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  • 2000-2004  (2)
  • Key words Quantitative idiogram  (1)
  • Ultrastructural ¶localization  (1)
  • 1
    ISSN: 1432-0533
    Keywords: Key words Aciculin ; Dystrophin ; Binding site ; Normal and dystrophic muscles ; Ultrastructural ¶localization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Aciculin is a novel adherens junction antigen extracted from human uterine smooth muscle that is reported to associate biochemically with dystrophin. We attempted to determine (i) the immunostainability of anti-aciculin antibody for the 6 histochemically normal human muscles and seven muscles from boys with Duchenne muscular dystrophy(DMD) and 11 disease control muscles, (ii) the ultrastructural localization of aciculin in normal skeletal myofibers, (iii) aciculin’s spacial relationship with dystrophin and β-spectrin, and (iv) if the aciculin is ultrastructurally colocalized with dystrophin, the distance from the aciculin epitope to the epitope of the dystrophin N- or C-terminal domain. For this, rabbit anti-aciculin antibody was generated against the synthetic peptide of aciculin fragment D [4]. Immunohistochemical staining showed that the immunostainability of DMD muscles for anti-aciculin antibody was markedly decreased as compared with normal and disease control muscles. Single and double immunogold labeling electron microscopy of 6 histochemically normal human quadriceps femoris muscles revealed that aciculin was present along the inner surface of muscle plasma membrane and that aciculin formed doublets more frequently with dystrophin (23.5 ± 1.8%; group mean ± SE) than with β-spectrin (12.8 ± 1.1%; P 〈 0.01 two tailed t test). Rabbit anti-aciculin antibody frequently formed doublets with monoclonal antibodies against the N- or C-terminal domain of dystrophin at the muscle cell surface. These results suggest that aciculin is associated with dystrophin and may interact with both the N- and C-terminal domains of dystrophin.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2242
    Keywords: Key words Quantitative idiogram ; Prometaphase chromosome ; Image analysis ; Fluorescence in situ hybridization ; T subgenome progenitor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Using DAPI-stained prometaphase chromosomes, quantitative idiograms were constructed for the T subgenome of Nicotiana tabacum (2n = 4x = 48, SSTT) and two putative candidates for its T subgenome progenitor, Nicotiana otophora and Nicotiana tomentosiformis (both have 2n = 24, TT). The large chromosomes of the three karyotypes could be identified from the distributional pattern of the DAPI signal. Fluorescence in situ hybridization (FISH) with 5S rDNA gave not only good cytogenetical landmarks for identification of small chromosomes of the karyotypes but also phylogenetical information. In all three idiograms, 5S rDNA was localized in the proximal region of the long arm of a small submetacentric pair, but an additional 5S rDNA locus was detected terminally on the short arm of a small metacentric pair in N. otophora. The 18S rDNA locus detected here corresponded to satellite regions in all three karyotypes. Two satellited pairs in N. otophora and one satellited pair in N. tomentosiformis had single large subterminal DAPI blocks and two interstitial DAPI bands on their long arms, respectively. For the T subgenome component of N. tabacum, the single intense DAPI band was depicted on the center of the long arm of a satellited pair in the idiogram, although two interstitial bands were often detected on the long arm of the satellited pair in some spreads. Therefore, it was suggested that the T component of N. tabacum was more similar to that of N. tomentosiformis than N. otophora, especially in respect of the number and location of rDNA and the distributional patterns of DAPI signals.
    Type of Medium: Electronic Resource
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