Changes in Actin during Cell Differentiation

  • Kazuhiro Nagata
  • Yasuo Ichikawa


Since the pioneering work by Loewy and Hoffman-Berling, the actomyosin system has been believed to have an important function not only in muscle cells but in nonmuscle cells (reviewed by Pollard and Weihing, 1974). Non-muscle cell actin was first purified from Physarum by Hatano and Oosawa (1966a,b). Success in identifying actin filaments as arrowhead figures in situ (Ishikawa et al., 1969), methods devised to purify nonmuscle cell actin (Gordon et al., 1976a), and the establishment of a DNase I inhibition assay that measures actin contents (Blikstad et al., 1978) show the great progress made in this field. In addition, there has been increased interest in various nonmuscle cell actins, functional and chemical differences among actin molecules from different sources, as well as differences in their control mechanisms.


Conditioned Medium Actin Filament Actin Polymerization Crude Cell Extract Skeletal Muscle Myosin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Abramowitz, J. W., Stracher, A., and Detwiler, T. C., 1975, A second form of actin: Platelet microfilaments depolymerized by ATP and divalent. cations, Arch. Bzochem. Biophys. 167: 230–237.CrossRefGoogle Scholar
  2. Bamburg, J. R., Harris, H. E., and Weeds, A. G., 1980, Partial purification and characterization of an actin depolymerizing factor from brain, FEBS Lett. 121: 178–182.PubMedCrossRefGoogle Scholar
  3. Blikstad, I., Markey, F., Carlsson, L., Persson, T., and Lindberg, U., 1978, Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I, Cell 15: 935–943.PubMedCrossRefGoogle Scholar
  4. Bosckek, C. B., Jockusch, B. M., Friis, R. R., Back, R., Grundmann, E., and Bauer, H., 1981, Early changes in the distribution and organization of microfilament proteins during cell transformation, Cell 24: 175–184.CrossRefGoogle Scholar
  5. Bray, ‘D., and Thomas, C., 1976, Unpolymerized actin in fibroblasts and brain, J. Mol. Biol. 105: 527–544.PubMedCrossRefGoogle Scholar
  6. Brenner, S. L., and Korn, E. D., 1980, Spectrin/actin complex isolated from sheep erythrocytes accelerates actin polymerization by simple nucleation, /. Biol. Chem. 255: 1670–1676.Google Scholar
  7. Bretscher, A., and Weber, K., 1978, Localization of actin and microfilament-associated proteins in the microvilli and terminal web of the intestinal brush border by immunofluorescence microscopy, J. Cell Biol. 79: 839–845.PubMedCrossRefGoogle Scholar
  8. Bretscher, A., and Weber, K., 1980, Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner, Cell 20: 839–847.PubMedCrossRefGoogle Scholar
  9. Bryan, J., and Kane, R. E., 1978, Separation and interaction of the major components of sea urchin actin gel, J. Mol. Biol. 125: 207–224.PubMedCrossRefGoogle Scholar
  10. Burridge, K., and Feramisco, J. R., 1981, Non-muscle a-actinins are calcium-sensitive actin-binding proteins, Nature 294: 565–567.PubMedCrossRefGoogle Scholar
  11. Carley, W. W., Barak, L. S., and Webb, W. W., 1981, F-actin aggregates in transformed cells, J. Cell Biol. 90: 797–802.PubMedCrossRefGoogle Scholar
  12. Carlsson, L., Nyström, L.-E., Sundkvist, I., Markey, F., and Lindberg, U., 1977, Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells, J. Mol. Biol. 115: 465–483.PubMedCrossRefGoogle Scholar
