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  • 1
    Electronic Resource
    Electronic Resource
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 83 (1998), S. 2228-2234 
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Structure, optical absorption and photoluminescence (PL) properties of SiOx films subjected to thermal annealing at 750–1100 °C are investigated. Si crystallites with a few nanometers in size are observed in the SiO1.3 and SiO1.65 films annealed at 1100 °C. Threshold energies in optical absorption of the Si nanocrystallites are higher than that for bulk Si, suggesting a contribution from quantum confinement effects. The PL spectrum shows a remarkable increase in intensity after annealing at temperatures above 1000 °C. This PL behavior is closely related to the formation of Si nanocrystallites by the annealing. The PL peak energy of the annealed films shifts to higher energy with decreasing crystallite size but does not follow the blueshift for the absorption threshold energy. These results suggest that a localized state contributes to the PL mechanism. The SiO1.8 film annealed at 1100 °C, which contains no Si crystallites, exhibits an intense PL similar to the annealed SiO1.3 and SiO1.65 films. It is implied that noncrystalline Si nanoparticles are formed in the SiO1.8 film under high-temperature annealing. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0009-8981
    Keywords: Cerebrospinal fluid ; Creatine kinase isoenzymes ; Creutzfeldt-Jakob disease ; Guanine nucleotide-binding protein ; Neuron-specific enolase ; S-100b protein
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-1440
    Keywords: Neuron-specific enolase level ; Cerebrospinal fluid ; Creutzfeldt-Jakob disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The measurement of neuron-specific enolase level in serum and cerebrospinal fluid was conducted time-sequentially in an autopsy confirmed patient with Creutzfeld-Jakob disease. The level was markedly high in the early stage of the disease at which time the brain CT showed no or minimal abnormalities, while falling into the normal range in the advanced stage. This is the first report of the elevated level of neuron-specific enolase in Creutzfeldt-Jakob disease.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 54 (1981), S. 189-197 
    ISSN: 1432-0533
    Keywords: Freeze fracture ; Membrane ; Muscular dystrophy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Freeze fracture analysis of intramembranous particle density in skeletal muscle plasma membrane from 7 patients with Duchenne muscular dystrophy (DMD), 5 patients with facioscapulohumeral muscular dystrophy (FSH) and 5 patients with myotonic dystrophy (MyD) were carried out. Marked deplction of intramembranous particles including orthogonal arrays were significantly decreased in FSH. No abnormalities were noted in MyD.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 72 (1986), S. 130-133 
    ISSN: 1432-0533
    Keywords: Freeze fracture ; Muscle plasma membrane ; Orthogonal array subunit particle ; Fukuyama type congenital muscular dystrophy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Freeze fracture analysis was carried out on the density of orthogonal array subunit particles in the plasma membrane of skeletal muscle of six patients with Fukuyama type congenital muscular dystrophy and seven control cases. The group mean density of orthogonal array subunit particles per one orthogonal array was significantly lower in the plasma membrane of Fukuyama patients. The results suggested the possible impairment of orthogonal array function in the plasma membrane of muscle fibers in congenital muscular dystrophy of the Fukuyama type.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-0533
    Keywords: Freeze fracture ; Muscle plasma membrane ; Cholesterol ; Fukuyama-type congenital muscular dystrophy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We used digitonin in freeze-fracture analysis of the muscle plasma membrane cholesterol content in six patients with Fukuyama-type congenital muscular dystrophy and six control children. A significantly greater proportion of surface area was taken up by digitonin-cholesterol complexes in the patients (51.2%±4.7%) than in controls (31.9%±2.9%) (P〈0.01). Since membrane cholesterol has a dynamic regulatory function in affecting the activity of membrane-bound proteins, the increased cholesterol content in the patients suggests a functional abnormality of the muscle plasma membrane in this disease.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 76 (1988), S. 179-184 
