Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1981 Sep 1;90(3):721–726. doi: 10.1083/jcb.90.3.721

Correlation between a specific molecular weight form of plasminogen activator and metabolic activity of 3T3 cells

PMCID: PMC2111885  PMID: 7197279

Abstract

In quiescent cultures of 3T3 cells, plasminogen activator (PA) is found predominantly as a 75,000 dalton species. When quiescent cells are exposed to mitogenic agents such as phorbol myristate acetate, Ca++, or 25% serum, the absolute levels of PA in cell lysates may either increase or decrease. However, a consistent observation is that in the stimulated cultures PA is found predominantly as a 49,000 dalton species. This also is the predominant form of PA in growing and transformed cells. Concomitant with the mitogen-induced stimulation of the 49,000 dalton PA in quiescent cultures is a change in morphology to one that is characteristic of growing and transformed cells. The data suggest that PA is not operative in causing the morphological change that occurs with activation; however, the 49,000 dalton PA in particular is closely related to the pleiotypic response accompanying growth stimulation and transformation.

Full Text

The Full Text of this article is available as a PDF (867.1 KB).

Selected References

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

  1. Beers W. H., Strickland S., Reich E. Ovarian plasminogen activator: relationship to ovulation and hormonal regulation. Cell. 1975 Nov;6(3):387–394. doi: 10.1016/0092-8674(75)90188-9. [DOI] [PubMed] [Google Scholar]
  2. Bell P. B., Jr Locomotory behavior, contact inhibition and pattern formation of 3T3 and polyoma virus-transformed 3T3 cells in culture. J Cell Biol. 1977 Sep;74(3):963–982. doi: 10.1083/jcb.74.3.963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Black P. H. Shedding from the cell surface of normal and cancer cells. Adv Cancer Res. 1980;32:75–199. doi: 10.1016/s0065-230x(08)60361-9. [DOI] [PubMed] [Google Scholar]
  4. Christman J. K., Copp R. P., Pedrinan L., Whalen C. E. Specificity of response in hamster cells induced to produce plasminogen activator by the tumor promoter, 12-O-tetradecanoylphorbol-13-acetate. Cancer Res. 1978 Nov;38(11 Pt 1):3854–3860. [PubMed] [Google Scholar]
  5. Dulbecco R., Elkington J. Induction of growth in resting fibroblastic cell cultures by Ca++. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1584–1588. doi: 10.1073/pnas.72.4.1584. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hozumi M., Ogawa M., Sugimura T., Takeuchi T., Umezawa H. Inhibition of tumorigenesis in mouse skin by leupeptin, a protease inhibitor from Actinomycetes. Cancer Res. 1972 Aug;32(8):1725–1728. [PubMed] [Google Scholar]
  7. Jaken S., Black P. H. Differences in intracellular distribution of plasminogen activator in growing, confluent, and transformed 3T3 cells. Proc Natl Acad Sci U S A. 1979 Jan;76(1):246–250. doi: 10.1073/pnas.76.1.246. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jaken S., Black P. H. Regulation of plasminogen activator in 3T3 cells: effect of phorbol myristate acetate on subcellular distribution and molecular weight. J Cell Biol. 1981 Sep;90(3):727–731. doi: 10.1083/jcb.90.3.727. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kaplan J. C., Kleinman L. F., Black P. H. Cell cycle dependence of simian virus 40 induction from transformed hamster cells by ultraviolet irradiation. Virology. 1975 Nov;68(1):215–220. doi: 10.1016/0042-6822(75)90162-2. [DOI] [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Loskutoff D. J., Paul D. Intracellular plasminogen activator activity in growing and quiescent cells. J Cell Physiol. 1978 Oct;97(1):9–16. doi: 10.1002/jcp.1040970103. [DOI] [PubMed] [Google Scholar]