  13. Chang, D., Tobin, K. D., Grumet, M., and Lin, S., 1980, Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation, J. Cell Biol. 84: 455–460.CrossRefGoogle Scholar
  14. Condeelis, J. S., and Taylor, D. L., 1977, The contractile bases of amoeboid movement. V. The control of gelation, solation and contraction in extracts from Dictyostelium discoideum, J. Cell Biol. 74: 901–927.PubMedPubMedCentralCrossRefGoogle Scholar
  15. Craig, S. W., and Powell, L., 1980, Regulation of actin polymerization by villin, a 95,000 dalton cytoskeletal component of intestinal brush borders, Cell 22: 739–746.PubMedCrossRefGoogle Scholar
  16. Fine, R. E., and Bray, D., 1971, Actin in growing nerve cells, Nature New Biol. 234: 115–118.PubMedCrossRefGoogle Scholar
  17. Fine, R. E., and Taylor, L., 1976, Decreased actin and tubulin synthesis in 3T3 cells after transformation by SV40 virus, Exp. Cell Res. 102: 162–168.PubMedCrossRefGoogle Scholar
  18. Flanagan, M. D., and Lin, S., 1980, Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin, J. Biol. Chem. 255: 835–838.PubMedGoogle Scholar
  19. Garrels, J. I., and Gibson, W., 1976, Identification and characterization of multiple forms of actin, Cell 9: 793–805.PubMedCrossRefGoogle Scholar
  20. Glenney, J. R., Jr., Kaulfus, P., and Weber, K., 1981, F actin assembly modulated by villin; Cadependent nucleation and capping of the barbed end, Cell 24: 471–480.PubMedCrossRefGoogle Scholar
  21. Gordon, D. J., Eisenberg, E., and Korn, E. D., 1976a, Characterization of cytoplasmic actinisolated from Acanthamoeba castellanii by a new method, J. Biol. Chem. 251: 4778–4786.PubMedGoogle Scholar
  22. Gordon, D. J., Yang, Y.-Z. and Korn, E. D., 19766, Polymerization of Acanthamoeba actin. Kinetics, thermodynamics, and co-polymerization with muscle actin, J. Biol. Chem. 251: 7474–7479.Google Scholar
  23. Gordon, D. J., Boyer, J. L., and Korn, E. D., 1977, Comparative biochemistry of non-muscle actins, J. Biol. Chem. 252: 8300–8309.PubMedGoogle Scholar
  24. Grumet, M., and Lin, S., 1980, A platelet inhibitor protein with cytochalasin-like activity against actin polymerization in vitro, Cell 21: 439–444.PubMedCrossRefGoogle Scholar
  25. Guez, M., and Sachs, L., 1973, Purification of the protein that induces cell differentiation to macrophages and granulocytes, FEBS Lett. 37: 149–154.PubMedCrossRefGoogle Scholar
  26. Harris, D. A., and Schwartz, J. H., 1981, Characterization of brevin, a serum protein that shortens actin filaments, Proc. Natl. Acad. Sci. USA 78: 6798–6802.PubMedPubMedCentralCrossRefGoogle Scholar
  27. Hartwig, J. H., and Stossel, T. P., 1975, Isolation and properties of actin, myosin, and a new actin-binding protein in rabbit alveolar macrophages, J. Biol. Chem. 250: 5696–5705.PubMedGoogle Scholar
  28. Hartwig, J. H., and Stossel, T. P., 1979, Cytochalasin B and the structure of actin gels, J. Mol. Biol. 134: 539–553.PubMedCrossRefGoogle Scholar
  29. Hasegawa, T., Takahashi, S., Hayashi, H., and Hatano, S., 1980, Fragmin: A calcium ion sensitive regulatory factor on the formation of actin filaments, Biochemistry 19: 2677–2683.PubMedCrossRefGoogle Scholar