    ISSN: 1432-0533
    Keywords: mdx mouse ; Freeze-fracture technique ; Muscle plasma membrane ; Orthogonal arrays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The structure of the muscle plasma membrane of extensor digitorum longus muscles of X chromosome-linked muscular dystrophy (mdx) mice was studied by freeze-fracture technique at several time points after birth. The common denominator of the abnormalities was the decreased density of orthogonal arrays throughout all the time points examined. The results demonstrated that the ultrastructural features of the muscle plasma membrane alterations in mdx mice were similar to those in Duchenne dystrophy.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-0533
    Keywords: mdx and control mice muscles ; Dystrophin ; Quick-freeze, deep-etch, rotary-shadow replica ; Muscle plasma membrane-associated cytoskeletons
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The Duchenne muscular dystrophy gene product “dystrophin” is a sarcolemma-associated cytoskeleton which is present just inside the sarcolemma. We investigated the ultrastructure and the relationship of this cytoskeleton to the muscle plasma membrane by immunoelectron microscopy and freeze-etch electron microscopy of liquid helium-frozen fresh muscles. The immunoelectron microscopy of the extensor digitorum longus muscles of six mdx mice and six control mice showed the location of anti-dystrophin antibody along the muscle plasma membrane undercoat of all the muscle samples from the control mice without any antibody reaction in the mdx mice muscles. Fresh extensor digitorum longus muscles of seven mdx and six control mice were quick-frozen in liquid helium in the rapid-freeze device. High-magnification electron microscopy of the deep-etch, rotary-shadow replicas of the frozen muscles showed the network formation and attachment of individual rod-shaped cytoskeletons of variable size to the cytoplasmic surface of the muscle plasma membrane in both mdx mice and control mice. The length of cytoskeletons attached to the muscle plasma membranes was measured and mean length±SE in mdx mice and control mice were 98±4 nm and 101±3 nm, respectively. Although these values were not statistically different (P〉0.1), the distribution frequency of 130–150 nm muscle plasma membrane-associated cytoskeletons was 7.9% in mdx mice versus 14.5% in control mice. Since the predicted length of dystrophin is 125–150 nm, the 130- to 150-nm plasma membrane-associated cytoskeletons of mdx control mice may include dystrophin.
    Type of Medium: Electronic Resource
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  • 9
    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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  • 10
    ISSN: 1432-0533
    Keywords: Key wordsα1-syntrophin ; Neuronal nitric oxide ; synthase ; Dystrophin ; Ultrastructural localization ; Skeletal muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We investigated the ultrastructural localization of α1-syntrophin and neuronal nitric oxide synthase (nNOS) in normal human skeletal myofibers and analyzed their relation to each other and to dystrophin using single and double immunogold-labeling electron microscopy. Single immunolabeling showed antibodies to α1-syntrophin and nNOS on the inner surface of the muscle plasma membrane, the sarcoplasmic side of plasma membrane invaginations, and the sarcoplasm near mitochondria of subsarcolemmal areas. The epitopes of α1-syntrophin and nNOS tended to be present in clusters. Double immunolabeling revealed that epitope combinations of α1-syntrophin-dystrophin, α1-syntrophin-nNOS, and nNOS-dystrophin occurred more frequently in doublet form than did other epitope combinations, such as α1-syntrophin-β-spectrin and nNOS-β-spectrin. These increased frequencies were noted both at the muscle plasma membrane undercoat and near mitochondria of subsarcolemmal areas. A significantly higher percentage of doublets comprised antibodies against α1-syntrophin and dystrophin (28.5 ± 1.5%, group mean ± SE) than those against α1-syntrophin and β-spectrin (9.2 ± 0.8%, P 〈 0.01). Furthermore, nNOS formed doublets significantly more frequently with dystrophin (25.2 ± 3.3%) and α1-syntrophin (26.0 ± 4.1%) than with β-spectrin (13.9 ± 2.3%; P 〈 0.05). These data support the association of dystrophin, α1-syntrophin, and nNOS at the inner surface of the muscle plasma membrane and near mitochondria of subsarcolemmal areas of normal human skeletal myofibers.
    Type of Medium: Electronic Resource
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