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. 1975 Mar;72(3):994–998. doi: 10.1073/pnas.72.3.994

Patterns of organization of actin and myosin in normal and transformed cultured cells.

R Pollack, M Osborn, K Weber
PMCID: PMC432450  PMID: 165499

Abstract

The patterns of distribution of intracellular actin and myosin were examined by specific immunofluorescence in a series of normal, simian-virus-40-transformed, and revertant cell lines of rat and mouse origin. A consistent correlation was found between sensitivity to anchorage-dependent growth control and the presence of large, thick sheaths of actin-containing material. The presence of these sheaths was temperature-dependent in a rat line transformed by a temperature-sensitive mutant in the complementation group A of the oncogenic virus simian virus 40.

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Selected References

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

  1. Abercrombie M., Heaysman J. E., Pegrum S. M. The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella. Exp Cell Res. 1971 Aug;67(2):359–367. doi: 10.1016/0014-4827(71)90420-4. [DOI] [PubMed] [Google Scholar]
  2. Adelstein R. S., Conti M. A., Johnson G. S., Pastan I., Pollard T. D. Isolation and characterization of myosin from cloned mouse fibroblasts. Proc Natl Acad Sci U S A. 1972 Dec;69(12):3693–3697. doi: 10.1073/pnas.69.12.3693. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ambrose E. J., Batzdorf U., Osborn J. S., Stuart P. R. Sub-surface structures in normal and malignant cells. Nature. 1970 Jul 25;227(5256):397–398. doi: 10.1038/227397a0. [DOI] [PubMed] [Google Scholar]
  4. Brugge J. S., Butel J. S. Role of simian virus 40 gene A function in maintenance of transformation. J Virol. 1975 Mar;15(3):619–635. doi: 10.1128/jvi.15.3.619-635.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Buckley I. K., Porter K. R. Cytoplasmic fibrils in living cultured cells. A light and electron microscope study. Protoplasma. 1967;64(4):349–380. doi: 10.1007/BF01666538. [DOI] [PubMed] [Google Scholar]
  6. Dermer G. B., Lue J., Neustein H. B. Comparison of surface material, cytoplasmic filaments, and intercellular junctions from untransformed and two mouse sarcoma virus-transformed cell lines. Cancer Res. 1974 Jan;34(1):31–38. [PubMed] [Google Scholar]
  7. Freedman V. H., Shin S. I. Cellular tumorigenicity in nude mice: correlation with cell growth in semi-solid medium. Cell. 1974 Dec;3(4):355–359. doi: 10.1016/0092-8674(74)90050-6. [DOI] [PubMed] [Google Scholar]
  8. Goldman R. D., Berg G., Bushnell A., Chang C. M., Dickerman L., Hopkins N., Miller M. L., Pollack R., Wang E. Fibrillar systems in cell motility. Ciba Found Symp. 1973;14:83–107. doi: 10.1002/9780470719978.ch5. [DOI] [PubMed] [Google Scholar]
  9. Goldman R. D., Lazarides E., Pollack R., Weber K. The distribution of actin in non-muscle cells. The use of actin antibody in the localization of actin within the microfilament bundles of mouse 3T3 cells. Exp Cell Res. 1975 Feb;90(2):333–344. doi: 10.1016/0014-4827(75)90323-7. [DOI] [PubMed] [Google Scholar]
  10. Gröschel-Stewart U. Comparative studies of human smooth and striated muscle myosins. Biochim Biophys Acta. 1971 Feb 16;229(2):322–334. doi: 10.1016/0005-2795(71)90191-7. [DOI] [PubMed] [Google Scholar]
  11. Harris A. Location of cellular adhesions to solid substrata. Dev Biol. 1973 Nov;35(1):97–114. doi: 10.1016/0012-1606(73)90009-2. [DOI] [PubMed] [Google Scholar]
  12. Ishikawa H., Bischoff R., Holtzer H. Formation of arrowhead complexes with heavy meromyosin in a variety of cell types. J Cell Biol. 1969 Nov;43(2):312–328. [PMC free article] [PubMed] [Google Scholar]
  13. Lazarides E., Weber K. Actin antibody: the specific visualization of actin filaments in non-muscle cells. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2268–2272. doi: 10.1073/pnas.71.6.2268. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Martin R. G., Chou J. Y. Simian virus 40 functions required for the establishment and maintenance of malignant transformation. J Virol. 1975 Mar;15(3):599–612. doi: 10.1128/jvi.15.3.599-612.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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]
  16. 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]
