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  • 1
    Electronic Resource
    Electronic Resource
    CEREBRAL ANOXIA: EFFECT ON NEURON-GLIA FRACTIONS AND POLYSOMAL PROTEIN SYNTHESIS (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 27 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The incorporation of [3H]leucine into proteins of neuron-enriched and glia-enriched fractions was studied after various periods of anoxia produced in vitro in rabbit brain. Protein synthesis was carried out with brain slices, and the cellular fractions were subsequently separated with Ficoll density gradient ultracentrifugation. Leucine incorporation decreased promptly even at the early stage of cerebral anoxia (less than 10 min) and the incorporation in the glial fraction declined at least as much as the incorporation in the neuronal fraction. To substantiate that these changes were based on functional alteration of post-transcriptional or translational mechanism at the polysomal level, polysomes were isolated from anoxic brain slices and polypeptide synthesis was carried out in vitro. The decrease of polypeptide synthesis correlated well with the decline of leucine incorporation in brain slices. Polypeptide synthesis decreased sharply between the 10-min and the 20-min anoxic period and a corresponding decrease of the polysomal peak was observed on the polysomal aggregation profile. This study indicated rapid and diffuse inhibition of protein synthesis in cerebral anoxia both in the neuronal and glial elements, the inhibition being based on the alteration of the mechanism for polypeptide synthesis at the polysomal level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb12279.x
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  • 2
    Electronic Resource
    Electronic Resource
    RNA METABOLISM IN RABBIT BRAIN: STUDY WITH NEURON-GLIA AND SUBCELLULAR FRACTIONS (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 23 (1974), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —Uridine incorporation into RNA of rabbit brain was studied by using an in vitro system for incubation of brain slices for up to 180 min. Neuron-enriched and glia-enriched fractions were prepared by ficoll density gradient centrifugation, and various subcellular fractions were prepared by sucrose density gradient centrifugation. Although the difference was not as great as in the case of l-leucine incorporation into protein, the neuron-enriched fraction consistently showed a higher specific radioactivity than the glia-enriched fraction. The specific radioactivity of the nuclei increased promptly and remained high at 180 min; the increase in the microsomes was gradual. Comparison of these data suggests that both neuron-enriched and glia-enriched fractions retain high radioactivities in their nuclei at 180 min when a considerable portion of the ribosomal RNA in these fractions is not labeled. The sharp diffusion gradient of nucleotides is discussed in relation to the acid-soluble radioactivity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1974.tb04410.x
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  • 3
    Electronic Resource
    Electronic Resource
    CEREBRAL ANOXIA: EFFECT ON TRANSCRIPTION AND TRANSLATION (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 22 (1974), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The activity of DNA-dependent RNA polymerase and the synthesis of microsomal protein were investigated after various periods of anoxic condition produced with rabbit brain in an in vitro experimental model. There was prompt inhibition of protein synthesis even after an anoxic period of 5 min, and inhibition was more than 80 per cent after an anoxic period of 30 min. However, RNA polymerase activity was retained during the early stage of anoxia, but definite inhibition appeared after an anoxic period of 15 min. Comparisons with other available information suggest that the inhibition of protein synthesis observed with brain slices is closely related to their polysomal function, that irreversibility of inhibition of protein synthesis might be related to the involvement of nuclear RNA synthesizing mechanism, and that these can occur both in the neuronal and glial elements.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1974.tb12186.x
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of anoxia and ischemia on ribonuclease activity in brain (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 32 (1979), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb04607.x
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  • 5
    Electronic Resource
    Electronic Resource
