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  • 1
    Electronic Resource
    Electronic Resource
    Regulation of sperm flagellar movement by protein phosphorylation and dephosphorylation (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 83-88 
    Details
    ISSN: 0886-1544
    Keywords: sea urchin ; spermatozoa ; Triton model ; protein kinase ; cyclic AMP ; phosphoprotein phosphatase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Flagellar motility of Triton models of sea urchin spermatozoa was reactivated by cyclic AMP-dependent protein kinase and a protein factor, termed motility activator, both of which were prepared from the detergent-extract of sea urchin spermatozoa. It was shown that phosphorylation of the motility activator by the protein kinase is necessary for the reactivation of flagellar motility [Ishiguro et al, J. Cell Biol. 92:777-782, 1982; Murofushi et al, in “Biological Functions of Microtubules and Related Structures,” Academic Press, 1982]. Reactivating factor was also detected in a KCI-extract of the axoneme fraction devoid of the detergent-extractable materials. The activity of this factor was also cyclic AMP- and protein kinase-dependent. Furthermore, when freshly prepared Triton models were treated with phosphoprotein phosphatase prepared from bovine cardiac muscle, the flagellar motility was drastically suppressed. This inhibition of the motility was partially recovered by the addition of cyclic AMP and protein kinase to the phosphatase-treated models.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060203
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  • 2
    Electronic Resource
    Electronic Resource
    Localization of mitotic-apparatus-associated 51-kD protein in unfertilized and fertilized sea urchin eggs (1988)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 10 (1988), S. 496-505 
    Details
    ISSN: 0886-1544
    Keywords: centrosome ; spindle matrix ; postembedding immunofluorescent labeling ; mitotic apparatus ; sea urchin eggs ; 51-kD protein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The 51-kD protein, a protein component of the mitotic apparatus in sea urchin eggs, is involved in the aster-forming activity previously shown in vitro [Toriyama et al., 1988]. Postembedding immunofluorescent labelings of eggs from fertilization through first cleavage showed that the 51-kD protein is localized in sperm asters, centrosomal regions, spindles, basal regions of astral microtubules, and regions surrounding daughter nuclei at telophase in situ. Immunofluorescence and immunoblot analyses detected the 51-kD protein uniformly in unfertilized eggs, but not in spermatozoa. When unfertilized eggs were treated with taxol, the 51-kD protein was shown to be associated with taxol-induced cytasters. Immunoblot analysis revealed that similar protein species are present in the mitotic apparatus of other species of sea urchin. It was suggested that the 51-kD protein may be involved in microtubule nucleation and microtubule matrix in sea urchin eggs in vivo.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970100406
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  • 3
    Electronic Resource
    Electronic Resource
    51-kd protein, a component of microtubule-organizing granules in the mitotic apparatus involved in aster formation in vitro (1988)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 9 (1988), S. 117-128 
    Details
    ISSN: 0886-1544
    Keywords: centrosome ; aster-forming activity ; tubulin polymerization ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Mitotic apparatuses (MAs) isolated from sea urchin metaphase eggs were chilled on ice to depolymerize microtubules, homogenized, and incubated with tubulin. This caused formation of many small asters with microtubules focusing on granules which were probably fragments of the centrosome. The aster-forming protein components of the granules in the homogenized MAs were solubilized in 0.5 M KCl containing 50% glycerol. After dialysis against low-ionic-strength buffer solution, proteins congregated to form granular assembly capable of initiating aster formation. Phosphocellulose column chromatography enabled the separation of the aster-forming protein fraction which contained a 51,000 molecular weight protein (51-kd protein) as a major component. The protein fraction possessing the aster-forming activity was also prepared from methaphase whole egg homogenate, and the elution profile of the 51-kd protein on phosphocellulose column also coincided with that of the aster-forming activity. The granular assembly reconstituted from the phosphocellulose fraction formed asters whose microtubules show the same growth rate and length distribution as those of asters reconstructed from the granules in the homogenized MAs. Anti-51-kd protein antibody that was raised in rabbit and affinity-purified stained the center of asters which were reconstructed either from the granules in the homogenized MAs or from the granular assembly reconstituted from the phosphocellulose fraction. These results suggest that the 51-kd protein is a component in the aster-forming activity of the centrosomal component in vitro.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970090204
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  • 4
    Electronic Resource
    Electronic Resource
    Formation of miniasters in the cytoplasm of hexyleneglycol-treated sea urchin eggs (1990)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 15 (1990), S. 23-33 
    Details
    ISSN: 0886-1544
