[Surgical treatment of esophago-bronchial fistula with pulsion diverticulum].
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Biomedical subjects
Publications and source records attributed to Y Fukazawa.
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We have investigated the chemical structure of the antigenic determinant of Candida krusei cell-wall mannan. Acetolysis of the mannan, obtained by extraction with alkali and purified as copper complex, gave five oligosaccharides (from mono- to pentasaccharide) and a minor amount of an octasaccharide. Partial acetolysis of the mannan gave a large amount of mannooctaose. We have examined the inhibition by these oligosaccharides of the precipitin reaction between anti-Candida krusei serum and homologous mannan, and found that the mannooctaose was the most effective inhibitor. Results obtained by proton magnetic resonance spectroscopy, methylation analysis, and other structural studies of Candida krusei mannan, suggest that the octasaccharide possesses six alpha (1-2) linkages and one alpha (1-6) linkage located in the middle of the chain, and that this mannooctaose may be responsible for the specificity of Candida krusei cell-wall mannan.
We investigated the chemical structure of the specific determinant in the mannan of Candida albicans M-1012 (serotype A) strain. Acetolysis of the mannan, obtained by alkali extraction and purified as the copper complex, gave mannose and six oligosaccharides (from di- to hexasaccharide) and a small amount of a heptasaccharide. We examined the inhibition by these oligosaccharides up to hexaose of the precipitin reaction between anti-factor 6 serum specific for serotype A and homologous mannan, and found that the mannohexaose was the most effective inhibitor. These, and results obtained by proton magnetic resonance (PMR) spectroscopy, methylation analysis, and other structural studies, suggest that the main component of this hexaose consists of one terminal alpha (1-3) linkage in addition to four alpha (1-2) linkages, and that this alpha (1-3)-containing mannohexaose may be responsible for the specificity of antigenic factor 6. Further results obtained by analyses of polarimetry, PMR spectroscopy, and chromium trioxide oxidation-methylation of C. albicans M-1012 mannan has a beta-linkage in addition to alpha-linkages, and that the mode of the beta-linkage is mainly (1-6) linkage. Further evidence obtained by Smith degradation-methylation analysis and by quantitative precipitin reactions of intact and acid-degraded mannan suggests that the antigenic determinant of antigenic factor 6 may be bound, via the beta (1-6) linkage, to C-6 of mannose residues involved in oligosaccharide side chains of serotype A mannan.
Antigenic analysis of the four serotypes of Cryptococcus neoformans was carried out by slide agglutination with reciprocal adsorption methods. With this procedure the antigenic patterns of the serotypes were established. Serotypes A and D had antigenic factors 1, 2, 3, 7 and 1, 2, 3, 8, respectively. Serotypes B and C were found to have antigenic factors 1, 2, 4, 5 and 1, 4, 6, respectively. Factor sera, prepared according to the antigenic patterns demonstrated by adsorption studies, proved to be useful for rapidly and accurately identifying C. neoformans serotypes. Some patterns similar to those of the C. neoformans serotypes were observed in five other Cryptococcus species and two Candida species. The proton magnetic resonance spectra of polysaccharides from the C. neoformans serotypes correlated well with their antigenic characteristics. Phenol oxidase test reactions and growth at 37 degrees C were useful criteria for determining which yeasts should be chosen for clinical application of factor sera for serotyping of C. neoformans. Sixty-two Japanese isolates of C. neoformans were serotyped. Fifty-eight of these isolates were serotype A, three were serotype A-D, and one was serotype D.
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We investigated the adherence of gelatinized lipid emulsion (GLE) to tissues and cells, the reaction system of this phenomenon and the clinical significance of the adherence-promoting factor (APF) in human serum. In the presence of fresh human serum, GLE adhered to all tested tissues and blood cells. APF was shown to be macromolecular alpha 2-globulin; it formed flocculent precipitate with gelatin, and adsorbed to gelatin-Sepharose. Therefore, we termed APF gelatin-reactive protein (GRP) although it may be identical or closely related to plasma fibronectin. We also noted a significant decrease in GRP activity in patients with systemic disorders including cancer, liver cirrhosis, and systemic lupus erythematosus when their sera were assayed by the GLE-rat liver system.