    PHOSPHORYLATION OF NUCLEAR PROTEINS FROM RABBIT CEREBRUM, CEREBELLUM AND LIVER IN VITRO (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 31 (1978), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Phosphorylation of nuclear protein was investigated with isolated nuclei from rabbit cerebral cortex, cerebellum and liver by using [γ-32P]ATP. The results were compared with the previously reported findings on phosphorylation with tissue slices and [32P]phosphate. Cerebral cortex showed a very high level of phosphorylation, while liver showed the lowest, the difference being several fold in magnitude. With each tissue source, the extent of phosphorylation was maximum at incubation period for 2–3 min with steady decline afterwards. When nuclear proteins were further fractionated into 0.14m-NaCl-soluble, 0.25 n-HCl-soluble (mainly histone) and acidic phenol-soluble proteins, NaCl-soluble protein showed the highest phosphorylation while HCl-soluble the lowest. The ratio among these tissue sources studied and the ratio among various protein fractions in each tissue source were strikingly similar to what had been shown with tissue slices. Further separation of acidic phenol-soluble protein with polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate revealed retention of the characteristic difference of the pattern of phosphorylation between liver and the CNS tissue as having been observed with tissue slices, although phosphorylation of proteins with molecular weights of less than 40,000 was much reduced with the isolated nuclei. Although other methods with extracted protein kinase or chromatic protein fractions might be more desirable under ordinary situations, the system for nuclear protein phosphorylation with isolated nuclei and [γ-32P]ATP may be useful under certain experimental conditions provided the incubation condition is carefully selected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1978.tb12452.x
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  • 6
    Electronic Resource
    Electronic Resource
    PROTEIN and RNA SYNTHESES and PRECURSOR UPTAKE WITH ISOLATED NERVE and GLIAL CELLS (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 32 (1979), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Protein and RNA syntheses were investigated with bulk isolated nerve and glial cells from rabbit brain. For polypeptide synthesis, ‘intact’ cells were incubated with [3H]leucine under various conditions and the results were compared with those of polyribosomal polypeptide synthesis. For RNA synthesis ‘intact’ cells were incubated with [3H]uridine or [3H]guanosine and the results were compared with those of DNA-dependent RNA polymerase assay. The bulk isolated ‘intact’ nerve cells were more active in protein synthesis than the ‘intact’ glial cells, while the latter synthesized RNA more actively than the former, although both polyribosomal polypeptide synthesis and DNA-dependent RNA polymerase activity were higher with the nerve cells, indicating a higher potential for the nerve cells. The observed discrepancy of RNA synthesis was explained by the significantly less active uptake of nucleosides with the nerve cells. Both protein and RNA syntheses with ‘intact’ cells were sensitive to hypoxic or glucose-deficient conditions. While both the nerve and glial cells were sensitive to hypoxia to a similar extent, the nerve cells were more sensitive to glucose deficiency. It was suggested that the bulk isolated nerve and glial cells still retain certain integral cell functions as viable cells, and can be utilized for various physiological and pharmacological investigations provided caution is exercised in their application and in the interpretation of the results.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb04524.x
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  • 7
    Electronic Resource
    Electronic Resource
    Phosphorylation of Chromatin Proteins in Cerebral Anoxia and Ischemia (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 35 (1980), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Phosphorylation of nuclear protein was investigated in cerebral anoxia up to 30 min with rabbit brain and in cerebral ischemia up to 6 h with gerbil brain in vitro. Isolated nuclei were incubated in the presence of [γ-32P]ATP and were then fractionated into the NaCl-soluble, HCl-soluble, and phenol-soluble protein fraction. Each protein fraction was further separated by gel electrophoresis, and profiles of 32P incorporation were evaluated in these pathophysiological conditions. 32P incorporation of the acidic phenol-soluble nonhistone chromatin protein became significantly suppressed in cerebral anoxia after 15 min, and there were decreases of 32P incorporation in protein with high molecular weight and increase in protein with low molecular weight on gel electrophoresis. With gerbil brain nuclei, 32P incorporation into the NaCl-soluble and HCl-soluble fraction was increased without significant de-crease in the phenol-soluble fraction after an ischemic period of 3 h. However, further separation of the phenol-soluble fraction demonstrated decrease of 32P incorporation in protein with high molecular weight and increase in protein with low molecular weight. At present, the significance of these findings, particularly in relation to chromatin template activity or irreversibility of these pathophysiological conditions, is not clear.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1980.tb07877.x
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  • 8
    Electronic Resource
    Electronic Resource