  30. Hatano, S., and Oosawa, F., 1966a, Extraction of an actin-like protein from the plasmodium of a myxomycete and its interaction with myosin A, J. Cell Physiol. 68: 197–202.PubMedCrossRefGoogle Scholar
  31. Hatano, S., and Oosawa, F., 19666, Isolation and characterization of plasmodium actin, Biochim. Biophys. Acta 127: 488–498.Google Scholar
  32. Helleweell, S. B., and Taylor, D. L., 1979, The contractile bases of amoeboid movement. VI. The solation-contraction coupling hypothesis, J. Cell Biol. 83: 633–648.CrossRefGoogle Scholar
  33. Hirai, K., Nagata, K., Maeda, M., and Ichikawa, Y., 1979, Changes in ultrastructures and enzyme activities during differentiation of myeloid leukemia cells to normal macrophages, Exp. Cell Res. 124: 269–283.PubMedCrossRefGoogle Scholar
  34. Hitchcock, S. E., Carlsson, L., and Lindberg, U., 1976, Depolymerization of F-actin by deoxyribonuclease I, Cell 7: 531–542.PubMedCrossRefGoogle Scholar
  35. Hoffman-Liebermann, B., and Sachs, L., 1978, Regulation of actin and other proteins in the differentiation of myeloid leukemia cells, Cell 14: 825–834.PubMedCrossRefGoogle Scholar
  36. Honma, Y., Kasukabe, T., and Hozumi, M., 1977, Structure requirements and affinity of steroids to bind with receptor for induction of differentiation of cultured mouse myeloid leukemia cells, Gann 68: 405–412.PubMedGoogle Scholar
  37. Honma, Y., Kasukabe, T., and Hozumi, M., 1978a, Production of differentiation-stimulating factor in cultured mouse myeloid leukemia cells treated by glucocorticoids, Exp. Cell Res. 111: 261–267.PubMedCrossRefGoogle Scholar
  38. Honma, Y., Kasukabe, T., and Hozumi, M., 19786, Relationships between leukemogenicity and in vivo inducibility of normal differentiation in mouse myeloid leukemia cells, J. Natl. Cancer Inst. 61: 837–841.Google Scholar
  39. Hozumi, M., 1982, A new approach to chemotherapy of myeloid leukemia: Control of leukemogenicity of myeloid leukemia cells by inducer of normal differentiation, in: Cancer Biology Reviews, Vol. 3 ( J. J. Marchalonis and M. G. Hanna Jr., eds.), pp. 153–211, Marcel Dekker, New York.Google Scholar
  40. Hozumi, M., Sugiyama, K., Mura, M., Takizawa, H., Sugimura, T., Matsushima, T., and Ichikawa, Y., 1974, Factor(s) stimulating differentiation of mouse myeloid leukemia cells found in ascitic fluid, in: Differentiation and Control of Malignancy of Tumor Cells ( W. Nakahara, T. Ono, T. Sugimura, and H. Sugano, eds.), pp. 471–483, University of Tokyo Press, Tokyo.Google Scholar
  41. Ichikawa, Y., 1969, Differentiation of a cell line of myeloid leukemia, J . Cell Physiol. 74: 223–234.PubMedCrossRefGoogle Scholar
  42. Ichikawa, Y., 1970, Further studies on the differentiation of a cell line of myeloid leukemia, J. Cell Physiol. 76: 175–184.PubMedCrossRefGoogle Scholar
  43. Ichikawa, Y., Maeda, M., and Horiuchi, M., 1975, Induction of differentiated functions which are reversibly suppressed by cytochalasin B, Exp. Cell Res. 90: 20–30.PubMedCrossRefGoogle Scholar
  44. Isenberg, G., Aebi, U., and Pollard, T. D., 1980, An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions, Nature 288: 455–459.PubMedCrossRefGoogle Scholar
