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. 1978 Jul 1;78(1):28–35. doi: 10.1083/jcb.78.1.28

Actin content and organization in normal and transformed cells in culture

PMCID: PMC2110180  PMID: 566761

Abstract

The amount of actin and total protein per cell in normal rat kidney (NRK) cells in culture is initially high in very low density cultures, but rapidly decreases as the cells come into contact in higher density cultures. In a viral transformant of NRK (442), the level of actin and total protein does not change significantly from low to high density cultures. NRK cells, which are flattened against the substrate, have prominent bundles of actinlike microfilaments in the basal cytoplasm adjacent to the substrate. 442 cells, which adhere poorly and are more spherical in shape, lack well-organized basal microfilament bundles, but may display microfilament bundles in cytoplasmic processes extending from the cell body. The percentage of insoluble actin is less than 20% in both cell lines, and 442 cells consistently contain smaller amounts than NRK cells.

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Selected References

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  1. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  2. Bray D., Brownlee S. M. Peptide mapping of proteins from acrylamide gels. Anal Biochem. 1973 Sep;55(1):213–221. doi: 10.1016/0003-2697(73)90306-0. [DOI] [PubMed] [Google Scholar]
  3. Bray D., Thomas C. The actin content of fibroblasts. Biochem J. 1975 May;147(2):221–228. doi: 10.1042/bj1470221. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bray D., Thomas C. Unpolymerized actin in fibroblasts and brain. J Mol Biol. 1976 Aug 25;105(4):527–544. doi: 10.1016/0022-2836(76)90233-3. [DOI] [PubMed] [Google Scholar]
  5. Edelman G. M., Yahara I. Temperature-sensitive changes in surface modulating assemblies of fibroblasts transformed by mutants of Rous sarcoma virus. Proc Natl Acad Sci U S A. 1976 Jun;73(6):2047–2051. doi: 10.1073/pnas.73.6.2047. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fine R. E., Taylor L. Decreased actin and tubulin synthesis in 3T3 cells after transformation by SV40 virus. Exp Cell Res. 1976 Oct 1;102(1):162–168. doi: 10.1016/0014-4827(76)90311-6. [DOI] [PubMed] [Google Scholar]
  7. Goldman R. D., Yerna M. J., Schloss J. A. Localization and organization of microfilaments and related proteins in normal and virus-transformed cells. J Supramol Struct. 1976;5(2):155–183. doi: 10.1002/jss.400050206. [DOI] [PubMed] [Google Scholar]
  8. Heaysman J. E., Pegrum S. M. Early contacts between fibroblasts. An ultrastructural study. Exp Cell Res. 1973 Mar 30;78(1):71–78. doi: 10.1016/0014-4827(73)90039-6. [DOI] [PubMed] [Google Scholar]
  9. Kane R. E. Actin polymerization and interaction with other proteins in temperature-induced gelation of sea urchin egg extracts. J Cell Biol. 1976 Dec;71(3):704–714. doi: 10.1083/jcb.71.3.704. [DOI] [PMC free article] [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. Malick L. E., Langenbach R. Scanning electron microscopy of in vitro chemically transformed mouse embryo cells. J Cell Biol. 1976 Mar;68(3):654–664. doi: 10.1083/jcb.68.3.654. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. McNutt N. S., Culp L. A., Black P. H. Contact-inhibited revertant cell lines isolated from SV 40-transformed cells. IV. Microfilament distribution and cell shape in untransformed, transformed, and revertant Balb-c 3T3 cells. J Cell Biol. 1973 Feb;56(2):412–428. doi: 10.1083/jcb.56.2.412. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. McNutt N. S., Culp L. A., Black P. H. Contact-inhibited revertant cell lines isolated from SV40-transformed cells. II. Ultrastructural study. J Cell Biol. 1971 Sep;50(3):691–708. doi: 10.1083/jcb.50.3.691. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Pollack R., Osborn M., Weber K. Patterns of organization of actin and myosin in normal and transformed cultured cells. Proc Natl Acad Sci U S A. 1975 Mar;72(3):994–998. doi: 10.1073/pnas.72.3.994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Pollard T. D. The role of actin in the temperature-dependent gelation and contraction of extracts of Acanthamoeba. J Cell Biol. 1976 Mar;68(3):579–601. doi: 10.1083/jcb.68.3.579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Porter K. R., Todaro G. J., Fonte V. A scanning electron microscope study of surface features of viral and spontaneous transformants of mouse Balb-3T3 cells. J Cell Biol. 1973 Dec;59(3):633–642. doi: 10.1083/jcb.59.3.633. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Rubin R. W., Maher M. Actin turnover during encystation in Acanthamoeba. Exp Cell Res. 1976 Nov;103(1):159–168. doi: 10.1016/0014-4827(76)90251-2. [DOI] [PubMed] [Google Scholar]
  18. SALZMAN N. P. Systematic fluctuations in the cellular protein, RNA and DNA during growth of mammalian cell cultures. Biochim Biophys Acta. 1959 Jan;31(1):158–163. doi: 10.1016/0006-3002(59)90451-2. [DOI] [PubMed] [Google Scholar]
  19. Tanaka K., Ichihara A. Effect of the growth state on protein turnover in L cells. Exp Cell Res. 1976 Apr;99(1):1–6. doi: 10.1016/0014-4827(76)90672-8. [DOI] [PubMed] [Google Scholar]
  20. Tilney L. G. The polymerization of actin. III. Aggregates of nonfilamentous actin and its associated proteins: a storage form of actin. J Cell Biol. 1976 Apr;69(1):73–89. doi: 10.1083/jcb.69.1.73. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Tsuboi A., Kurotsu T., Terasima T. Changes in protein content per cell during growth of mouse L cells. Exp Cell Res. 1976 Dec;103(2):257–261. doi: 10.1016/0014-4827(76)90262-7. [DOI] [PubMed] [Google Scholar]
  22. Vollet J. J., Brugge J. S., Noonan C. A., Butel J. S. The role of SV40 gene A in the alteration of microfilaments in transformed cells. Exp Cell Res. 1977 Mar 1;105(1):119–126. doi: 10.1016/0014-4827(77)90157-4. [DOI] [PubMed] [Google Scholar]
  23. Wang E., Goldberg A. R. Changes in microfilament organization and surface topogrophy upon transformation of chick embryo fibroblasts with Rous sarcoma virus. Proc Natl Acad Sci U S A. 1976 Nov;73(11):4065–4069. doi: 10.1073/pnas.73.11.4065. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Willingham M. C., Yamada K. M., Yamada S. S., Pouysségur J., Pastan I. Microfilament bundles and cell shape are related to adhesiveness to substratum and are dissociable from growth control in cultured fibroblasts. Cell. 1977 Mar;10(3):375–380. doi: 10.1016/0092-8674(77)90024-1. [DOI] [PubMed] [Google Scholar]

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