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  • 1
    Electronic Resource
    Electronic Resource
    Incorporation and Turnover of Labeled Exogenous Tubulin in the Mitotic Spindles of HeLa Cells and Chaetopterus Oocytes (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 466 (1986), 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.1749-6632.1986.tb38450.x
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  • 2
    Electronic Resource
    Electronic Resource
    Book reviews (1982)
    Springer
    Origins of life and evolution of the biospheres 12 (1982), S. 119-121 
    Details
    ISSN: 1573-0875
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00926916
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Meeting report: Conference on cellular evolution (1982)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 83-89 
    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.970020107
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  • 4
    Electronic Resource
    Electronic Resource
    Incorporation and turnover of labeled exogenous tubulin in the mitotic spindles of Chaetopterus oocytes and HeLa cells (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 114-121 
    Details
    ISSN: 0886-1544
    Keywords: mitosis ; microtubules ; tubulin incorporation ; assembly polarity ; Chaetopterus ; HeLa cells ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The incorporation of tubulin into mitotic spindles in situ was studied by incubating permeabilized mitotic cells in solutions containing [3H]GTP-labeled or dichlorotriazinylamino fluorescein (DTAF)-labeled tubulin. Metaphase HeLa cells or spindle-containing “minicells” from Chaetopterus oocytes were lysed in a microtubule-assembly buffer plus 0.5% Nonidet P-40, 1 mg/ml 120,000g supernatant mammalian brain tubulin, and [3H]GTP. After different periods of incubation, mitotic spindles were isolated in 2 M-glycerol-containing assembly buffer and separated from unbound counts by centrifugation through a 4 M-glycerol cushion; 3H counts per mg protein increase linearly for 8-12 min and then reach a plateau or steady state in both Chaetopterus oocytes and HeLa cells. Addition of 4 mM CaCl2 blocks or reverses incorporation. Little or no [3H]GTP is incorporated if exogenous tubulin or lysed cells are omitted from the assembly mixture.To measure the loss rate of [3H]GTP-tubulin from mitotic spindles, cells were incubated in tubulin plus [3H]GTP for 30 min, and a 20-fold excess of cold GTP (2 mM) was added. Samples were removed after incubation for different periods, and spindles were isolated as described above and counted for 3H content. [3H]GTP is lost from spindles at a rate of about 16%/min until a new steady state is reached in about 8 min. These results are consistent with an incorporation and turnover of [3H]GTP-tubulin in spindle microtubules of these lysed-cell models.The location of this newly incorporated tubulin in the spindle was investigated by incorporating fluorescent DTAF-tubulin into mitotic spindles of these lysed cell types. A short pulse (2-5 min) appears to label microtubules (MTs) near metaphase chromosomes and longer exposures label the entire spindle.The rates of incorporation and turnover that we see by [3H]GTP and fluorescent tubulin incorporation in situ are faster than those observed with brain MTs at steady state in vitro but are in the range of the rates of spindle fiber formation in prophase, and spindle MT reassembly after cooling.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060208
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  • 5
    Electronic Resource
    Electronic Resource
    Microtubule-dependent transport of secretory granules during stalk secretion in a peritrich ciliate (1982)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 47-71 
    Details
    ISSN: 0886-1544
    Keywords: microtubules ; transport ; secretion ; peritrich ciliate ; directional turnover ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The role of microtubules in secretory granule translocation was studied during stalk secretion in the peritrich ciliate, Zoothamnium arbuscula. In each cell, the release of stalk-forming secretory materials is restricted to a specialized region of the cytoplasm, the scopula. Many of the membrane-bound secretory granules that dominate the scopular cytoplasm appear to be aligned along cortical microtubules that converge on the scopular surface. This arrangement is consistent with the hypothesis that microtubules transport granules relative to the sites of exocytosis. To establish the role of microtubules in stalk secretion, telotrochs were exposed to agents with different disruptive effects on microtubule function. Exocytosis itself is not prevented by these drugs, and granules positioned for secretion prior to treatment are released. Maytansine and isopropyl-n-phenyl carbamate (IPC) completely inhibit stalk elongation. In maytansine-treated cells, microtubules are absent from the scopular cytoplasm, and granules are absent from the scopular surface. Microtubules are present in IPC-treated cells, but the granules are misdirected to the cytoplasm lateral to the scopula where no secretory sites exist. Even though the rate of stalk secretion is decreased by deuterium oxide (D2O), a control length stalk is eventually produced. In D2O-treated cells microtubules are present and in their normal orientation. The inhibition of secretion when microtubules are absent (maytansine) or misdirected (IPC) and the retardation of secretion when microtubule turnover is reduced (D2O) supports a mechanism of granule transport based on the directional turnover of microtubule subunits.
    Additional Material: 17 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970020105
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  • 6
    Electronic Resource
    Electronic Resource
    Ca+2-accumulating components in developing skeletal muscle (1977)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 151 (1977), S. 213-237 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: This ultrastructural study on the localization of Ca+2 in developing skeletal muscle indicates that the formation of calcium-accumulating components begins during embryonic development. Both oxalate and pyroantimonate techniques are used to localize Ca+2 in distinct cellular components of chick pectoral and sartorius muscles. Two major sites for Ca+2 accumulation are present in ultrathin sections of embryonic and post-embryonic muscles: the terminal cisternae of the sarcoplasmic reticulum and specific lines in the I-bands. Calcium oxalate-accumulating vesicles are present in the smallest recognizable myotubes at the twelfth day of incubation, but calcium-accumulating components are not seen at myofibrillar I-band sites until the fourteenth to seventeenth days of incubation. The fact that myofibrils first form and later in development accumulate a Ca+2-binding component suggests that this Ca+2-binding component is not necessary for the formation of myofibrils, but is added to myofibrils before hatching to serve a probable regulatory role in contraction.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051510204
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  • 7
    Electronic Resource
    Electronic Resource
    Backscattered electron imaging of immunogold-labeled and silver-enhanced microtubules in cultured mammalian cells (1987)
    New York, NY : Wiley-Blackwell
    Journal of Electron Microscopy Technique 5 (1987), S. 263-273 
    Details
    ISSN: 0741-0581
    Keywords: Immunocytochemistry ; Cell culture ; Cytoskeleton ; Scanning electron microscopy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: This technique permits the visualization of microtubules in situ by employing silver-enhanced immunogold labeling and backscattered electron imagery. For best results, monolayer cultures of PtK2 cells are lysed with Triton X-100 in a microtubule stabilizing buffer, fixed with 1% glutaraldehyde, reduced with NaBH4, incubated with monoclonal antitubulin and 5-nm gold-labeled anti-IgG, silver enhanced, freeze dried, lightly coated with aluminum, and examined in an SEM equipped with a backscattered electron detector. A high contrast view of the entire microtubule complex of each cell is obtained. Microtubules in freeze-dried preparations have relatively smooth surfaces, whereas those in critical point dried preparations are more irregular or beaded. At high magnifications, an unstained inner core of each microtubule can be resolved. Backscattered electron imaging appears to be a promising technique for localizing cytoskeletal proteins and other intracellular antigens that can be labeled with immunogold and enhanced with silver.
    Additional Material: 20 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1060050306
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