  45. Ishikawa, H., Bischoff, R., and Holtzer, H., 1969, Formation of arrowhead complexes with heavy meromyosin in a variety of cell types, J. Cell Biol. 43: 312–328.PubMedPubMedCentralCrossRefGoogle Scholar
  46. Ishiura, M., and Okada, Y., 1979, The role of actin in temperature-dependent gel-sol transformation of extracts of Ehrlich ascites tumor cells, J. Cell Biol. 80: 465–480.PubMedCrossRefGoogle Scholar
  47. Kane, R. E., 1975, Preparation and purification of polymerized actin from sea urchin egg extracts, J. Cell Biol. 66: 305–315.PubMedCrossRefGoogle Scholar
  48. Kane, R. E., 1976, Actin polymerization and interaction with other proteins in temperature-induced gelation of sea urchin egg extracts, J. Cell Biol. 71: 704–714.PubMedCrossRefGoogle Scholar
  49. Kasai, M., Asakura, S., and Oosawa, F., 1962a, The G-F equilibrium in actin solutions, under various conditions, Biochim. Biophys. Acta 57: 13–21.PubMedCrossRefGoogle Scholar
  50. Kasai, M., Asakura, S., and Oosawa, F., 1962b, The cooperative nature of G-F transformation of actin, Biochim. Biophys. Acta 57: 22–31.PubMedCrossRefGoogle Scholar
  51. Kasukabe, T., Honma, Y., and Hozumi, M., 1977, Induction of lysosomal enzyme activities with glucocorticoids during differentiation of cultured mouse myeloid leukemia cells, Gann 68: 765–773.PubMedGoogle Scholar
  52. Lazarides, E., 1976, Actin, a-actinin, and tropomyosin interaction in the structural organization of actin filaments in nonmuscle cells, J. Cell Biol. 68: 202–219.PubMedCrossRefGoogle Scholar
  53. Lazarides, E., and Lindberg, U., 1974, Actin is the naturally occurring inhibitor of deoxyribonuclease I, Proc. Natl. Acad. Sci. USA 71: 4742–4746.PubMedPubMedCentralCrossRefGoogle Scholar
  54. Lazarides, E., and Weber, K., 1974, Actin antibody: The specific visualization of actin filaments in non-muscle cells, Proc. Natl. Acad. Sci. USA 71: 2268–2272.PubMedPubMedCentralCrossRefGoogle Scholar
  55. Leavitt, J., Leavitt, A., and Attallah, A. M., 1980, Dissimilar modes of expression of (3- and y-actin in normal and leukemic human T lymphocytes, J. Biol. Chem. 255: 4984–4987.PubMedGoogle Scholar
  56. Lotem, J., and Sachs, L., 1976, Control of Fc and C3 receptors on myeloid leukemic cells, J. Immunol. 116: 580–586.Google Scholar
  57. Lotem, J., and Sachs, L., 1978, In vivo induction of normal differentiation in myeloid leukemia cells, Proc. Natl. Acad. Sci. USA 75: 3781–3785.PubMedPubMedCentralCrossRefGoogle Scholar
  58. Mabuchi, I., 1981, Purification from starfish eggs of a protein that depolymerizes actin, J. Biochem. 89: 1341–1344.PubMedGoogle Scholar
  59. Mabuchi, I., Hosoya, H., and Sakai, H., 1980, Actin in the cortical layer of the sea urchin egg. Changes in its content during and after fertilization, Biomed. Res. 1: 417–426.Google Scholar
  60. MacLean-Fletcher, S. D., and Pollard, T. D., 1980a, Mechanism of action of cytochalasin B on actin, Cell 20: 329–341.PubMedCrossRefGoogle Scholar
  61. MacLean-Fletcher, S. D., and Pollard, T. D., 19806, Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors, J. Cell Biol. 85: 414–428.Google Scholar
  62. Maeda, M., and Ichikawa, Y., 1973, Spontaneous development of macrophage-like cells in a culture of myeloid leukemia cells, Gann 64: 265–271.PubMedGoogle Scholar
  63. Maeda, M., and Ichikawa, Y., 1980, Production of a colony-stimulating factor following differ-entiation of leukemic myeloblasts to macrophages, J. Cell. Physiol. 102: 323–331.PubMedCrossRefGoogle Scholar
  64. Maeda, M., Horiuchi, M., Numa, S., and Ichikawa, Y., 1977, Characterization of a differentia-tion-stimulating factor for mouse meyloid leukemia cells, Gann 68: 435–447.PubMedGoogle Scholar
  65. Markey, F., Lindberg, U., and Eriksson, L., 1978, Human platelets contain profilin, a potential regulator of actin polymerisability, FEBS Lett. 88: 75–79.PubMedCrossRefGoogle Scholar
  66. Marks, P., and Rifkind, R. A., 1978, Erythroleukemic differentiation, Annu. Rev. Biochem. 47: 419–448.PubMedCrossRefGoogle Scholar
  67. Maruta, H., and Korn, E. D., 1977, Purification from Acanthamoeba castellanii of proteins that induce gelation and syneresis of F-actin, J. Biol. Chem. 252: 399–402.PubMedGoogle Scholar
  68. Mimura, N., and Asano, A., 1979, Catsensitive gelation of actin filaments by a new protein factor, Nature 282: 44–48.PubMedCrossRefGoogle Scholar
  69. Nagata, K., and Ichikawa, Y., 1979, Requirements for RNA and protein synthesis in the induction of several differentiation-markers in a myeloid leukemia cell line, J. Cell. Physiol. 98: 167–176.PubMedCrossRefGoogle Scholar
  70. Nagata, K., Takahashi, E., Saito, M., Ono, J., Kuboyama, M., and Ogasa, K., 1976, Differentiation of a cell line of mouse myeloid leukemia. I. Simultaneous induction of lysosomal enzyme activities and phagocytosis, Exp. Cell Res. 100: 322–328.PubMedCrossRefGoogle Scholar
  71. Nagata, K., Ooguro, K., Saito, M., Kuboyama, M., and Ogasa, K., 1977, A factor inducing differentiation of mouse myeloid leukemia cells in human amniotic fluid, Gann 68: 757–764.PubMedGoogle Scholar
  72. Nagata, K., Sagara, J., and Ichikawa, Y., 1980, Changes in contractile proteins during differentiation of myeloid leukemia cells. I. Polymerization of actin, J. Cell Biol. 85: 273–282.PubMedCrossRefGoogle Scholar
  73. Nagata, K., Sagara, J., and Ichikawa, Y., 1982a, Changes in contractile proteins during differentiation of myeloid leukemia cells. II. Purification and characterization of actin, J. Cell Biol. 93: 470–478.PubMedPubMedCentralCrossRefGoogle Scholar
  74. Nagata, K., Sagara, J., and Ichikawa, Y., 1982b, A new protein factor inhibiting actin-polymerization in leukemic myeloblasts, Cell Struct. Funct. 7: 1–7.CrossRefGoogle Scholar
  75. Nagata, K., Sagara, J., and Ichikawa, Y., 1983, Changes in actin-related gelation of crude cell extracts during differentiation of myeloid leukemia cells, Cell Struct. Fund. 8: 171–183.CrossRefGoogle Scholar
  76. Nakayasu, M., Shimamura, S., Takeuchi, T., Sato, S., and Sugimura, T., 1978, A factor in human saliva that induces differentiation of mouse myeloid leukemia cells, Cancer Res. 38: 103–109.PubMedGoogle Scholar
  77. O’Farrell, P. H., 1975, High resolution two-dimensional electrophoresis of proteins, J. Biol. Chem. 250: 4007–4021.PubMedPubMedCentralGoogle Scholar
  78. Oosawa, F., and Kasai, M., 1962, A theory of linear and helical aggregation of macromolecules, J. Mol. Biol. 4: 10–21.PubMedCrossRefGoogle Scholar
  79. Pollard, T. D., 1981, Cytoplasmic contractile proteins, J. Cell Biol. 91: 156s - 165s.PubMedCrossRefGoogle Scholar