    SUBCELLULAR DISTRIBUTION OF RADIOACTIVITY IN NEURONAL AND GLIAL-ENRICHED FRACTIONS AFTER INCORPORATION OF [3H]LEUCINE IN VIVO AND IN VITRO (1971)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 18 (1971), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The distribution of protein-bound radioactivity among subcellular organelles of cerebral cortex was followed after intravenous administration of [3H]leucine and after incubation of brain slices in the presence of [3H]leucine. Neuronal and glial cell-enriched fractions were prepared by discontinuous sucroseFicol1 gradient centrifugation of cerebral cortex cell suspensions. Subcellular fractions were obtained from each of the cell prepara- tions and the protein-bound radioactivity determined after in uiuo and in vitro incorporation of [3H]leucine. The unfractionated neuronal material had a considerably higher level of protein-bound radioactivity than the glial material. The most marked neuronal-glial dif- ferences were observed in microsomes and soluble proteins, while the radioactive labelling of the nuclear and mitochondria1 fractions was similar for the two cell types.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb00009.x
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  • 9
    Electronic Resource
    Electronic Resource
    Trypsin-like protease of mites: purification and characterization of trypsin-like protease from mite faecal extract Dermatophagoides farinae. Relationship between trypsin-like protease and Der f III (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 23 (1993), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A serine protease from mite faecal extract, Dermatophagoides farinae, was purified using DEAE-Sephacel anion exchange chromatography and Supcrdex 75 pg gel chromato-graphy. The molecular weight of this protease was 34 kD on SDS-PAGE under reducing conditions. The optimal pH and temperature of the protease were 8-0 and 47 C, respectively. In addition, this protease cleaved arginyl or lysyl residue containing substrates selectively and was only inhibited by aprotinin, PUT-175, tind soy bean trypsin inhibitor and not by chymostatin, E-64 and iodoacetic acid. These results show that our purified serine protease belongs to the trypsin-type. Purified trypsin-like protease was shown to be allergenic by enzyme-linked immunosorbent assay. Antigeni-city of trypsin-like protease was completely different from those of Der f I and Der f II. Both, 20 N-terminal amino acid sequence and amino acid compositions of the purified protease were very similar to those of Der f III. Good similarities were found between trypsin-like protease and Der f III concerning physicochemical properties such as molecular weight on SDS-PAGE and ammonium sulphate solubility. Summarizing the above data, it can be concluded that a trypsin-like protease from mite faecal extract is actually the Der f III allergen and that it may be involved in the digestive process of the mite as it was found not in mite body but in mite faeces.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1993.tb00366.x
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  • 10
    Electronic Resource
    Electronic Resource
    Significance of urinary binucleated podocytes in IgA nephropathy (2001)
    Melbourne, Australia : Blackwell Science Pty
    Nephrology 6 (2001), S. 0 
    Details
    ISSN: 1440-1797
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background: We have reported clinico-pathological significance of podocytes excreted in urine in previous papers. During these studies we found the presence of binucleated podocytes in urine. The aim of the present study was to look for the significance of urinary binucleated podocytes in IgA nephropathy.Patients and methods: 123 patients aged 2–25-year-old with various renal diseases were studied: UTI, five cases; nephrotic syndrome, 30 cases; MGN, three cases; MPGN, six cases; Alport syndrome, five cases; lupus nephritis, seven cases; HSPN, 12 cases; IgA GN, 50 cases. A total of 1225 urine samples from these diseases were examined. As a control, 203 urine samples from 100 normal healthy children were examined.Usual IF using monoclonal antibody to podocalyxin was used to detect urinary podocytes and binucleated podocytes.The presence of urinary binucleated podocytes were confirmed by immunoelectron microscopic examination and confocal immunofluorescent examination.Pathological changes were scored into six items: acute intracapillary, chronic intracapillary, acute extracapillary, chronic extracapillary, acute tubulo-interstitial and chronic tubulo-interstitial lesions.Results:〈list style="custom"〉1Urinary binucleated podocytes were found in various renal disases.2In IgA GN, patients with u-binucleated podocytes had significantly higher level of proteinuria.2The number of u-binucleated podocytes paralleled that of u-mononucleated podocytes.4. Patients with u-binucleated podocytes had significantly more acute lesions histologically.Conclusion: Urinary binucleated podocytes were found in IgA GN with acute glomerular lesions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1440-1797.2001.00011.x
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