  17. Osborn M., Weber K. Simian virus 40 gene A function and maintenance of transformation. J Virol. 1975 Mar;15(3):636–644. doi: 10.1128/jvi.15.3.636-644.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Ostlund R. E., Pastan I., Adelstein R. S. Myosin in cultured fibroblasts. J Biol Chem. 1974 Jun 25;249(12):3903–3907. [PubMed] [Google Scholar]
  19. Pollack R. E., Green H., Todaro G. J. Growth control in cultured cells: selection of sublines with increased sensitivity to contact inhibition and decreased tumor-producing ability. Proc Natl Acad Sci U S A. 1968 May;60(1):126–133. doi: 10.1073/pnas.60.1.126. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Pollack R., Risser R., Conlon S., Rifkin D. Plasminogen activator production accompanies loss of anchorage regulation in transformation of primary rat embryo cells by simian virus 40. Proc Natl Acad Sci U S A. 1974 Dec;71(12):4792–4796. doi: 10.1073/pnas.71.12.4792. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Pollack R., Vogel A. Isolation and characterization of revertant cell lines. II. Growth control of a polyploid revertant line derived from SV40-transformed 3T3 mouse cells. J Cell Physiol. 1973 Aug;82(1):93–100. doi: 10.1002/jcp.1040820111. [DOI] [PubMed] [Google Scholar]
  22. Pollard T. D., Weihing R. R. Actin and myosin and cell movement. CRC Crit Rev Biochem. 1974 Jan;2(1):1–65. doi: 10.3109/10409237409105443. [DOI] [PubMed] [Google Scholar]
  23. Risser R., Pollack R. A nonselective analysis of SV40 transformation of mouse 3T3 cells. Virology. 1974 Jun;59(2):477–489. doi: 10.1016/0042-6822(74)90457-7. [DOI] [PubMed] [Google Scholar]
  24. Risser R., Rifkin D., Pollack R. The stable classes of transformed cells induced by SV40 infection of established 3T3 cells and primary rat embryonic cells. Cold Spring Harb Symp Quant Biol. 1975;39(Pt 1):317–324. doi: 10.1101/sqb.1974.039.01.042. [DOI] [PubMed] [Google Scholar]
  25. Spooner B. S., Yamada K. M., Wessells N. K. Microfilaments and cell locomotion. J Cell Biol. 1971 Jun;49(3):595–613. doi: 10.1083/jcb.49.3.595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Stossel T. P., Pollard T. D. Myosin in polymorphonuclear leukocytes. J Biol Chem. 1973 Dec 10;248(23):8288–8294. [PubMed] [Google Scholar]
  27. Tegtmeyer P. Function of simian virus 40 gene A in transforming infection. J Virol. 1975 Mar;15(3):613–618. doi: 10.1128/jvi.15.3.613-618.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Tilney L. G., Mooseker M. Actin in the brush-border of epithelial cells of the chicken intestine. Proc Natl Acad Sci U S A. 1971 Oct;68(10):2611–2615. doi: 10.1073/pnas.68.10.2611. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Vogel A., Pollack R. Isolation and characterization of revertant cell lines. IV. Direct selection of serum-revertant sublines of SV40-transformed 3T3 mouse cells. J Cell Physiol. 1973 Oct;82(2):189–198. doi: 10.1002/jcp.1040820207. [DOI] [PubMed] [Google Scholar]
  30. Weber K., Groeschel-Stewart U. Antibody to myosin: the specific visualization of myosin-containing filaments in nonmuscle cells. Proc Natl Acad Sci U S A. 1974 Nov;71(11):4561–4564. doi: 10.1073/pnas.71.11.4561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Weber K., Lazarides E., Goldman R. D., Vogel A., Pollack R. Localization and distribution of actin fibers in normal transformed and revertant cells. Cold Spring Harb Symp Quant Biol. 1975;39(Pt 1):363–369. doi: 10.1101/sqb.1974.039.01.047. [DOI] [PubMed] [Google Scholar]
  32. Wessells N. K., Spooner B. S., Ash J. F., Bradley M. O., Luduena M. A., Taylor E. L., Wrenn J. T., Yamada K. Microfilaments in cellular and developmental processes. Science. 1971 Jan 15;171(3967):135–143. doi: 10.1126/science.171.3967.135. [DOI] [PubMed] [Google Scholar]
  33. Wessells N. K., Spooner B. S., Ludueña M. A. Surface movements, microfilaments and cell locomotion. Ciba Found Symp. 1973;14:53–82. doi: 10.1002/9780470719978.ch4. [DOI] [PubMed] [Google Scholar]
  34. Yang Y. Z., Perdue J. F. Contractile proteins of cultured cells. I. The isolation and characterization of an actin-like protein from cultured chick embryo fibroblasts. J Biol Chem. 1972 Jul 25;247(14):4503–4509. [PubMed] [Google Scholar]

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