Mice immunized with viable C. albicans cells demonstrated a high incidence of cell-mediated and a low incidence of humoral immune response. There was good agreement between the final survival rate of C. albicans infected mice and the rate of simultaneous cell-mediated and humoral immune response acquisition. Immunized mice with positive delayed hypersensitivity (DTH) against C. albicans crude antigen showed significant protection against intravenous challenge with C. albicans. Furthermore, the transfer of immunoglobulins from rabbit anti-C. albicans serum to DTH-positive mice enhanced protection, while it did not protect control mice against a subsequent challenge with C. albicans. These results suggest that cell-mediated immunity plays a major role and humoral immunity a side role in the defense mechanism(s) of C. albicans infected mice.
The phagocytic and intracellular killing activities of normal mouse phagocytes against Candida albicans were studied to elucidate the role of these activities in nonspecific and specific defense mechanisms. In the presence of fresh normal mouse serum, viable C. albicans cells were ingested by mouse peripheral blood leukocytes (PBLs) and peritoneal macrophages (PMPs) at the same rate. Serum-chelation experiments indicated that the factors involved in the alternative complement pathway are opsonins for C. albicans. PBLs killed intracellular C. albicans more effectively than PMPs. Lymphokine-activated PMPs manifested marked intracellular killing activity and the occurrence of increased superoxide anion- and singlet oxygen production, in the absence of increased myeloperoxidase (MPO) production, suggests that the enhanced, MPO-independent, oxidative mechanism may play an important role in the candidacidal activity. Specific rabbit antibodies played no role in the phagocytosis and intracellular killing of C. albicans. These results suggest that PMNs and factors involved in the alternative complement pathways, and lymphokine-activated macrophages play major roles in the protection of mice against C. albicans infection.
Activation of macrophages with macrophage activating factor (MAF) was evaluated by measuring the intracellular killing activity of murine macrophages against Salmonella typhimurium. Concanavalin A (Con A)-induced MAF-rich fraction was obtained by a Sephadex G-100 column, which contained molecules ranging from 25,000 to 67,000 daltons. The intracellular killing ability of mouse peritoneal macrophages against S. typhimurium was found to be increased by 0.1 M D-mannose as well as by Con A-induced MAF-rich fraction. Both 0.1 M D-mannose and MAF exhibited a similar timing pattern for macrophage activation. The same concentration of D-glucose or L-rhamnose did not change bacterial uptake and intracellular killing by macrophages. Moreover, when MAF-rich fraction was applied to a Con A-Sepharose column, a fraction that was adsorbed on Con A and eluted with 0.1 M alpha-methyl D-mannoside exhibited MAF activity. These results suggest the possibility that mannopyranosyl residues in the MAF molecules play an important role as a ligand in macrophage activation.
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The character of the antibody response in the rabbit to Salmonella typhimurium somatic (O) antigen was similar to the response to each of several serotypes of Shigella flexneri O antigens, namely a predominance of production of immunoglobulin M (IgM) antibody. Lipopolysaccharide protein (LPSP) and lipopolysaccharide (LPS) fractions of Salmonella O antigen differed significantly in both quantitative and qualitative aspects of their immunogenicity. LPSP elicited high levels of agglutinins and also induced the production of a significant amount of immunoglobulin G (IgG) antibody at a late period. LPS antigen elicited low levels of agglutinins which were exclusively IgM antibody. These results suggested that the chemical nature of the antigen is one important factor in the determination of the character of the antibody response. Further, it is suggested that the protein moiety of the O antigen complex is a carrier active in allowing induction of early IgM and of late IgG antibodies; in contrast, the lipid moiety may compete with this action of the carrier protein, thereby suppressing IgG antibody in the primary stage of the antibody-forming process.
Considerable amounts of immunoglobulin G (IgG) antibody appeared in hyperimmune rabbit serum at a late period during a course of immunization with several injections of Shigella flexneri O antigens. High yields of IgG antibody possessing homogenous specificity could be fractionated from crude gamma-globulin solution on a diethylaminoethyl-Sephadex column with 0.02 m phosphate buffer (pH 6.6) containing 0.1 m NaCl. Specificities of IgG antibodies for six serotypes of S. flexneri were demonstrated to be high as compared with those of whole sera and their IgM antibodies. Type-specific factors for antigens I to VI were shown in each IgG fraction according to serotype employed. Further, in most sera, subtype-specific factors could be detected in the IgG fraction. These results suggest that it would be desirable to use IgG antibodies for the typing of S. flexneri.
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