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  • 1
    ISSN: 1432-0533
    Keywords: Key words Monoamine oxidase-B ; Senescence-accelerated mouse (SAM) ; Monoamine ; oxidase-B-positive granular structure ; Periodic ; acid-Schiff-positive granular structure ; Aging
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We examined the histochemical localization of monoamine oxidase in the hippocampus of young and old senescence-accelerated mouse (SAM). We found a monoamine oxidase-B-positive granular structure (MGS) in the hippocampus of old SAMP8, an accelerated senescence-prone line of SAM. The MGS was a round-shaped granular structure of 0.5 to 5 μm diameter and usually formed a cluster, the largest diameter of which ranged from 50 to 150 μm. No MGS were found in the hippocampus of young SAMP8 or of young SAMR1, an accelerated senescence resistant line of SAM, and only few, if any, were seen in old SAMR1. A monoamine oxidase-positive astrocyte was usually observed in the central area of each cluster of MGS. Furthermore, the MGS was in close anatomical relationship with monoamine oxidase-positive astrocytic processes. The enzyme inhibition experiments showed that monoamine oxidase activities localized in the MGS and astrocytes were both predominantly of type B. These findings suggest MGS occurs at least partly in monoamine oxidase-B-positive astrocytes. Furthermore, the MGS was similar to a periodic acid-Schiff-positive granular structure, a polyglucosan body previously documented in the brains of old SAMP8 and some other aged mice strains including C57BL/6 and nude mice, in terms of their size, morphological appearances and topographical distribution in the hippocampus. Thus, the present results suggest that monoamine oxidase type B is a proteinaceous component of the periodic acid-Schiff-positive granular structure in aged mice brains, and might provide some clues for clarifying the mechanisms of age-related occurrence of periodic acid-Schiff-positive granular structures in mice brains.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0533
    Keywords: In situ hybridization ; Mitochondrial DNA ; Mitochondrial myopathy ; Ophthalmoplegia ; Cytochromec oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To determine whether a mitochondrial mRNA deficiency exists in mitochondrial myopathies, muscle biopsies from a patient with chronic progressive external ophthalmoplegia (CPEO) and a patient with mitochondrial myopathy, encephalopathy, lactic acidosis and stroke-like episodes (MELAS) were studied using in situ hybridization. Histochemistry and immunohistochemistry were performed along with hybridization. Hybridization reactions were widely distributed over the sarcoplasm of all muscle fibers in the patient with MELAS. In the patient with CPEO, 80% of the fibers showed a marked decrease in density of autoradiographic grains. This marked decrease corresponded to the histochemical and immunohistochemical findings of a very weak staining of cytochromec oxidase (CCO). The isotope-labeled cDNA probe used in in situ hybridization in this study complements a part of subunit I of CCO and a part of subunit II of complex I in the mitochondrial gene. Our results suggest a defect in the mRNA in this CPEO patient.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0533
    Keywords: Menkes kinky hair syndrome ; Macular mottled mouse ; Mitochondrion ; Cytochromec oxidase ; Gold-labeling immuno-electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The macular mottled mouse is a murine model of the kinky hair syndrome, characterized by a deficiency in copper transport. Cytochromec oxidase (CCO), a respiratory enzyme, is located in the inner mitochondrial membrane and consists of seven subunits, along with copper and iron. Biochemical and histochemical findings indicated that CCO activity was decreased in the cerebellum of the macular mottled mice but not in that of the controls. Immunocytochemical analysis, using anti-CCO and anti-complex III rabbit sera, revealed that CCO in the macular mottled mice was stained more weakly than that in the controls. Immuno-electron microscopic examination of CCO and complex III, using a method of gold labeling, was also performed. In the control mice, a high concentration of gold particles present over CCO and complex III could be seen in the inner mitochondrial membrane. The number of CCO-labeled gold particles was remarkably less, however, in the macular mottled mice, while no significant difference was found in the labeling of complex III between the two groups. It may concluded that the very low CCO enzyme content in the macular mottled mouse results not only from a copper transport disorder but also from a CCO protein synthesis disorder which impairs the localization of CCO protein in the cerebellum.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1615-6102
    Keywords: Aging ; Chlamydomonas ; Plastid nucleoid condensation ; Mutant ; Plastid nucleoids ; O2 evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary To study the mechanism of condensation of dispersed plastid (pt) nucleoids into a single pt nucleoid with aging of the cells ofChlamydomonas reinhardtii, two mutants, designated cond-1 and cond-2, were isolated. A plastid of a wild type cell, 6.5 μm in diameter, contained ten dispersed spherical pt nucleoids within one week of culture on an agar plate. At about one week of culture, the cell number was saturated and pt nucleoids began to associate with each other, condensing into a single pt nucleoid at three weeks of culture. In contrast, cond-1 and cond-2 cells, which had about 20 and 45 pt nucleoids and whose cell diameters were 7.8 and 9.5 μm at one week of culture respectively, still had about 10 and 20 pt nucleoids at even 7 weeks of culture. Doubling times of the three cell types were similar. From genetic analysis, each of the two mutants had one gene mutation. The two mutations are probably linked. The measurement of O2 evolution showed that the two mutations did not affect the photosynthetic system. Lipid contents of the two mutant cells were clearly higher than that of wild type cells. The role of a higher number of pt nucleoids is probably to increase the activity of lipid and/or membrane synthesis for lipid storage.
    Type of Medium: Electronic Resource
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