ACTA HISTOCHEMICA ET CYTOCHEMICA
Online ISSN : 1347-5800
Print ISSN : 0044-5991
ISSN-L : 0044-5991
Volume 13, Issue 1
Displaying 1-14 of 14 articles from this issue
  • TAKAYOSHI TOBE
    1980 Volume 13 Issue 1 Pages 2-8
    Published: 1980
    Released on J-STAGE: February 26, 2010
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  • TIBOR BARKA
    1980 Volume 13 Issue 1 Pages 9-22
    Published: 1980
    Released on J-STAGE: July 27, 2010
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  • C. P. LEBLOND, GLENDA M. WRIGHT
    1980 Volume 13 Issue 1 Pages 23-34
    Published: 1980
    Released on J-STAGE: February 26, 2010
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  • WALTER SANDRITTER
    1980 Volume 13 Issue 1 Pages 35-39
    Published: 1980
    Released on J-STAGE: February 26, 2010
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  • SETSUYA FUJITA
    1980 Volume 13 Issue 1 Pages 40-48
    Published: 1980
    Released on J-STAGE: February 26, 2010
    JOURNAL FREE ACCESS
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  • WILLIAM H. FISHMAN
    1980 Volume 13 Issue 1 Pages 49-57
    Published: 1980
    Released on J-STAGE: February 26, 2010
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  • KOZO OKAMOTO
    1980 Volume 13 Issue 1 Pages 58-65
    Published: 1980
    Released on J-STAGE: February 26, 2010
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  • LUDWIG A. STERNBERGER
    1980 Volume 13 Issue 1 Pages 66-70
    Published: 1980
    Released on J-STAGE: February 26, 2010
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  • TOYOSHI FUJIMOTO, KAZUO OGAWA
    1980 Volume 13 Issue 1 Pages 72-89
    Published: 1980
    Released on J-STAGE: February 26, 2010
    JOURNAL FREE ACCESS
    The chemical composition and the function of intramembranous particles (IMP) of erythrocyte membranes were examined.
    Firstly, the sulfhydryl (SH) groups detected by the Fast Blue BBN method on ultrathin sections of rabbit erythrocyte ghosts were found to show a correlative distribution with IMP. Secondly, after treating human erythrocyte ghosts with mercuric chloride, IMP appeared to have become larger than the controls. The mean diameter of IMP was approximately 165 A on the P face and 160 A on the E face for the ghosts treated with mercuric chloride, whereas it was 94 A on the P face and 100 A on the E face for fresh ghosts. This result indicates that protein molecules which have SH groups are included in IMP of erythrocyte membrane. Thirdly, acetylcholinesterase (AchEase) activity was detected cytochemically in human erythrocyte ghosts from which IMP-free vesicles were blebbing. AchEase activity was found to be localized only on the external surface of IMP-aggregated ghosts and not on the IMP-free vesicles, suggesting a close relationship of AchEase and IMP. A cytochemical method for detecting AchEase activity on freeze-etched replicas was also described.
    The present results indicate that IMP in erythrocyte membranes are proteinaceous in nature and that some of them are enzyme molecules.
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  • HIROSHI MAYAHARA, KAZUO OGAWA
    1980 Volume 13 Issue 1 Pages 90-102
    Published: 1980
    Released on J-STAGE: February 26, 2010
    JOURNAL FREE ACCESS
    A new one-step method for light and electron microscopic localization of the K-dependent phosphatase (K-NPPase) component of the Na-K-ATPase complex was applied to the rat kidney. In the cortex, intense K-NPPase reaction was localized to the distal convoluted tubules and collecting tubules. Proximal convoluted tubules, especially the first segment, showed weak activity. In the medulla, thick ascending segments of the Henle's loop showed high activity, while thin segments never showed activity. The reaction products of K-NPPase activity were localized on the cytoplasmic side of the lateral and basal plasma membranes of the renal tubular epithelium, indicating the direction of the phosphate liberation by the enzyme to be the cytoplasmic side. The above results were discussed with special reference to the renal physiological function.
