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  • 1
    Electronic Resource
    Electronic Resource
    Spatial regulation of β-actin translation by Src-dependent phosphorylation of ZBP1 (2005)
    [s.l.] : Nature Publishing Group
    Nature 438 (2005), S. 512-515 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Localization of β-actin messenger RNA to sites of active actin polymerization modulates cell migration during embryogenesis, differentiation and possibly carcinogenesis. This localization requires the oncofetal protein ZBP1 (Zipcode binding protein 1), which binds to a conserved ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature04115
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  • 2
    Electronic Resource
    Electronic Resource
    THE GREAT ESCAPE: When Cancer Cells Hijack the Genes for Chemotaxis and Motility (2005)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 21 (2005), S. 695-718 
    Details
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: The combined use of the new technologies of multiphoton-based intravital imaging, the chemotaxis-mediated collection of invasive cells, and high sensitivity expression profiling has allowed the correlation of the behavior of invasive tumor cells in vivo with their gene expression patterns. New insights have resulted including a gene expression signature for invasive cells and the tumor microenvironment invasion model. This model proposes that tumor invasion and metastasis can be studied as a problem resembling normal morphogenesis. We discuss how these new insights may lead to a better understanding of the molecular basis of the invasive behavior of tumor cells in vivo, which may result in new strategies for the diagnosis and treatment of metastasis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.cellbio.21.122303.120306
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  • 3
    Electronic Resource
    Electronic Resource
    The Arrangement of the Actin Lattice in the Basal Cytoplasm of Toad Urinary Bladder Epithelial Cells (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 435 (1984), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1984.tb13790.x
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  • 4
    Electronic Resource
    Electronic Resource
    Identification of an actin-binding protein from Dictyostelium as elongation factor 1a (1990)
    [s.l.] : Nature Publishing Group
    Nature 347 (1990), S. 494-496 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] To investigate the mechanism of actin binding of ABP-50 and its regulation by chemotactic stimulation, ABP-50 was cloned and sequenced. Affinity purified polyclonal antibodies raised against ABP-509 were used to screen a Agtll cDNA library (kindly provided by Peter Devreotes of Johns Hopkins ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/347494a0
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  • 5
    Electronic Resource
    Electronic Resource
    The effect of vasopressin on the cytoskeleton of the epithelial cell (1993)
    Springer
    Pediatric nephrology 7 (1993), S. 672-679 
    Details
    ISSN: 1432-198X
    Keywords: Vasopressin ; Actin ; Cytoskeleton ; Urine concentration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Vasopressin (AVP) promotes the fusion of vesicles containing water channels with the apical membrane of receptor cells in the amphibian bladder and mammalian kidney. Fusion is accompanied by depolymerization of the actin cytoskeleton. In this review, we present the evidence for actin depolymerization by AVP in the whole cell, and the application of confocal microscopy and immunogold electron microscopy in localizing depolymerization to the apical region of the receptor cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00852577
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  • 6
    Electronic Resource
    Electronic Resource
    Chemotaxis of metastatic tumor cells: Clues to mechanisms from the Dictyostelium paradigm (1992)
    Springer
    Cancer and metastasis reviews 11 (1992), S. 55-68 
    Details
    ISSN: 1573-7233
    Keywords: cortical expansion model ; actin ; actin binding proteins ; signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Amoeboid movement, and in some cases, amoeboid chemotaxis, is a key step in tumor metastasis. The high degree of conservation in signal transduction pathways and motile machinery in eukaryotic cells suggests that insights and molecular probes developed from the study of these processes in easily manipulated experimental model systems will be applicable directly to experimentally intractable tumor cells. One such model system, Dictyostelium discoideum, is discussed in terms of the molecular events involved in amoeboid chemotaxis. The application of insights and assays developed with Dictyostelium to early events in the chemotaxis of Lewis lung carcinoma cells is reviewed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00047603
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  • 7
    Electronic Resource
    Electronic Resource
    Isolation of a new actin-binding protein from dictyostelium discoideum (1982)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 273-285 
    Details
    ISSN: 0886-1544
