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  • 1
    Electronic Resource
    Electronic Resource
    Increased dopamine and its metabolites in SH-SY5Y neuroblastoma cells that express tyrosinase (2003)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 87 (2003), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Oxidized metabolites of dopamine, known as dopamine quinone derivatives, are thought to play a pivotal role in the degeneration of dopaminergic neurons. Although such quinone derivatives are usually produced via the autoxidation of catecholamines, tyrosinase, which is a key enzyme in melanin biosynthesis via the production of DOPA and subsequent molecules, may potentially accelerate the induction of catecholamine quinone derivatives by its oxidase activity. In the present study, we developed neuronal cell lines in which the expression of human tyrosinase was inducible. Overexpression of tyrosinase in cultured cell lines resulted in (i) increased intracellular dopamine content; (ii) induction of oxidase activity not only for DOPA but also for dopamine; (iii) formation of melanin pigments in cell soma; and (iv) increased intracellular reactive oxygen species. Interestingly, the expressed tyrosinase protein was initially distributed in the entire cytoplasm and then accumulated to form catecholamine-positive granular structures by 3 days after the induction. The granular structures consisted of numerous rounded, dark bodies of melanin pigments and were largely coincident with the distribution of lysosomes. This cellular model that exhibits increased dopamine production will provide a useful tool for detailed analyses of the potentially noxious effects of oxidized catecholamine metabolites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2003.02008.x
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  • 2
    Electronic Resource
    Electronic Resource
    Alteration in calcium channel properties is responsible for the neurotoxic action of a familial frontotemporal dementia tau mutation (2003)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 87 (2003), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Tau, a microtubule binding protein, is not only a major component of neurofibrillary tangles in Alzheimer's disease, but also a causative gene for hereditary frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). We show here that an FTDP-17 tau mutation (V337M) in SH-SY5Y cells reduces microtubule polymerization, increases voltage-dependent calcium current (ICa) density, and decreases ICa rundown. The reduced rundown of ICa by V337M was significantly inhibited by nifedipine (L-type Ca channel blocker), whereas ω-conotoxin GVIA (N-type Ca channel blocker) showed smaller effects, indicating that tau mutations affect L-type calcium channel activity. The depolarization-induced increase in intracellular calcium was also significantly augmented by the V337M tau mutation. Treatment with a microtubule polymerizing agent (taxol), an adenylyl cyclase inhibitor, or a protein kinase A (PKA) inhibitor, counteracted the effects of mutant tau on ICa. Taxol also attenuated the Ca2+ response to depolarization in cells expressing mutant tau. Apoptosis in SH-SY5Y cells induced by serum deprivation was exacerbated by the V337M mutation, and nifedipine, taxol, and a PKA inhibitor significantly protected cells against apoptosis. Our results indicate that a tau mutation which decreases its microtubule-binding ability augments calcium influx by depolymerizing microtubules and activating adenylyl cyclase and PKA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2003.02020.x
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  • 3
    Electronic Resource
    Electronic Resource
    P2 Protein in Oligodendrocytes and Myelin of the Rabbit Central Nervous System (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 40 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: P2 protein, a myelin-specific protein, was detected immunocyto-chemically and biochemically in rabbit central nervous system (CNS) myelin. P2 protein was synthesized by rabbit oligodendrocytes and was present in varying amounts throughout the rabbit CNS. Comparison of P2 and myelin basic protein (MBP) stained sections revealed that P2 antiserum did not stain all myelin sheaths within the rabbit CNS. The proportion of myelin sheaths stained by P2 antiserum and the amount of P2 detected biochemically were greater in more caudal regions of the rabbit CNS. The highest concentration of P2 protein was found in rabbit spinal cord myelin, where P2 antiserum stained the majority of myelin sheaths. P2 protein was barely detectable biochemically in myelin isolated from frontal cortex, and in sections of frontal cortex only occasional myelin sheaths reacted with P2 antiserum. These results suggest that the regional variations in the amount of P2 protein are due to regional differences in the number of myelin sheaths that contain P2 protein. P2 protein was detected immunocytochemically and biochemically in rabbit sciatic nerve myelin. Immunocytochemically, P2 antiserum only stained a portion of the myelin sheaths present. The myelin sheaths not reacting with P2 antiserum had small diameters and represented less than 10% of the total myelinated fibers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb12651.x
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  • 4
    Electronic Resource
    Electronic Resource
    Mild ALS in Japan associated with novel SOD mutation (1993)
    [s.l.] : Nature Publishing Group
    Nature genetics 5 (1993), S. 323-324 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Sir — Amyotrophic lateral sclerosis (ALS) is a degenerative disorder characterized by selective damage to the neural system that mediates voluntary movement. Although the pathophysiologic process of ALS remains unknown, about 5–10% of cases are familial1–3 and recent work has ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng1293-323
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  • 5
    Electronic Resource
    Electronic Resource
    Microsatellite polymorphism in the human heme oxygenase-1 gene promoter and its application in association studies with Alzheimer and Parkinson disease (1997)
    Springer
    Human genetics 〈Berlin〉 100 (1997), S. 145-147 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Oxidative stress has been suggested to be involved in the pathogenesis of neurodegenerative diseases, such as Alzheimer disease (AD) and Parkinson disease (PD). Heme oxygenase-1 (HO-1), a key enzyme in heme catabolism, also functions as an antioxidant enzyme. Here, we show that a (GT)n repeat in the human HO-1 gene promoter region is highly polymorphic, although no particular alleles are associated with AD or PD. This newly identified genetic marker should allow us to study the possible involvement of HO-1 in certain human diseases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050480
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  • 6
    Electronic Resource
    Electronic Resource
    Leucocyte migration inhibition in myasthenia gravis (1976)
    Springer
    Journal of neurology 213 (1976), S. 33-40 
    Details
    ISSN: 1432-1459
    Keywords: Myasthenia gravis ; Leucocyte migration inhibition test ; Thymus antigens ; Cellular immunity ; Thymectomy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Mit der Methode des Leukocytenmigrations-Hemmtestes wurde die celluläre Überempfindlichkeit der Myastheniepatienten gegenüber Thymus, Muskel und peripherem Nervengewebe untersucht. In der Gruppe von Myastheniepatienten ohne Thymom ließ sich eine Hemmung der Leukocytenmigration durch Thymusantigene nachweisen. Nach Thymektomie normalisierten sich die entsprechenden Befunde. In der Gruppe der Myastheniepatienten mit Thymon jedoch wurde die Hemmung der Leukocytenmigration durch Thymusantigene auch nach der Thymektomie festgestellt. Es wurde keine nennenswerte Hemmung der Leukocytenmigration bei Verwendung von Muskel- bzw. peripherer Nervenantigene festgestellt. Die celluläre Immunität bei der Myasthenie und die Pathogenese der Krankheit werden diskutiert.
    Notes: Summary Cellular hypersensitivity in myasthenia gravis (MG) to the thymus, muscles and peripheral nerves was examined by the method of the leucocyte migration inhibition test. The group of MG patients without thymoma had inhibition of leucocyte migration by thymus antigens. After thymectomy, they had a normal value of leucocyte migration. However, in the group of MG patients with thymoma, the inhibition of leucocyte migration by thymus antigens was observed after thymectomy. No significant inhibition of leucocyte migration was observed using muscle and peripheral nerve antigens. Cellular immunity in myasthenia gravis and the pathogenesis of the disease was discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00316337
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  • 7
    Electronic Resource
    Electronic Resource
    Optic-spinal form of multiple sclerosis and anti-thyroid autoantibodies (1999)
    Springer
    Journal of neurology 246 (1999), S. 449-453 
    Details
    ISSN: 1432-1459
    Keywords: Key words Multiple sclerosis ; Optic-spinal form ; Anti-thyroid ; autoantibodies ; Chronic ; autoimmune thyroiditis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The optic-spinal form of multiple sclerosis (OSMS), characterized by recurrent involvement of optic nerve and spinal cord with rare brain magnetic resonance imaging lesions, is relatively common among Asians. While individual cases of OSMS with anti-thyroid autoantibodies (ATABs) have been reported, the frequency of ATAbs in OSMS and classical multiple sclerosis has not been studied. We studied serum ATAbs and anti-nuclear antibodies (ANA) in 46 Japanese patients with multiple sclerosis: 14 with OSMS, and 32 with non-OSMS. Six patients were positive for ATAbs: five women with OSMS and one man with non-OSMS. The frequency of ATAbs in OSMS (5/14) was significantly higher than that in non-OSMS (1/32; P = 0.007), but the frequency of ANA did not differ between OSMS (3/14) and non-OSMS (6/32; P = 0.99). There may be a pathogenetic link between anti-thyroid autoimmunity and a subgroup of OSMS in Japanese.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004150050381
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  • 8
    Electronic Resource
    Electronic Resource
    Immunocytochemical method to identify basic protein in myelin-forming oligodendrocytes of newborn rat C.N.S. (1978)
    Springer
    Journal of neurocytology 7 (1978), S. 251-263 
    Details
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary An immunocytochemical method for detecting myelin basic protein in oligodendrocytes and myelin of newborn rat C.N.S. is described. C.N.S. tissue is perfused and fixed in HgCl2-formaldehyde and 20 μm Vibratome sections are treated with antibodies to myelin basic protein using the peroxidase-antiperoxidase method. Oligodendrocytes in the newborn rat are intensely stained by antiserum to basic protein and multiple stained processes extend from the perikaryon to myelin sheaths. With this procedure it is possible to demonstrate the geometric relationships between a single oligodendrocyte and multiple myelin sheaths. Stained oligodendrocytes and myelin are present in newborn cervical spinal cord, medulla oblongata, pons and midbrain. By 25 days of age, staining in oligodendrocytes is less intense than in newborn rats and differences in amount of staining can be detected in areas that are myelinating at different rates. With anticerebroside serum, cerebroside, of newborn and developing rat C.N.S. tissue is localized only in myelin. In the developing P.N.S., myelin basic protein is localized in Schwann cell cytoplasm and myelin sheaths of the trigeminal ganglion. Cerebroside is found only in myelin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01217922
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  • 9
    Electronic Resource
    Electronic Resource
    Molecular Analyses of the Cu/Zn Superoxide Dismutase Gene in Patients with Familial Amyotrophic Lateral Sclerosis (ALS) in Japan (1998)
    Springer
    Cellular and molecular neurobiology 18 (1998), S. 639-647 
    Details
    ISSN: 1573-6830
    Keywords: amyotrophic lateral sclerosis ; Cu/Zn superoxide dismutase ; familial ; gene ; mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. Amyotrophic lateral sclerosis (ALS) is a degenerative disorder characterized by selective damage to the neural system that mediates voluntary movement. Although the pathophysiologic process of ALS remains unknown, about 5 to 10% of cases are familial. According to genetic linkage studies, the familial ALS (FALS) gene has been mapped on chromosome 21 in some families and recent work identified some different missense mutations in the Cu/Zn superoxide dismutase gene in FALS families. 2. We recently identified five mutations in six FALS families. The mutations identified in our FALS families are H46R, L84V, I104F, S134N, and V148I. The H46R mutation that locates in the active site of Cu/Zn SOD gene is associated with two Japanese families with very slow progression of ALS. On the other hand, the L84V mutation associated with a rapidly progressive loss of motor function with predominant lower motor neuron manifestations. 3. In the family with the V148I, the phenotype of the patient varied very much among the affected members. One case had weakness of the lower extremities at first and died without bulbar paresis. The second case first noticed wasting of the upper limbs with bulbar symptoms, but the third had weakness of upper extremities without developing dysarthria nor dysphagia until death. These mutations account for 50% of all FALS families screened, although Cu/Zn SOD gene mutations are responsible for less than about 13–21% in the Western population. 4. Our results indicate that the progression of disease with mutations of Cu/Zn SOD is well correlated with each mutation. The exact mechanism by which the abnormal Cu/Zn SOD molecules selectively affect the function of motor neurons is still unknown.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020681802277
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