  13. Miskin R., Easton T. G., Maelicke A., Reich E. Metabolism of acetylcholine receptor in chick embryo muscle cells: effects of RSV and PMA. Cell. 1978 Dec;15(4):1287–1300. doi: 10.1016/0092-8674(78)90054-5. [DOI] [PubMed] [Google Scholar]
  14. Miskin R., Easton T. G., Reich E. Plasminogen activator in chick embryo muscle cells: induction of enzyme by RSV, PMA and retinoic acid. Cell. 1978 Dec;15(4):1301–1312. doi: 10.1016/0092-8674(78)90055-7. [DOI] [PubMed] [Google Scholar]
  15. Ossowski L., Biegel D., Reich E. Mammary plasminogen activator: correlation with involution, hormonal modulation and comparison between normal and neoplastic tissue. Cell. 1979 Apr;16(4):929–940. doi: 10.1016/0092-8674(79)90108-9. [DOI] [PubMed] [Google Scholar]
  16. Quigley J. P. Association of a protease (plasminogen activator) with a specific membrane fraction isolated from transformed cells. J Cell Biol. 1976 Nov;71(2):472–486. doi: 10.1083/jcb.71.2.472. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Quigley J. P. Phorbol ester-induced morphological changes in transformed chick fibroblasts: evidence for direct catalytic involvement of plasminogen activator. Cell. 1979 May;17(1):131–141. doi: 10.1016/0092-8674(79)90301-5. [DOI] [PubMed] [Google Scholar]
  18. Robin R., Chou I. N., Black P. H. Proteolytic enzymes, cell surface changes, and viral transformation. Adv Cancer Res. 1975;22:203–260. doi: 10.1016/s0065-230x(08)60178-5. [DOI] [PubMed] [Google Scholar]
  19. Roblin R. O., Young P. L., Bell T. E. Concomitant secretion by transformed SVWI38-VA13-2RA cells of plasminogen activator(s) and substance (s) which prevent their detection. Biochem Biophys Res Commun. 1978 May 15;82(1):165–172. doi: 10.1016/0006-291x(78)90591-0. [DOI] [PubMed] [Google Scholar]
  20. Rohrlich S. T., Rifkin D. B. Patterns of plasminogen activator production in cultured normal embryonic cells. J Cell Biol. 1977 Oct;75(1):31–42. doi: 10.1083/jcb.75.1.31. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Strickland S., Reich E., Sherman M. I. Plasminogen activator in early embryogenesis: enzyme production by trophoblast and parietal endoderm. Cell. 1976 Oct;9(2):231–240. doi: 10.1016/0092-8674(76)90114-8. [DOI] [PubMed] [Google Scholar]
  22. Troll W., Klassen A., Janoff A. Tumorigenesis in mouse skin: inhibition by synthetic inhibitors of proteases. Science. 1970 Sep 18;169(3951):1211–1213. doi: 10.1126/science.169.3951.1211. [DOI] [PubMed] [Google Scholar]
  23. Unkeless J. C., Tobia A., Ossowski L., Quigley J. P., Rifkin D. B., Reich E. An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. I. Chick embryo fibroblast cultures transformed by avian RNA tumor viruses. J Exp Med. 1973 Jan 1;137(1):85–111. doi: 10.1084/jem.137.1.85. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Vetterlein D., Young P. L., Bell T. E., Roblin R. Immunological characterization of multiple weight forms of human cell plasminogen activators. J Biol Chem. 1979 Feb 10;254(3):575–578. [PubMed] [Google Scholar]
  25. Wigler M., Weinstein I. B. Tumour promotor induces plasminogen activator. Nature. 1976 Jan 22;259(5540):232–233. doi: 10.1038/259232a0. [DOI] [PubMed] [Google Scholar]
  26. Willingham M. C., Yamada S. S., Pastan I. Ultrastructural antibody localization of alpha2-macroglobulin in membrane-limited vesicles in cultured cells. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4359–4363. doi: 10.1073/pnas.75.9.4359. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Wilson E. L., Reich E. Modulation of plasminogen activator synthesis in chick embryo fibroblasts by cyclic nucleotides and phorobol myristate acetate. Cancer Res. 1979 May;39(5):1579–1586. [PubMed] [Google Scholar]
  28. Wilson E. L., Reich E. Plasminogen activator in chick fibroblasts: induction of synthesis by retinoic acid; synergism with viral transformation and phorbol ester. Cell. 1978 Oct;15(2):385–392. doi: 10.1016/0092-8674(78)90007-7. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES