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  • Electronic Resource  (11)
  • 1995-1999  (11)
  • 1965-1969
  • 1996  (11)
  • 1
    Electronic Resource
    Electronic Resource
    Photovoltage generation of Si/C60 heterojunction (1996)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 79 (1996), S. 2798-2800 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Photovoltage generation was observed for C60/Si heterojunction fabricated by the deposition of C60 thin film on Si substrate. Four types of Si substrates (two for p-type and two for n-type) were used. All junctions showed rectifying behaviors and photovoltage generation under illumination of Ar-ion laser. The highest value of the photovoltage was 0.40 V. From the saturated photovoltage values for four junctions, the Fermi level of C60 thin film was estimated to be located about 4.7 eV below the vacuum level. © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.361114
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  • 2
    Electronic Resource
    Electronic Resource
    Aminophlline is effective on acute exacerbations of asthma in adults–objective improvements in peak flow, spirogram, arterial blood gas measurements and lung sounds (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 26 (1996), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1996.tb01141.x
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  • 3
    Electronic Resource
    Electronic Resource
    NUCLEATION OF INTERGRANULAR CRACKS DURING HIGH TEMPERATURE LOW CYCLE FATIGUE OF SUS316 STAINLESS STEEL (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Fatigue & fracture of engineering materials & structures 19 (1996), S. 0 
    Details
    ISSN: 1460-2695
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Fundamental behaviour of intergranular cracking of SUS316 stainless steel which characterises the high temperature low cycle fatigue process has been studied with a special emphasis on the interaction between oxidation and a grain boundary sliding. Two types of specimens were prepared for fatigue experiment to extract a sole effect of surface oxidation on crack nucleation. One was heat-treated in air and the other was in vacuum so that the specimens had the same history of heat treatment except oxidation to the surface. Results of fatigue tests of these specimens well explain the relationship between oxidation and surface cracking as follows. The morphology of the oxidised surface of the specimen subjected to low-cycle fatigue at 700°C is quite different from that of the oxidised surface caused by simply holding at the same temperature in air for several hours with no applied stress. Localised oxidation along the grain boundary is a characteristic feature for the specimen fatigued at 700°C, while no localised oxidation was observed when the specimens were simply held at the same 700°C, i.e. with no fatigue loading. Accordingly, intergranular cracking in high temperature low cycle fatigue in air occurs when grain boundary sliding due to cyclic loading is accelerated by localised oxidation along the grain boundary.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1460-2695.1996.tb00994.x
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  • 4
    Electronic Resource
    Electronic Resource
    Role of dopaminergic neuronal system in dizocilpine-induced acetylcholine release in the rat brain (1996)
    Springer
    Journal of neural transmission 103 (1996), S. 651-660 
    Details
    ISSN: 1435-1463
    Keywords: Dizocilpine (MK-801) ; N-methyl-D-aspartate ; acetylcholine ; dopamine receptors ; in vivo microdialysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The effects of dopaminergic receptor antagonists on dizocilpineinduced increase in extracellular acetylcholine (ACh) levels in the rat parietal cortex were examined in freely-moving rats, using an in vivo brain microdialysis method. Dizocilpine (0.5 mg/kg) significantly increased extracellular ACh levels in the rat parietal cortex and hippocampus, but not in the striatum. Pretreatment with α-methyl-p-tyrosine methyl ester (αMpT) delayed the onset but prolonged the duration of the dizocilpine-induced increases in extracellular ACh levels. The dopamine D2 receptor antagonist, haloperidol, showed dual effects similarly to αMpT, while the dopamine D1 receptor antagonist, SCH23390, prolonged, but did not delay, the onset of the dizocilpine-induced increases in ACh levels. These results suggest that the dopaminergic system is involved in the dizocilpine-induced increase in the extracellular ACh level in the parietal cortex in two ways, through both dopamine D1 and D2 receptors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01271225
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  • 5
    Electronic Resource
    Electronic Resource
    Insulin-induced activation of phosphoinositide 3-kinase in Fao cells (1996)
    Springer
    Diabetologia 39 (1996), S. 515-522 
    Details
    ISSN: 1432-0428
    Keywords: Insulin ; insulin receptor substrate-1 ; phosphoinositide 3-kinase ; signal transduction ; phosphotyrosine ; enzyme activation ; conformational change ; Fao cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Phosphoinositide 3-kinase (PI3-kinase) plays a crucial role in insulin signal transduction. We studied the molecular mechanism of the insulin-induced activation of PI3-kinase in rat hepatoma Fao cells using an antibody against the 110-kDa catalytic subunit (p110) and two against the 85-kDa regulatory subunit (p85α). PI3-kinase activity increased 1.6-fold in anti-p85 immunoprecipitates after insulin stimulation, whereas it did not increase when cell lysates were first immunoprecipitated with anti-phosphotyrosine or anti-insulin receptor substrate-1 (IRS-1), then with anti-p85, suggesting that the PI3-kinase which associates with tyrosyl phosphoproteins including IRS-1 is responsible for the increase in kinase activity. The activated PI3-kinase molecules constituted 4–6% of the total PI3-kinase, and their specific activity was 11–14 times higher than that of the basal state. Anti-p110 recognized the catalytically active form of p110, and immunoprecipitated p110 only after exposure to insulin. Hence, the epitope of anti-p110, P200-C215, seems to be included in the portion of p110, the conformation of which is changed by insulin stimulation. We conclude that, in response to insulin stimulation, only a small fraction of p85 in the PI3-kinase pool associates with tyrosyl phosphoproteins including IRS-1, and that the specific activity of p110 is increased presumably through a conformational change including the P200-C215 region.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00403297
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  • 6
    Electronic Resource
    Electronic Resource
    Mouse islet cell lysis mediated by interleukin-1-induced Fas (1996)
    Springer
    Diabetologia 39 (1996), S. 1306-1312 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Islets of Langerhans ; Fas ; CD95 ; apoptosis ; interleukin-1 ; interferon-γ ; DNA cleavage.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary This study was conducted to investigate the possible involvement of Fas in β-cell death in insulitis of Type 1 (insulin-dependent) diabetes mellitus. Although primary cultured Balb/c mouse islet cells did not express Fas mRNA, 4–12 hours of treatment with 102-105 U/l of mouse interleukin-1 α (IL-1α) induced the expression of Fas mRNA. Surface Fas expression was detected by immunofluorescence flow cytometry using a non-cytolytic anti-Fas monoclonal antibody after 6 or 12 h of incubation with 103 U/l of IL-1α. Primary islet cells were resistant to an agonistic anti-Fas monoclonal antibody. However, 12 h pretreatment with IL-1α sensitized islet cells to its cytolytic effect. Significant cell death was observed 24 h after the addition of anti-Fas, and progressively increased until 72 h, when specific 51Cr release was 72 ± 6 %. Agarose gel electrophoresis of DNA extracted from cells exposed to IL-1α and agonistic anti-Fas showed internucleosomal DNA fragmentation, a hallmark of apoptotic cell death. Since the Fas antibody showed no cross-reactive activity of tumour necrosis factor (TNF), the cytotoxic effect was not mediated by TNF receptors. A protein synthesis inhibitor cycloheximide augmented Fas-mediated islet cell death. The Fas-mediated killing of islet cells was not l-arginine-dependent, or blocked by NG-monomethyl-l-arginine. β-TC1 cells also expressed Fas mRNA when exposed to IL-1α or IL-1α plus interferon-γ. These observations suggest that Fas-mediated apoptosis may be a mechanism of islet cell death in autoimmune insulitis. [Diabetologia (1996) 39: 1306–1312]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250050574
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  • 7
    Electronic Resource
    Electronic Resource
    Insulin-induced activation of phosphoinositide 3-kinase in Fao cells (1996)
    Springer
    Diabetologia 39 (1996), S. 515-522 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Insulin ; insulin receptor substrate-1 ; phosphoinositide 3-kinase ; signal transduction ; phosphotyrosine ; enzyme activation ; conformational change ; Fao cells.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Phosphoinositide 3-kinase (PI3-kinase) plays a crucial role in insulin signal transduction. We studied the molecular mechanism of the insulin-induced activation of PI3-kinase in rat hepatoma Fao cells using an antibody against the 110-kDa catalytic subunit (p110) and two against the 85-kDa regulatory subunit (p85α). PI3-kinase activity increased 1.6-fold in anti-p85 immunoprecipitates after insulin stimulation, whereas it did not increase when cell lysates were first immunoprecipitated with anti-phosphotyrosine or anti-insulin receptor substrate-1 (IRS-1), then with anti-p85, suggesting that the PI3-kinase which associates with tyrosyl phosphoproteins including IRS-1 is responsible for the increase in kinase activity. The activated PI3-kinase molecules constituted 4–6 % of the total PI3-kinase, and their specific activity was 11–14 times higher than that of the basal state. Anti-p110 recognized the catalytically active form of p110, and immunoprecipitated p110 only after exposure to insulin. Hence, the epitope of anti-p110, P200–C215, seems to be included in the portion of p110, the conformation of which is changed by insulin stimulation. We conclude that, in response to insulin stimulation, only a small fraction of p85 in the PI3-kinase pool associates with tyrosyl phosphoproteins including IRS-1, and that the specific activity of p110 is increased presumably through a conformational change including the P200–C215 region. [Diabetologia (1996) 39: 515–522]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00403297
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  • 8
    Electronic Resource
    Electronic Resource
    Cytochrome oxidase activity during acute focal ischaemia in rat brain (1996)
    Springer
    Acta neurochirurgica 138 (1996), S. 1126-1131 
    Details
    ISSN: 0942-0940
    Keywords: Cerebral ischaemia ; ischaemic brain damage ; cytochrome oxidase ; middle cerebral artery occlusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary An enzyme-histochemical technique was used to examine the changes in cytochrome oxidase activity during acute focal ischaemia in the rat. In the somatosensory cortex, the enzyme activity began to increase significantly (p 〈 0.01) 1 hour after middle cerebral artery occlusion (MCAO) and continued to increase up to 3 hours, during which ischaemic cell damage was not detected. In the striatum, the enzyme activity increased significantly (p 〈 0.01) 1 hour after MCAO in the absence of morphological evidence of ischaemic cell damage; a peak activity was reached at 2 hours, and began to decline 3 hours after MCAO when moderate ischaemic change was detected. In both cortical and subcortical areas, the enzyme activity tended to decrease from 4 hours after MCAO, and was reduced to a level similar to or below that of the non-ischaemic hemisphere 5 hours after MCAO, when severe ischaemic damage was demonstrated. The relation of this transient increase of cytochrome oxidase activity in the early stage of acute ischaemia and the hypermetabolism of neuronal cells during ischaemic insult was discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01412318
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  • 9
    Electronic Resource
    Electronic Resource
    The effects of activators of G-proteins, mastoparan and compound 48/80, on the G-protein/adenylate cyclase system in cultured melanophores of the black-moor goldfish, Carassius auratus (1996)
    Springer
    Journal of comparative physiology 166 (1996), S. 467-472 
    Details
    ISSN: 1432-136X
    Keywords: Key words Melanophore ; Mastoparan ; Compound 48/80 ; GTP-binding protein ; Goldfish ; Carassius auratus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  To investigate the functions of GTP-binding protein(s) in the melanosome-aggregating response in fish melanophores, the effects of activators of G-proteins, namely, mastoparan and compound 48/80, were examined in cultured melanophores of the balck-moor goldfish, Carassius auratus. Both mastoparan and compound 48/80 induced an approximately 40% increase in the GTP-hydrolyzing activity in the melanophore membranes compared to the basal level. In intact melanophores, these compounds inhibited the effect of 3-isobutyl-1-methylxanthine, which induced the accumulation of intracellular cAMP. Pretreatment of melanophores with pertussis toxin at 1 μg ⋅ ml-1 for 15 h attenuated the inhibitory effect of mastoparan on the accumulation of cAMP. However, pretreatment with the toxin only slightly attenuated the inhibitory effect of compound 48/80 on the accumulation of cAMP. In addition, compound 48/80 at 1 mg ⋅ ml-1 induced full aggregation of the melanosomes in melanophores, though mastoparan at 5 μmol ⋅ l-1 induced only 10–20% aggregation of melanophores. These results suggest that mastoparan and compound 48/80 can each activate the inhibitory G-protein in goldfish melanophores, which results in inhibition of adenylate cyclase activity. This signal-transduction pathway is involved in the aggregation of melanosomes in these cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003600050034
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  • 10
    Electronic Resource
    Electronic Resource
    The effects of activators of G-proteins, mastoparan and compound 48/80, on the G-protein/adenylate cyclase system in cultured melanophores of the black-moor goldfish,Carassius auratus (1996)
    Springer
    Journal of comparative physiology 166 (1996), S. 467-472 
    Details
    ISSN: 1432-136X
    Keywords: Melanophore ; Mastoparan ; Compound 48/80 ; GTP-binding protein ; Goldfish,Carassius auratus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract To investigate the functions of GTP-binding protein(s) in the melanosome-aggregating response in fish melanophores, the effects of activators of G-proteins, namely, mastoparan and compound 48/80, were examined in cultured melanophores of the balck-moor goldfish,Carassius auratus. Both mastoparan and compound 48/80 induced an approximately 40% increase in the GTP-hydrolyzing activity in the melanophore membranes compared to the basal level. In intact melanophores, these compounds inhibited the effect of 3-isobutyl-1-methylxanthine, which induced the accumulation of intracellular cAMP. Pretreatment of melanophores with pertussis toxin at 1 μg·ml-1 for 15 h attenuated the inhibitory effect of mastoparan on the accumulation of cAMP. However, pretreatment with the toxin only slightly attenuated the inhibitory effect of compound 48/80 on the accumulation of cAMP. In addition, compound 48/80 at 1 mg·ml-1 induced full aggregation of the melanosomes in melanophores, though mastoparan at 5 μmol·l-1 induced only 10–20% aggregation of melanophores. These results suggest that mastoparan and compound 48/80 can each activate the inhibitory G-protein in goldfish melanophores, which results in inhibition of adenylate cyclase activity. This signal-transduction pathway is involved in the aggregation of melanosomes in these cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02338289
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