Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1974 Sep;71(9):3372–3376. doi: 10.1073/pnas.71.9.3372

Biological Activity of a Growth Factor for Ovarian Cells

Kenneth L Jones 1,2,3, Denis Gospodarowicz 1,2,3
PMCID: PMC433774  PMID: 4372617

Abstract

The biological activity of a protein growth factor is described. This factor was isolated from bovine pituitary tissue, and its activity was tested on cells of rat ovarian origin. Activity was assayed as growth-promoting potential measured by cell counts and is concentrationdependent. Similar growth stimulation was not produced by several cyclic nucleotides tested, neither was there crossreactivity between this growth factor and a chemically similar one produced by rat liver cells.

Keywords: pituitary, purification, tumor

Full text

PDF
3372

Images in this article

3373Image
on p.3373

Selected References

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

  1. Armelin H. A. Pituitary extracts and steroid hormones in the control of 3T3 cell growth. Proc Natl Acad Sci U S A. 1973 Sep;70(9):2702–2706. doi: 10.1073/pnas.70.9.2702. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Burger M. M., Bombik B. M., Breckenridge B. M., Sheppard J. R. Growth control and cyclic alterations of cyclic AMP in the cell cycle. Nat New Biol. 1972 Oct 11;239(93):161–163. doi: 10.1038/newbio239161a0. [DOI] [PubMed] [Google Scholar]
  3. Clark J. L., Jones K. I., Gospodarowicz D., Sato G. H. Growth response to hormones by a new rat ovary cell line. Nat New Biol. 1972 Apr 12;236(67):180–181. doi: 10.1038/newbio236180a0. [DOI] [PubMed] [Google Scholar]
  4. Corvol M. T., Malemud C. J., Sokoloff L. A pituitary growth-promoting factor for articular chondrocytes in monolayer culture. Endocrinology. 1972 Jan;90(1):262–271. doi: 10.1210/endo-90-1-262. [DOI] [PubMed] [Google Scholar]
  5. Dulak N. C., Temin H. M. A partially purified polypeptide fraction from rat liver cell conditioned medium with multiplication-stimulating activity for embryo fibroblasts. J Cell Physiol. 1973 Apr;81(2):153–160. doi: 10.1002/jcp.1040810204. [DOI] [PubMed] [Google Scholar]
  6. Dulak N. C., Temin H. M. Multiplication-stimulating activity for chicken embryo fibroblasts from rat liver cell conditioned medium: a family of small polypeptides. J Cell Physiol. 1973 Apr;81(2):161–170. doi: 10.1002/jcp.1040810205. [DOI] [PubMed] [Google Scholar]
  7. Frazier W. A., Angeletti R. H., Bradshaw R. A. Nerve growth factor and insulin. Science. 1972 May 5;176(4034):482–488. doi: 10.1126/science.176.4034.482. [DOI] [PubMed] [Google Scholar]
  8. Gospodarowicz D., Jones K. L., Sato G. Purification of a growth factor for ovarian cells from bovine pituitary glands. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2295–2299. doi: 10.1073/pnas.71.6.2295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gospodarowicz D. Single step purification of ovine luteinizing hormone by affinity chromatography. J Biol Chem. 1972 Oct 25;247(20):6491–6498. [PubMed] [Google Scholar]
  10. Hershko A., Mamont P., Shields R., Tomkins G. M. "Pleiotypic response". Nat New Biol. 1971 Aug;232(33):206–211. [PubMed] [Google Scholar]
  11. Hollenberg M. D., Cuatrecasas P. Epidermal growth factor: receptors in human fibroblasts and modulation of action by cholera toxin. Proc Natl Acad Sci U S A. 1973 Oct;70(10):2964–2968. doi: 10.1073/pnas.70.10.2964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Holley R. W., Kiernan J. A. "Contact inhibition" of cell division in 3T3 cells. Proc Natl Acad Sci U S A. 1968 May;60(1):300–304. doi: 10.1073/pnas.60.1.300. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Jainchill J. L., Todaro G. J. Stimulation of cell growth in vitro by serum with and without growth factor. Relation to contact inhibition and viral transformation. Exp Cell Res. 1970 Jan;59(1):137–146. doi: 10.1016/0014-4827(70)90632-4. [DOI] [PubMed] [Google Scholar]
  14. Liao T. H., Pierce J. G. The presence of a common type of subunit in bovine thyroid-stimulating and luteinizing hormones. J Biol Chem. 1970 Jul 10;245(13):3275–3281. [PubMed] [Google Scholar]
  15. Masui H., Garren L. D. Inhibition of replication in functional mouse adrenal tumor cells by adrenocorticotropic hormone mediated by adenosine 3':5'-cyclic monophosphate. Proc Natl Acad Sci U S A. 1971 Dec;68(12):3206–3210. doi: 10.1073/pnas.68.12.3206. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Paul D., Lipton A., Klinger I. Serum factor requirements of normal and simian virus 40-transformed 3T3 mouse fibroplasts. Proc Natl Acad Sci U S A. 1971 Mar;68(3):645–652. doi: 10.1073/pnas.68.3.645. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Pierson R. W., Jr, Temin H. M. The partial purification from calf serum of a fraction with multiplication-stimulating activity for chicken fibroblasts in cell culture and with non-suppressible insulin-like activity. J Cell Physiol. 1972 Jun;79(3):319–330. doi: 10.1002/jcp.1040790302. [DOI] [PubMed] [Google Scholar]
  18. Robison G. A., Butcher R. W., Sutherland E. W. Cyclic AMP. Annu Rev Biochem. 1968;37:149–174. doi: 10.1146/annurev.bi.37.070168.001053. [DOI] [PubMed] [Google Scholar]
  19. Temin H. M. Studies on carcinogenesis by avian sarcoma viruses. 3. The differential effect of serum and polyanions on multiplication of uninfected and converted cells. J Natl Cancer Inst. 1966 Aug;37(2):167–175. [PubMed] [Google Scholar]
  20. Uthne K. Human somatomedians. Purification and some studies on their biological actions. Acta Endocrinol Suppl (Copenh) 1973;175:1–35. [PubMed] [Google Scholar]
  21. Whitfield J. F., Rixon R. H., MacManus J. P., Balk S. D. Calcium, cyclic adenosine 3',5'-monophosphate, and the control of cell proliferation: a review. In Vitro. 1973 Jan-Feb;8(4):257–278. doi: 10.1007/BF02615905. [DOI] [PubMed] [Google Scholar]
  22. Yamasaki N., Kangawa K., Kobayashi S., Kikutani M., Sonenberg M. Amino acid sequence of a biologically active fragment of bovine growth hormone. J Biol Chem. 1972 Jun 25;247(12):3874–3880. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES