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  • 1
    Electronic Resource
    Electronic Resource
    Characterization of Two Distinct Monoclonal Antibodies to Paired Helical Filaments: Further Evidence for Fetal-Type Phosphorylation of the τ in Paired Helical Filaments (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 60 (1993), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Two monoclonal antibodies C5 and M4 raised against Sarkosyl-insoluble paired helical filaments (PHF) specifically labeled fetal τ, but hardly labeled normal adult τ. C5 immunoreactivity was eliminated by alkaline phosphatase treatment at 37°C, whereas M4 reactivity could be removed only by the treatment at 67°C. Epitope analysis showed that C5 and M4 recognition sites are in residues 386–406 and 198–250, respectively, according to the numbering of the longest human τ isoform. Thus, the phosphorylation sites are located in the amino- and carboxyl-terminal portions of the microtubule-binding region. These two well-characterized monoclonals should be valuable in the identification of a protein kinase(s) that converts normal τ into PHF-τ.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1993.tb03491.x
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  • 2
    Electronic Resource
    Electronic Resource
    Subcellular Localization of Functionally Differentiated Microtubules in Squid Neurons: Regional Distribution of Microtubule-Associated Proteins and β-Tubulin Isotypes (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 51 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The subcellular localization of microtubule proteins in the neurons of squid (Doryteuthis bleekeri) was immu-nologically studied using monoclonal antibodies against the microtubule proteins. We found that (1) the squid neurons contained three kinds of high-molecular-weight microtubule-associated proteins [MAP A of ∼ 300 kilodaltons (kD), MAP B of 260 kD, and axolinin of 260 kD] and two kinds of β-tubulin isotypes (β1 and β2); (2) the cell body of the squid giant neuron contained MAP A, MAP B, and the two β-tubulin isotypes (β1 and β2); (3) axolinin and the β1 isotype were present exclusively in the peripheral axoplasm of the giant axon; and (4) a small amount of axolinin, MAP A, and the β1 isotype was found in the insoluble aspect of the central axoplasm, whereas the soluble aspect of the central axoplasm contained an abundant amount of MAP A along with the modified form of the β1 isotype. The regional difference of the distribution of the microtubule protein components may explain the differences in stability among axonai microtubules. Microtubules in the soluble aspect of the central axoplasm are sensitive to any treatment with colchicine, cold temperature, and high ionic strength but those both in the insoluble aspect of the central axoplasm and in the peripheral axoplasm are highly insensitive to the treatment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb01164.x
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  • 3
    Electronic Resource
    Electronic Resource
    Axolinin Localization in the Nervous Tissue of Squid Revealed by Monoclonal Antibodies Specific for Axolinin: Cellular and Subcellular Localization of Axolinin in the Squid Neuron (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 52 (1989), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Cellular and subcellular distributions of axolinin, the 260-kilodalton (kD) microtubule-associated glycoprotein originally purified from squid axons, in various squid tissues such as optical lobes, bundles of small nerve fibers (fin nerves), giant stellate ganglia, skin, muscle, liver, and gill, were immunologicaly studied using monoclonal antibodies specifically recognizing the polypeptide chain of axolinin. The following results were obtained: (1) Axolinin is confined to squid neurons and skin; (2) axolinin is localized in the axon whereas another 260-kD microtubule-associated protein, MAP B, is localized in the cell bodies; and (3) axolinin is localized mainly in the peripheral part of the axoplasm of the squid giant axon. The last result has confirmed our previous conclusion obtained using polyclonal antisera against axolinin, which contain antibodies recognizing not only axolinin-specific epitopes but also nonspecific epitopes. The physiological importance of the localization of axolinin in axons and the skin is discussed based on its possible relationship to excitability function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1989.tb10902.x
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  • 4
    Electronic Resource
    Electronic Resource
    Heterogeneity of microtubules in dividing sea urchin eggs revealed by immunofluorescence microscopy: Spindle microtubules are composed of tubulin isotypes different from those of astral microtubules (1990)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 16 (1990), S. 239-250 
    Details
    ISSN: 0886-1544
    Keywords: mitosis ; mitotic apparatus ; monoclonal antibodies ; sand dollar egg ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The heterogeneity of mitotic microtubules in dividing sea urchin eggs was investigated by indirect immunofluorescence using five anti-α-tubulin (YL1/2, DM1A, E3B8, D2D6, and 6-11B-1) and two anti-β-tubulin (E6B6 and DM1B) antibodies. These antibodies were divided into four classes in regard to the different immunofluorescent staining patterns: class I, which strongly stained both the spindle and aster (YL1/2, DM1A, E3B8 and E6B6); class II, which strongly stained the spindle but weakly stained the aster (D2D6); class III, which stained only the aster (DM1B); and class IV, which did not stain the mitotic apparatus (6-11B-1). These results suggest that tubulin isotypes are distributed differently in the sea urchin mitotic microtubules and that α-tubulin isotype(s) recognized by D2D6 is (are) localized mainly in spindle microtubules, whereas β-tubulin isotype(s) recognized by DM1B is (are) found only in astral microtubules.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970160404
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  • 5
    Electronic Resource
    Electronic Resource
    Different reactivity with monoclonal anti-tubulin antibodies between native and fixed mitotic microtubules in sea urchin eggs (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 29 (1994), S. 241-249 
    Details
    ISSN: 0886-1544
    Keywords: immunofluorescence ; microinjection ; mitotic apparatus ; monoclonal antibodies ; sand dollar egg ; tubulin isotypes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effect on fixation on the reactivities of mitotic microtubules with monoclonal anti-tubulin antibodies was investigated by the indirect immunofluorescence procedure. All of the seven antibodies used intensely stained mitotic microtubules in sea urchin eggs lysed and fixed with methanol at -20°C, whereas only two of them stained the stabilized microtubules in the lysed eggs before the fixation. The other five did not stain the mitotic microtubules even after microtubule components other than tubulin were removed by treating the lysed eggs with 0.4 M KCl solution containing taxol. These results exclude the possibility that the fixation affects proteins, which interact with microtubules including microtubule-associated proteins (MAPs) and interfere with the binding of monoclonal antibodies with tubulin, and strongly suggest that the fixation directly affects the three-dimensional conformation of tubulin Furthermore, microinjection of these antibodies indicated the results as follows [combining the results reported previously; Oka et al., 1990: Cell Struct. Funct. 15: 373-378]: The antibodies which stained mitotic microtubules stabilized in the lysed eggs induced disassembly of native mitotic microtubules in the living eggs, but those which did not stain the stabilized microtubules did not disassemble the native microtubules. From these results, it is suggested that the monoclonal antibodies which stain microtubules in the eggs lysed but not fixed are useful for microinjection experiments. © 1994 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970290307
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