A. Rev. Cell Biol. (in the press).
Pearson, C. H., Winterbottom, N., Fackre, D. S., Scott, P. G. & Carpenter, M. R. J. biol. Chem. 258, 15101–15104 (1983).
Glössl, J., Beck, M. & Kresse, H. J. biol. Chem. 259, 14144–14150 (1980).
Brennan, M. J., Oldberg, Å., Pierschbacher, M. D. & Ruoslahti, E. J. biol Chem. 259, 13742–13750 (1984).
Krusius, T. & Ruoslahti, E. Proc. natn. Acad. Sci. U.S.A. 83, 7683–7687 (1986).
Day, A. A., McQuillan, C. I., Termine, J. D. & Young, M. R. Biochem. J. 248, 801–805 (1987).
Schmidt, G. et al. J. Cell Biol. 104, 1683–1691 (1987).
Mulligan, R. C. & Berg, P. Science 209, 1423–1427 (1980).
Subramani, S., Mulligan, R. & Berg, P. Molec. Cell Biol. 1, 854–864 (1981).
Kaufman, R. J. & Sharp, P. A. J. molec. Biol. 159, 601–621 (1982).
Knox, P. & Wells, P. J. Cell Science 40, 77–88 (1979).
Brennan, M. J., Oldberg, Å., Hayman, E. G. & Ruoslahti, E. Cancer Res. 43, 4302–4307 (1983).
Rosenberg, L. C., Choi, H. U., Poole, A. R. Lewandowska, K. & Culp, L. A. Ciba Fdn Symp. 124, 47–68 (1986).
Fritze, L. M. S., Reilly, C. F. & Rosenberg, R. D. J. Cell Biol. 100, 1041–1049 (1985).
Ishihara, M., Fedarko, N. S. & Conrad, H. E. J. biol Chem. 262, 4708–4716 (1987).
Vogel, K. G. & Heinegard, D. Biochem. J. 223, 587–597 (1984).
Scott, J. E. Biochem. J. 218, 229–233 (1984).
Saunders, S. & Bernfield, M. J. Cell Biol. 106, 423–430 (1988).
Izzard, C. S., Radinsky, R. & Culp, L. A. Expl. Cell Res. 165, 320–336 (1986)
Woods, A., Couchman, J. R., Johansson, S. & Höök, M. EMBO J. 5, 665–670 (1986).
Bassols, A. & Massagué, J. J. biol Chem. 263, 3039–3045 (1988).
Sporn, M. B., Roberts, A. B., Wakefield, L. M. & de Crombrugghe, B. J. Cell Biol. 105, 1039–1045 (1987).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Yamaguchi, Y., Ruoslahti, E. Expression of human proteoglycan in Chinese hamster ovary cells inhibits cell proliferation. Nature 336, 244–246 (1988). https://doi.org/10.1038/336244a0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/336244a0
This article is cited by
-
Sequence features, structure, ligand interaction, and diseases in small leucine rich repeat proteoglycans
Journal of Cell Communication and Signaling (2021)
-
Small leucine-rich proteoglycans (SLRPs) in the endometrium of polycystic ovary syndrome women: a pilot study
Journal of Ovarian Research (2017)
-
Modulation of small leucine-rich proteoglycans (SLRPs) expression in the mouse uterus by estradiol and progesterone
Reproductive Biology and Endocrinology (2011)
-
The novel use of decorin in prevention of the development of proliferative vitreoretinopathy (PVR)
Graefe's Archive for Clinical and Experimental Ophthalmology (2011)
-
Presence of activating KRAS mutations correlates significantly with expression of tumour suppressor genes DCN and TPM1 in colorectal cancer
BMC Cancer (2009)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.