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  • ARVID B. MAUNSBACH, ELISABETH SKRIVER, NOBUHIRO DEGUCHI, PETER LETH J& ...
    1980 Volume 13 Issue 1 Pages 103-112
    Published: 1980
    Released on J-STAGE: November 26, 2010
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  • KEI-ICHI HIRAI, SATOKI UENO, KAZUO OGAWA
    1980 Volume 13 Issue 1 Pages 113-126
    Published: 1980
    Released on J-STAGE: July 27, 2010
    JOURNAL FREE ACCESS
    In alveolar macrophages in rat lungs, NAD (P) H oxidase activity was demonstrated by the cytochemical method by Briggs and his coworkers when cerous ions were used as the capture of hydrogen peroxide which was generated from the oxidase reaction. The oxidase could utilize both NADH and NADPH as the substrate and was potassium cyanide-insensitive. The enzyme activity was very weak in the resting cells, with no activity in many cells, but strongly stimulated in the intact cells after a lipopolysaccharide-treatment or particle ingestion. The deposits of cerium perhydroxide were found on the plasma and phagosomal membranes, which must be derived from the former. The activity was suppressed by the addition of tiron (scavenger of superoxide), catalase (scavenger of hydrogen peroxide) and higher concentration of diethyldithiocarbamate (an inhibitor of superoxide dismutase) .
    As to the generation of hydrogen peroxide which is formed by NAD (P) H oxidase reaction, the participation of superoxide dismutase was considered. An attempt to demonstrate superoxide dismutase activity was done by using the substrate, superoxide-forming system consisted of xanthine oxidase plus xanthine. The reaction product, hydrogen peroxide, was sedimented by cerium chloride by modifying the Briggs' method. Precipitation was seen in the cytoplasm throughout except the cell organelles, and on the plasma membrane. The reaction also occurred in the erythrocyte matrix, including the plasma membrane site. All reaction was abolished by diethyldithiocarbamate, potassium cyanide, tiron and catalase. Therefore, it may be concluded that there are NAD (P) H oxidase and superoxide dismutase in the pulmonary macrophages, and these enzymes may have a coupled function in oxygen consumption after phagocytosis or membrane stimulation.
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  • HIROSHI HIRANO
    1980 Volume 13 Issue 1 Pages 127-138
    Published: 1980
    Released on J-STAGE: February 26, 2010
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  • MASAO YOKOYAMA
    1980 Volume 13 Issue 1 Pages 139-153
    Published: 1980
    Released on J-STAGE: February 26, 2010
    JOURNAL FREE ACCESS
    The plasma membranes of human solid tumor cells as well as normal tissue cells were dissociated and purturbed by labeled lectins and the cellular responses were compared. Lectins used were concanavalin A (Con A) and Ricinus communis agglutinin (RCA) labeled by either ferritins (Fer) or horseradish peroxidase (HRP) . Lectin-binding sites were found over the external cell surface of the fixed normal and carcinoma cells of the human kidney. Lectin-induced redistribution of the binding sites was more pronounced in the tumor cells than normal cells, revealing uneven surface label and membrane internalization. The polarity of tubule cells was maintained after dissociation and lectin treatment. Dissociated cancer cells of human urothelium showed a marked mobility of binding sites after lectin exposure. The results indicate the human solid tumor cells have highly fluid membranes as has already been seen in cultured transformed cells.
    The luminal plasma membrane of the rat bladder was evenly stained by HRP-lectins and Fer-lectins after fixation. RCA-Fer was distributed evenly over the concave plaques and ridges of tbe fixed bladder surface, while the distribution of RCA-Fer was uneven and found only over the ridges in the unfixed bladder surface. Similar changes were observed in the label by cationized ferritins. The surface property seems to be different between plaque and interplaque (ridge) regions. Preliminary observation on preneoplastic and neoplastic lesions of rat bladder induced by BBN showed an increase in the numbers of RCA-binding sites as well as their mobility in the plasma membrane. It was associated with the appearance of microvilli, loss of concave plaques and of discoid vesicles in the urothelial surfaces. This approach is feasible for the evaluation of the mechanism in bladder carcinogenesis.
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