  80. Pollard, T. D., and Ito, S., 1970, Cytoplasmic filaments of Amoeba proteus. I. The role of filaments in consistency changes and movement, J. Cell Biol. 46: 267–289.PubMedPubMedCentralCrossRefGoogle Scholar
  81. Pollard, T. D., and Korn, E. D., 1971, Filaments of Amoeba proteus. II. Binding of heavy meromyosin by thin filaments of motile cytoplasmic extracts, J. Cell Biol. 48: 216–219.PubMedPubMedCentralCrossRefGoogle Scholar
  82. Pollard, T. D., and Weihing, R. R., 1974, Actin and myosin and cell movement, CRC Grit. Rev. Biochem. 2: 1–65.CrossRefGoogle Scholar
  83. Rubenstein, P. A., and Spudich, J. A., 1977, Actin microheterogeneity in chick embryo fibroblasts, Proc. Natl. Acad. Sci. USA 74: 120–123.PubMedPubMedCentralCrossRefGoogle Scholar
  84. Sachs, L., 1978, Control of normal cell differentiation and the phenotypic reversion of malignancy in myeloid leukemia, Nature 274: 535–539.PubMedCrossRefGoogle Scholar
  85. Sachs, L., 1982, Normal development programs in myeloid leukaemia: Regulatory proteins in the control of growth and differentiation, Cancer Surv. 1: 321–342.Google Scholar
  86. Sagara, J., Nagata, K., and Ichikawa, Y., 1982, Changes in myosin during differentiation of myeloid leukemia cells, J. Biochem. 91: 1363–1372.PubMedGoogle Scholar
  87. Sakiyama, S., Fujimura, S., and Sakiyama, H., 1981, Absence of y-actin expression in the mouse fibroblast cell line, L, J. Biol. Chem. 256: 31–33.PubMedGoogle Scholar
  88. Schmitt, H., 1976, Control of tubulin and actin synthesis and assembly during differentiation of neuroblastoma cells, Brain Res. 115: 165–173.PubMedCrossRefGoogle Scholar
  89. Schmitt, H., Gozes, I., and Littauer, U. Z., 1977, Decrease in levels and rates of synthesis of tubulin and actin in developing rat brain, Brain Res. 121: 327–342.PubMedCrossRefGoogle Scholar
  90. Shimizu, N., and Obinata, T., 1980, Presence of three actin types in skeletal muscle of chick embryos, Dev. Growth Diff. 22: 789–796.CrossRefGoogle Scholar
  91. Shizuta, Y., Shizuta, H., Gallo, M., Davies, P., and Pastan, I., 1976, Purification and properties of filamin, an actin binding protein from chicken gizzard, J. Biol. Chem. 251: 6562–6567.PubMedGoogle Scholar
  92. Southwick, F. S., and Stossel, T. P., 1981, Isolation of an inhibitor of actin polymerization from human polymorphonuclear leukocytes, J. Biol. Chem. 256: 3030–3036.PubMedGoogle Scholar
  93. Spudich, J. A., and Watt, S., 1971, The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin, J. Biol. Chem. 246: 4866–4871.PubMedGoogle Scholar
  94. Stendahl, O. I., Hartwig, J. H., Brotschi, E. A., and Stossel, T. P., 1980, Distribution of actin-binding protein and myosin in macrophages during spreading and phagocytosis, J. Cell Biol. 84: 215–224.PubMedCrossRefGoogle Scholar
  95. Storti, R. V., and Rich, A., 1976, Chick cytoplasmic actin and muscle actin have different structural genes, Proc. Natl. Acad. Sci. USA 73: 2346–2350.PubMedPubMedCentralCrossRefGoogle Scholar
  96. Storti, R. V., Coen, D. M., and Rich, A., 1976, Tissue-specific forms of actin in the developing chick, Cell 8: 521–527.PubMedCrossRefGoogle Scholar
