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Changes in Actin during Cell Differentiation

  • Chapter
The Cytoskeleton

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Abstract

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.

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References

  • 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.

    Article  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  Google Scholar 

  • Bray, ‘D., and Thomas, C., 1976, Unpolymerized actin in fibroblasts and brain, J. Mol. Biol. 105: 527–544.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Burridge, K., and Feramisco, J. R., 1981, Non-muscle a-actinins are calcium-sensitive actin-binding proteins, Nature 294: 565–567.

    Article  PubMed  CAS  Google Scholar 

  • Carley, W. W., Barak, L. S., and Webb, W. W., 1981, F-actin aggregates in transformed cells, J. Cell Biol. 90: 797–802.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  Google Scholar 

  • 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.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Fine, R. E., and Bray, D., 1971, Actin in growing nerve cells, Nature New Biol. 234: 115–118.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • Garrels, J. I., and Gibson, W., 1976, Identification and characterization of multiple forms of actin, Cell 9: 793–805.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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 

  • Gordon, D. J., Boyer, J. L., and Korn, E. D., 1977, Comparative biochemistry of non-muscle actins, J. Biol. Chem. 252: 8300–8309.

    PubMed  CAS  Google Scholar 

  • Grumet, M., and Lin, S., 1980, A platelet inhibitor protein with cytochalasin-like activity against actin polymerization in vitro, Cell 21: 439–444.

    Article  PubMed  CAS  Google Scholar 

  • Guez, M., and Sachs, L., 1973, Purification of the protein that induces cell differentiation to macrophages and granulocytes, FEBS Lett. 37: 149–154.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • Hartwig, J. H., and Stossel, T. P., 1979, Cytochalasin B and the structure of actin gels, J. Mol. Biol. 134: 539–553.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Hatano, S., and Oosawa, F., 19666, Isolation and characterization of plasmodium actin, Biochim. Biophys. Acta 127: 488–498.

    Google Scholar 

  • 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.

    Article  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Hitchcock, S. E., Carlsson, L., and Lindberg, U., 1976, Depolymerization of F-actin by deoxyribonuclease I, Cell 7: 531–542.

    Article  PubMed  CAS  Google Scholar 

  • Hoffman-Liebermann, B., and Sachs, L., 1978, Regulation of actin and other proteins in the differentiation of myeloid leukemia cells, Cell 14: 825–834.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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 

  • 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 

  • 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 

  • Ichikawa, Y., 1969, Differentiation of a cell line of myeloid leukemia, J . Cell Physiol. 74: 223–234.

    Article  PubMed  CAS  Google Scholar 

  • Ichikawa, Y., 1970, Further studies on the differentiation of a cell line of myeloid leukemia, J. Cell Physiol. 76: 175–184.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Kane, R. E., 1975, Preparation and purification of polymerized actin from sea urchin egg extracts, J. Cell Biol. 66: 305–315.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Kasai, M., Asakura, S., and Oosawa, F., 1962a, The G-F equilibrium in actin solutions, under various conditions, Biochim. Biophys. Acta 57: 13–21.

    Article  PubMed  CAS  Google Scholar 

  • Kasai, M., Asakura, S., and Oosawa, F., 1962b, The cooperative nature of G-F transformation of actin, Biochim. Biophys. Acta 57: 22–31.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Lazarides, E., and Lindberg, U., 1974, Actin is the naturally occurring inhibitor of deoxyribonuclease I, Proc. Natl. Acad. Sci. USA 71: 4742–4746.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • 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.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • Lotem, J., and Sachs, L., 1976, Control of Fc and C3 receptors on myeloid leukemic cells, J. Immunol. 116: 580–586.

    Google Scholar 

  • Lotem, J., and Sachs, L., 1978, In vivo induction of normal differentiation in myeloid leukemia cells, Proc. Natl. Acad. Sci. USA 75: 3781–3785.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • Mabuchi, I., 1981, Purification from starfish eggs of a protein that depolymerizes actin, J. Biochem. 89: 1341–1344.

