Biomedical subjects
Publications and source records attributed to K Kudo.
In vivo effect of gold salts on the IgE immune response was investigated in mice and rats. It was demonstrated that gold salts did not suppress but rather enhanced the antigen-specific IgE immune response in mice. Moreover, gold salt had on mast cell degranulation in vivo in rats.
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Characterization and purification of the allergenic components of the house dust mite, Dermatophagoides farinae, were investigated. It was found that the mite antigen was heat-stable, pronase-sensitive, and periodate-resistant, which suggested that the antigenic determinants of the mite antigen resided mainly in the protein component. Purification of the mite antigen was tried using Sephadex G-150, DEAE cellulose, and isoelectrofocusing columns. The most potent allergenic fraction was around 20,000-30,000 in molecular weight, although the allergenic activity spread in a wide molecular weight range. Prausnitz-Küstner type skin reactions were performed on rats using mouse homocytotropic antibodies for allergenic evaluation, and the clinical usefulness of this method is discussed.
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Rat ascites hepatoma AH109A cells (present as a free form in vivo) can aggregate and then develop well-defined tripartite junctional complexes, including intermediate junctions, desmosomes and focal tight junctions, on incubation with a glycoprotein separated from rat ascites hepatoma AH136B cells (forming cell islnds in vivo). The development of binding structures was strongly inhibited by actinomycin D. AH109A cells or rat ascites hepatoma YS cells (present as a free form in vivo) previously treated with the glycoprotein for 24 h, when inoculated i.p., proliferated as free cells in the ascitic fluid, like the untreated cells. AH109A cells actively proliferating in the skin do not form any junctional complexes. The reason for the failure of island formation by AH109A cells or YS cells in vivo is discussed.
The previously described glycoprotein that promotes tumour cell aggregation, derived from rat ascites hepatoma cells and capable of partial purification by chromatography, was found to be a mixture of 2 factors with different antigenic property. One was not absorbed by immunoadsorbent chromatography with anti-rat serum antibody and the other was. The action of the unabsorbed factor was clearly more potent than that of the absorbed factor. Both the factors were found in the serum of tumour bearing rats and the action of the unabsorbed factor was also more potent than that of the absorbed factor; its amount increased with time after i.p. inoculation of the cells. The serum of healthy rats contained the absorbed factor but not the unabsorbed factor. It was thus assumed that the unabsorbed factor was associated with the hepatoma cell surface itself and released into the serum, while the absorbed factor was associated with serum protein coating the cell.
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In order to better understand the role of riboflavin in the lens, we investigated the lenses of rats fed on a riboflavin deficient diet for 7 weeks to determine changes in the inactivation of cortisol, the glucose-6-phosphate dehydrogenase (G-6-PD) activity and the histidine or 5-hydroxytryptophan decarboxylase activity. The cortisol-binding capacity and G-6-PD activity in the lenses of rats fed on a riboflavin deficient diet were found to be decreased as compared with a control. Histidine decarboxylase activity was found twice as high in the riboflavin deficient rats as in the normal lenses however, 5-hydroxytryptophan decarboxylase was somewhat decreased. These findings show that catabolical changes in the metabolism of rat lenses are induced comprehensively by feeding on a riboflavin deficient diet in the same manner as changes are seen in the cataractous lens.
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A substance capable of promoting tumour cell aggregation was released from rat ascites hepatoma cell (possibly from the cell surface) kept in Hanks' balanced salt solution (free of calcium and magnesium) in the cold, and then partially purified by chromatography with DEAE-Sephadex and gel filtration with Bio-gel. The thermostable substance seemed to be a glycoprotein and its molecular weight was about 72,000 when measured by gel filtration on Sephadex G-200. It had no proteolytic activity. The material was clearly effective for rat ascites hepatoma cells as well as SV40 transformed cells, but less effective for Chang's cells and apparently ineffective for normal rat liver cells and red blood cells. The action of this material was more potent than that of Jack bean concanavalin A when assayed for aggregation of SV40 transformed cells. Its effect was not influenced by concanavalin A inhibitors such as alpha-methyl-D-glucopyranoside, N-acetyl-D-glucosamine and D-glucose.
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