  97. Stossel, T. P., and Hartwig, J. H., 1976, Interaction of actin, myosin, and a new actin-binding protein of rabbit pulmonary macrophages. II. Role in cytoplasmic movement and phagocytosis, J. Cell Biol. 68: 602–619.PubMedCrossRefGoogle Scholar
  98. Sugimura, T., Matsushima, T., Kawachi, T., Kogure, K., Tanaka, N., Miyake, S., Hozumi, M., Sato, S., and Sato, H., 1972, Disdifferentiation and carcinogenesis, Gann Monogr. 13: 31–45.Google Scholar
  99. Sugiyama, K., Tomida, M., and Hozumi, M., 1979, Differentiation-associated changes in mem- brane proteins of mouse myeloid leukemia cells, Biochim. Biophys. Acta 587: 169–179.PubMedCrossRefGoogle Scholar
  100. Taylor, D. L., and Condeelis, J. S., 1979, Cytoplasmic structure and contractility in amoeboid cells, Int. Rev. Cytol. 56: 57–144.PubMedCrossRefGoogle Scholar
  101. Tilney, L. G., 1976, The polymerization of actin. III. Aggregates of nonfilamentous actin and its associated proteins: A storage form of actin, J. Cell Biol. 69: 73–89.PubMedCrossRefGoogle Scholar
  102. Tilney, I.. G., 1978, Polymerization of actin. V. A new organelle, the actomere, that initiates the assembly of actin filaments in Thyone sperm, J. Cell Biol. 77: 551–564.PubMedCrossRefGoogle Scholar
  103. Tilney, L. G., and Detmers, P., 1975, Actin in erythrocyte ghosts and its association with spectrin. Evidence for a nonfilamentous form of these two molecules in situ, J. Cell Biol. 66: 508–520.PubMedCrossRefGoogle Scholar
  104. Tomida, M., Yamamoto, Y., and Hozumi, M., 1978, Induction by synthetic polyribonucleotide poly(I) of differentiation of cultured mouse myeloid leukemic cells, Cell Diff. 7: 305–312.CrossRefGoogle Scholar
  105. Uyemura, D. G., Brown, S. S., and Spudich, J. A., 1978, Biochemical and structural characterization of actin from Dictyostelium discoideum, J. Biol. Chem. 253: 9088–9096.Google Scholar
  106. Vandekerckhove, J., and Weber, K., 1978, At least six different actins are expressed in a higher mammal: An analysis based on the amino acid sequence of the amino-terminal tryptic peptide, J. Mol. Biol. 126: 782–802.CrossRefGoogle Scholar
  107. Wang, K., 1977, Filamin, a new high-molecular-weight protein found in smooth muscle and nonmuscle cells. Purification and properties of chicken gizzard filaroin, Biochemistry 16: 1857–1865.PubMedCrossRefGoogle Scholar
  108. Weiss, B., and Sachs, L., 1978, Indirect induction of differentiation in myeloid leukemic cells by lipid A, Proc. Natl. Acad. Sci. USA 75: 1374–1378.PubMedPubMedCentralCrossRefGoogle Scholar
  109. Wickus, G., Gruenstein, E., Robbins, P. W., and Rich, A., 1975, Decrease in membrane-associated actin of fibroblasts after transformation by Rous sarcoma virus, Proc. Natl. Acad. Sci. USA 72: 746–749.PubMedPubMedCentralCrossRefGoogle Scholar
  110. Yin, H. L., and Stossel, T. P., 1979, Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein, Nature 281: 583–586.PubMedCrossRefGoogle Scholar
  111. Yin, H. L., Zaner, K. S., and Stossel, T. P., 1980, Cat control of actin gelation. Interaction of gelsolin with actin filaments and regulation of actin gelation, J. Biol. Chem. 255: 9494–9500.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Kazuhiro Nagata
    • 1
  • Yasuo Ichikawa
    • 1
  1. 1.Department of Cytochemistry, Chest Disease Research InstituteKyoto UniversityKyotoJapan

Personalised recommendations