    Keywords: centrosome ; cytaster ; MTOG ; pericentriolar material ; 51 kD protein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Miniasters formed in mitotic sea urchin egg after treatment with 5% hexylene-glycol were investigated with the combined techniques of indirect immunofluo-rescence using anti-tubulin and anti-51 kD protein antibodies and electron microscopy.The formation of miniasters was dependent on the mitotic cycle. In the cytoplasm of eggs treated with hexyleneglycol at early prometaphase, a small number of microtubule fragments was observed, whereas in those treated at pro-metaphase, many miniasters and microtubule fragments were seen. When treated at metaphase, we found a great number of miniasters: 250-350 in one egg. In contrast, no miniasters were seen in eggs treated at anaphase, although many long microtubules that spread throughout the cytoplasm were observed. In the eggs treated at telophase, we scarcely noticed microtubule structures in the cytoplasm. In the center of miniasters, granules were found, showing the same size and electron density as those of the microtubule-organizing granules (MTOGs). Furthermore, the 51 kD protein, a component of the centrosome and mitotic spindle, was observed to be localized in the region of miniasters.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970150105
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  • 5
    Electronic Resource
    Electronic Resource
    The molecular structure of adrenal medulla kinesin (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 12 (1989), S. 264-272 
    Details
    ISSN: 0886-1544
    Keywords: rotary shadowing ; microtubules ; cytoplasmic movement ; conformation change ; two-headed molecule ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The molecular structure of bovine adrenal kinesin was studied by electron microscopy using the low-angle rotary shadowing technique. Adrenal kinesin exhibited either a folded or an extended configuration; the ratio of the two is dependent on the salt concentration. Almost all adrenal kinesin molecules were folded in a low-ionic solution, and the ratio of extended molecules increased to 40-50% in a solution containing 1 M ammonium acetate. Kinesin in the extended configuration displayed a rod-shaped structure with a mean length of about 80 nm. The morphologies of the ends were different; one end was composed of two globular particles, similar to the two-headed structure of myosin, while the other end had a more ill-defined structure, appearing either as a globular particle, an aggregate of two to four small granules, or a frayed, fan-like structure. The folded kinesin molecule possessed a hinge region in the middle of the rod, at about 32 nm from the neck of the two heads. In our preparations, the majority of adrenal kinesin molecules were folded at physiological salt concentrations. Adrenal kinesin bound to microtubules in the presence of adenylyl imidodiphosphate (AMP-PNP) also displayed a folded morphology.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970120407
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  • 6
    Electronic Resource
    Electronic Resource
    Binding of kinesin to stress fibers in fibroblasts under condition of microtubule depolymerization (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 12 (1989), S. 71-77 
    Details
    ISSN: 0886-1544
    Keywords: microtubule ; colchicine ; cold-treatment ; kinesin localization ; EBTr cells ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The localization of kinesin in EBTr (bovine embryonic trachea fibroblast) cells was studied by indirect immunofluorescence microscopy using an affinity-purified antibody against bovine adrenal kinesin.It has already been shown that in interphase cells a part of kinesin is located on microtubules and the rest diffusely distributed throughout the cytoplasm [Murofushi et al., 1988]. When microtubules were depolymerized with cold or colchicine treatment, antikinesin antibody-stained fibrous components distinct from microtubules. These fibrous structures were considered to be stress fibers because they were stained with rhodamine-phalloidin and because the fibrous staining with antikinesin antibody was completely lost by treating the cells with cytochalasin D along with colchicine. When cold-treated cells in which a major part of kinesin had been localized on stress fibers were incubated at 37°C, kinesin reappeared on reconstituted microtubules. These observations strongly suggest that kinesin has affinity not only to microtubules but also to stress fibers in culture cells.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970120202
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  • 7
    Electronic Resource
    Electronic Resource
    Localization of sea urchin egg cytoplasmic dynein in mitotic apparatus studied by using a monoclonal antibody against sea urchin sperm flagellar 21S dynein (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 7 (1987), S. 97-109 
    Details
    ISSN: 0886-1544
    Keywords: dynein ; mitosis ; chromosome movement ; immnunofluorescence observation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A monoclonal antibody against sea urchin (Hemicentrotus pulcherrimus) sperm flagellar 21S dynein was characterized and sued to identify and localized cytoplasmic dynein of sea urchin eggs by the methods of immunoblotting and indirect immunofluorescence microscopy. D57, the monoclonal antibody used in this study, was directed to the Aβ polypeptide of 21S dynein. D57 stained sperm flagella specifically but did not inhibit Mg-ATPase activity of 21S dynein, its recombination ability with NaCl-extracted axonemes, or the movement of demembranated sperm. D57 cross-reacted with sea urchin egg cytoplasmic dynein. High molecular weight cytoplasmic dynein polypeptide which had the same electrophoretic mobility s flagellar dynein. A chains was the only polypeptide that reacted with D57 in the crude extract from unfertilized sea urchin eggs. Indirect immunofluorescence observations showed that the mitotic apparatus was stained most intensely in the frozen sections and lysed eggs. In the mitotic apparatus isolated at metaphase, the half spindles were stained more strongly than the astral regions. The regions near chromosomes in the half spindle appeared to be stained particularly. Staining of the interzone was also observed in the mitotic spindle isolated at anaphase. Comparison of the staining patterns for cytoplasmic dynein with that for tubulin suggested that cytoplasmic dynein was localized where microtubules were densely organized, but its distribution may not necessarily be identical with that of microtubules.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970070202
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