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  • 1
    ISSN: 1432-0533
    Keywords: Myoglobin ; Messenger RNA ; In situ hybridization ; Duchenne muscular dystrophy ; Amyotophic lateral sclerosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The intracellular localization of myoglobin(Mb) mRNA in the skeletal muscles of normal subjects and patients with Duchenne muscular dystrophy(DMD) or amyotrophic lateral sclerosis(ALS) was examined by in situ hybridization using a biotin-labeled cDNA probe. In cross sections of normal muscles, Mb mRNA signals were demonstrated to be diffusely distributed as granular reaction products throughout the sarcoplasm, and in longitudinal sections the products were observed preferentially on the A-band. In DMD or ALS muscles, the distribution of granular mRNA signals showed some similarities with that in normal muscles, although degenerated fibers revealed a heterogenous distribution of the signals. In DMD muscles, the optical density(OD) of stained signal was higher in non-atrophic fibers and lower in atrophic fibers than in normal muscles. In ALS muscles, the OD was lower than in normal muscles. These results suggest that Mb mRNA is distributed preferentially on the A-band of the muscle fibers, and that in diseased muscle fibers Mb synthesis is affected by pathological changes.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0533
    Keywords: Key wordsα-Sarcoglycan ; γ-Sarcoglycan ; Sarcoglycanopathy ; Immunohistochemistry ; Gene ; mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We investigated the expression of α-sarcoglycan, β-sarcoglycan, γ-sarcoglycan, and δ-sarcoglycan immunohistochemically in three patients with mutations of the α-sarcoglycan gene and a patient with a mutation of the γ-sarcoglycan gene. Although each of the four sarcoglycans were decreased on the muscle membranes of all the patients, different expression patterns for each were seen among the patients. In patients with mutations of the α-sarcoglycan gene, β-, γ- and δ-sarcoglycans were relatively preserved as compared to greatly reduced α-sarcoglycan. However, the patient with a mutation of the γ-sarcoglycan gene showed marked reduction of γ-sarcoglycan as compared to partially preserved α- and β-sarcoglycans, and well-preserved δ-sarcoglycan. These results suggest that each sarcoglycan component in sarcoglycanopathy does not decrease in the same manner, and that mutations of the sarcoglycan gene can be predicted, at least in part, by means of sensitive immunohistochemistry for each sarcoglycan.
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  • 3
    ISSN: 1432-1459
    Keywords: Duchenne muscular dystrophy ; Glucocorticoid treatment ; 3-Methylhistidine ; Proteolysis ; Contractile protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Seven patients, aged 10–17 years, with Duchenne muscular dystrophy were treated orally with prednisolone (PSL) at a dose of 0.8–1.0 mg/kg per day for 8 weeks. During the treatment their muscle strength, serum creatine kinase (CK) activity, serum levels of myoglobin (Mb), and urinary excretion of 3-methyl-histidine (3-MeH) and glycine (Gly) were measured serially. In all the patients, the motor function or muscle strength improved, and the serum CK activity and Mb level decreased during PSL treatment. Urinary excretion of 3-MeH, a unique constituent of muscle contractile proteins, decreased to 51–63% of the baseline value in weeks 6–9 after the start of PSL administration, and returned to the baseline level in week 12. The ratios of 3-MeH to creatinine and to Gly also decreased during the treatment. Urinary excretion of Gly, which is ubiquitous in all tissues including muscle, did not decrease during the treatment. These findings suggest that PSL inhibits proteolysis of muscle contractile protein.
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  • 4
    ISSN: 1435-232X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The isozyme patterns of leukocyte α-d-mannosidase in two sisters with mannosidosis, their parents and a patient with trisomy 19 were studied. The isozyme pattern of liver mannosidase of a normal subject was also studied. In the patients with mannosidosis the neutral isozyme (isozyme C or fraction C) was present, but the acidic isozymes (isozyme A and B or fraction A and B) were not detectable. In their parents the activity of the acidic isozymes was one-third of the normal activity. These findings suggest that the patients are homozygous and their parents are heterozygous in terms of deficiency of acidic isozymes. In the patients with trisomy 19, the activity of α-d-mannosidase was 4.9 times the upper limit of the normal value, while the levels of other lysozomal enzymes were normal. This increase was mainly due to increases of the A and B isozymes of mannosidase. This finding suggests that the gene encoding acidic isozymes, but not that encoding the neutral isozyme, is located on chromosome 19. The isozyme pattern of α-d-mannosidase differed in different tissues of normal subjects, and the difference in severity of lesions in different organs of the patients with mannosidosis could be explained by differences in the isozyme patterns of the enzyme in these organs.
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