    Keywords: actin gelation ; F-actin nucleation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A new actin binding protein has been purified to homogeneity from amoebae of Dictyostelium discoideum. This protein is a single polypeptide with a molecular weight of 120,000 upon sodium dodecyl sulfate gel electrophoresis. It is soluble and trypsin-sensitive, contains no carbohydrate, increases the viscosity and sedimentation rate of F actin, and inhibits the actin-stimulated Mg ATPase of rabbit muscle heavy meromyosin. The interaction of 120,000-dalton protein with F actin is not inhibited by millimolar ATP, pyrophosphate, or micromolar calcium. The 120,000-dalton actin binding protein increases the initial rate of actin polymerization and decreases the critical concentration of actin at steady state.These properties demonstrate that 120,000-dalton protein from Dictyostelium discoidum is not a myosinlike protein. Rather, this protein is probably involved in regulating the assembly of the actin cytoskeletion.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970020307
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  • 8
    Electronic Resource
    Electronic Resource
    Changes in the association of actin-binding proteins with the actin cytoskeleton during chemotactic stimulation of Dictyostelium discoideum (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 13 (1989), S. 57-63 
    Details
    ISSN: 0886-1544
    Keywords: ABP-120 ; myosin ; actin polymerization ; amoeboid chemotaxis ; cAMP ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Triton-insoluble cytoskeletons were isolated from Dictyostelium discoideum AX3 cells prior to and following stimulation with 2′deoxy cyclic adenosine monophos-phate (cAMP). Temporal changes in the content of actin and a 120,000 dalton actin-binding protein (ABP-120) in cytoskeletons following stimulation were monitored. Both actin and ABP-120 were incorporated into the cytoskeleton at 30-40 seconds following stimulation, which is cotemporal with the onset of pseudopod extension during stimulation of amoebae with chemoattraciants. Changes in the content of total cytoskeletal protein and cytoskeletal myosin were determined under the same experimental conditions as controls. These proteins exhibited different kinetics from those of cytoskeletal ABP-120 and actin following the addition of 2′deoxy cAMP. The authors concluded that the association of ABP-120 with the cytoskeleton is regulated during cAMP signalling. Furthermore, these results indicate that ABP-120 is involved in cross-linking newly assembled actin filaments into the cytoskeleton during chemoattractant-stimulated pseudopod extension.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970130107
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  • 9
    Electronic Resource
    Electronic Resource
    Isolation of an immunoreactive analogue of brain fodrin that is associated with the cell cortex of Dictyostelium amoebae (1988)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 11 (1988), S. 303-317 
    Details
    ISSN: 0886-1544
    Keywords: spectrin ; actin ; membrane skeleton ; cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have used a polyclonal affinity-purified antibody made against chicken brain fodrin (both 240 and 235 Kd subunits) as a probe to determine if a fodrinlike protein exists in amoebae of Dictyostelium discoideum. In Western blots of whole cells and the isolated cell cortex, polypeptides measuring 220 and 70 Kd are recognized by the fodrin antibodies. In situ localization by indirect immunofluorescence with antifodrin indicates that the immunoreactive polypeptides are cortical. The immunoreactive analogues copatch and cocap with concanavalin A. At the level of resolution of the electron microscope, immunocytochemistry with antifodrin and colloidal gold confirms that the immunoreactive analogues are cortical proteins associated with microfilaments on the cytoplasmic side of the plasma membrane. We have isolated and characterized the 220 Kd protein to determine if it is similar to fodrin and to investigate its relationship to the 70 Kd polypeptide. The 220 Kd protein can be extracted from the cortex in the absence of detergent and isolated by gel filtration and sucrose density gradient sedimentation. The 220 Kd is a rod-shaped protein 118 ± 17.8 nm (N = 37) in length. It has a sedimentation coefficient of 9.3 S and Stokes' radius of 13 nm and exists as a dimer of approximately 500,000 daltons (Mr). Isolated 220 Kd binds to actin filaments in vitro when assayed by rotary shadowing. Morphological criteria distinguish 220 Kd from Dictyostelium myosin II heavy chain (215 Kd) and the filaminlike protein at 240 Kd. The 70 Kd polypeptide appears to be a cleavage fragment of the 220 Kd, since it is found after prolonged storage when formerly only the 220 Kd was present. Furthermore, the 220 and 70 Kd polypeptides exhibit similar one-dimensional peptide maps when treated with TPCK trypsin. On the basis of its physical and immunoreactive characteristics, and location in the cell, the 220 Kd may be a fodrinlike protein.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970110408
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  • 10
    Electronic Resource
    Electronic Resource
    Preface (1988)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 10 (1988), S. 1-1 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970100102
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