    PubMed  CAS  Google Scholar 

  • 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.

    CAS  Google Scholar 

  • MacLean-Fletcher, S. D., and Pollard, T. D., 1980a, Mechanism of action of cytochalasin B on actin, Cell 20: 329–341.

    Article  PubMed  CAS  Google Scholar 

  • 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 

  • Maeda, M., and Ichikawa, Y., 1973, Spontaneous development of macrophage-like cells in a culture of myeloid leukemia cells, Gann 64: 265–271.

    PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • Markey, F., Lindberg, U., and Eriksson, L., 1978, Human platelets contain profilin, a potential regulator of actin polymerisability, FEBS Lett. 88: 75–79.

    Article  PubMed  CAS  Google Scholar 

  • Marks, P., and Rifkind, R. A., 1978, Erythroleukemic differentiation, Annu. Rev. Biochem. 47: 419–448.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • Mimura, N., and Asano, A., 1979, Catsensitive gelation of actin filaments by a new protein factor, Nature 282: 44–48.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • Nagata, K., Sagara, J., and Ichikawa, Y., 1982b, A new protein factor inhibiting actin-polymerization in leukemic myeloblasts, Cell Struct. Funct. 7: 1–7.

    Article  CAS  Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • O’Farrell, P. H., 1975, High resolution two-dimensional electrophoresis of proteins, J. Biol. Chem. 250: 4007–4021.

    PubMed  PubMed Central  Google Scholar 

  • Oosawa, F., and Kasai, M., 1962, A theory of linear and helical aggregation of macromolecules, J. Mol. Biol. 4: 10–21.

    Article  PubMed  CAS  Google Scholar 

  • Pollard, T. D., 1981, Cytoplasmic contractile proteins, J. Cell Biol. 91: 156s - 165s.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • 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.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • Pollard, T. D., and Weihing, R. R., 1974, Actin and myosin and cell movement, CRC Grit. Rev. Biochem. 2: 1–65.

    Article  CAS  Google Scholar 

  • Rubenstein, P. A., and Spudich, J. A., 1977, Actin microheterogeneity in chick embryo fibroblasts, Proc. Natl. Acad. Sci. USA 74: 120–123.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • Sachs, L., 1978, Control of normal cell differentiation and the phenotypic reversion of malignancy in myeloid leukemia, Nature 274: 535–539.

    Article  PubMed  CAS  Google Scholar 

  • 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 

  • Sagara, J., Nagata, K., and Ichikawa, Y., 1982, Changes in myosin during differentiation of myeloid leukemia cells, J. Biochem. 91: 1363–1372.

    PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • Schmitt, H., 1976, Control of tubulin and actin synthesis and assembly during differentiation of neuroblastoma cells, Brain Res. 115: 165–173.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Shimizu, N., and Obinata, T., 1980, Presence of three actin types in skeletal muscle of chick embryos, Dev. Growth Diff. 22: 789–796.

    Article  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • Storti, R. V., Coen, D. M., and Rich, A., 1976, Tissue-specific forms of actin in the developing chick, Cell 8: 521–527.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Taylor, D. L., and Condeelis, J. S., 1979, Cytoplasmic structure and contractility in amoeboid cells, Int. Rev. Cytol. 56: 57–144.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • 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 

  • 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.

    Article  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • 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.

    Article  PubMed  CAS  PubMed Central  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

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  1. Department of Cytochemistry, Chest Disease Research Institute, Kyoto University, Kyoto, Japan

    Kazuhiro Nagata & Yasuo Ichikawa

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  1. Kazuhiro Nagata
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  2. Yasuo Ichikawa
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  1. University of Texas Health Science Center, Dallas, Texas, USA

    Jerry W. Shay

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© 1984 Plenum Press, New York

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Nagata, K., Ichikawa, Y. (1984). Changes in Actin during Cell Differentiation. In: Shay, J.W. (eds) The Cytoskeleton. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4592-3_4

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