[A case of multiple tumor-cell embolism to the central nervous system simulating neoplastic angioendotheliosis].
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Biomedical subjects
Publications and source records attributed to T Miyazaki.
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About 50 mg/kg of paromomycin sulfate was administered orally in a single or 2 divided doses to patients with Diphyllobothrium latum infections. The following results were obtained. After the treatment with paromomycin sulfate mature strobilae were expelled in all of 7 patients with Diphyllobothrium latum infections. We couldn't find scolices in all cases. Although these stools were examined for 2 months after the treatment, the eggs of Diphyllobothrium latum were not identified. No side effects were observed in all cases. It was concluded that paromomycin sulfate was effective on the treatment of Diphyllobothrium latum infections.
A solid-phase, non-competitive radioimmunoassay for aldolase A in human serum has been developed. Human aldolase A was purified from muscle, and specific antisera to the purified aldolase A were obtained from chickens. Specific IgG anti-human aldolase A was purified by affinity chromatography. Disposable polypropylene plates were coated with specific IgG antibody and used for radioimmunoassay with 125I-specific IgG antibody to aldolase A. The non-specific binding was minimized by saturating the binding sites of the plates with 2% ovalbumin in 0.1% Tween 20. This radioimmunoassay is specific for the aldolase A subunit, with no cross-reactivity with human aldolase B subunit or homopolymeric human aldolase C(C4). The serum aldolase A immunoreactivities of 33 normal subjects ranged from 124 to 212 ng/ml with a mean of 178 +/- 41 ng/ml (+/- 2 SD). Ninety-three patients' sera were assayed with both a solid-phase non-competitive radioimmunoassay and a competitive double antibody radioimmunoassay developed in our laboratory and the results showed a high degree of correlation (r = 0.912; p less than 0.001). Rapidity and simplicity of the solid-phase assay makes it superior to other methods for the measurement of serum aldolase isozymes.
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We have demonstrated that 125 I-CEA (carcinoembryonic antigen) from two commercial sources (Roche and CIS RIA kit) can be precipitated by antibody to alpha 1-acid glycoprotein (AG) dose-dependently. The binding of 125 I-CEA to anti-AG can be displaced by unlabelled AG, though, there was no cross-reaction between AG and anti-CEA. The data strongly suggest that CEA has an immunological similarity to AG. The perchloric acid extract from cancerous tissue was fractionated on a Sephadex G-200 column, and the first eluted fraction (containing large amounts of CEA) was subjected to affinity chromatography using anti-AG bound to Sepharose. The bound fraction was eluted, labelled with 125 I, and then applied to a Sephadex G-200 column with carrier protein. The radioactivity was found mainly in the large molecular size eluted fraction (Fr 1). Almost all radioactivity of Fr 1 was precipitated by anti-AG and anti-CEA. This experiment also demonstrated that a large molecular weight component (Mr: 180 000) obtained from tumor was immunologically related to both CEA and AG. Based on differences in binding affinities between CEA with anti-CEA and with anti-AG we postulate that CEA may be a large molecular precursor of AG (big form of AG).
We have recently suggested that carcinoembryonic antigen (CEA) may contain alpha 1-acid glycoprotein (AG) antigenic determinant. In the present work we examined a protein with CEA-like activity in the feces of healthy subjects (NCA) for immunological cross-reactivity with AG. When the perchloric acid extract of feces was fractionated on a Sephadex G-200, two fractions (large and small molecular weight) were obtained. The large molecular weight fraction had higher CEA activity than the small one. The perchloric acid (PCA) extract of feces was subjected to affinity chromatography using anti-CEA bound to Sepharose, and the bound protein was labelled with 125I, and then fractionated on a Sephadex G-200 column. Two radioactive peaks, Peak 1 corresponding to an approximate Mr of 180 000 and Peak 2, corresponding to an approximate Mr of 60 000 were found. Both peaks showed immunoreactivity with either anti-CEA or anti-AG. This experiment suggests the presence of two kinds of CEA-reactive proteins in feces: one which may be a big protein with immunological similarity to AG and a second which appears to be a hydrolysed fragment of this protein.
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The case of a paraventricular cerebral cyst with a partial defect of the corpus callosum is reported. The cyst wall was studied using light and electron microscopy. Electron microscopy revealed that the lining of the cyst consisted by a single layer of epithelial cells. The cells of the cyst wall, which rested on a basement membrane, had microvilli and abnormal cilia, and there were desmosomes between the cells, In accordance with the pathological findings, the cyst was classified as a type transitional between a choroidal epithelial cyst and an ependymal cyst.
Dipeptidyl peptidase (DPP) IV activities in normal human sera and in the sera of patients with malignant tumors of the oral region were assayed. Patients with oral squamous cell carcinoma had significantly lower enzyme activity than that of normal controls (p less than 0.001). Patients with advanced carcinoma showed a more significant reduction of serum enzyme activity. On the other hand, in oral squamous cell carcinoma patients with hepatic dysfunction, the serum enzyme activity was significantly increased (p less than 0.02).
The effects of tunicamycin (TM) on cell adhesion and on the biosynthesis of the membrane-associated glycoproteins in aggregation-competent cells of Dictyostelium discoideum were investigated. The cohesiveness due to the EDTA-stable contact site was completely inhibited in the presence of 1 microgram/ml of TM. In contrast, when cells were treated with high concentrations of TM, the EDTA-sensitive contact site in the early developmental stage remained functional. Scanning electron microscopy showed the surface of TM-treated cells to be smoother than that of untreated cells. The membrane proteins of the aggregation-competent cells and TM-treated cells were analyzed by polyacrylamide gel electrophoresis (PAGE) in the presence of sodium dodecyl sulfate (SDS). The results showed that several protein bands at 190 kd, 170 kd, 150 kd, 135 kd, 127 kd, 94 kd, 80 kd, 68 kd, 61 kd, and 52 kd which were observed in the untreated cells disappeared in the TM-treated cells, and protein bands at 105 kd and 70 kd were newly detected in the treated cells. Tunicamycin inhibited the incorporation of [3H]mannose or [14C]glucosamine into the trichloroacetic acid (TCA)-insoluble material of the aggregation-competent cells, while it did not affect [3H]leucine incorporation. These results suggest that an asparagine-linked carbohydrate moiety of membrane-associated glycoprotein(s) is involved in cell adhesion of aggregation-competent cells of D. discoideum.
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We typed coded sera from 135 healthy controls, seventy-six patients with autoimmune goitrous and seventy-three with atrophic thyroiditis for IgG heavy chain markers (Gm). All subjects were Caucasian from Newfoundland. An increase in the Gm phenotype ag was found in the 149 patients with thyroiditis compared to controls (chi 1(2) = 5.82, P less than 0.01); significance was, however, not maintained after correction for the number of variables tested. The difference in ag phenotype was more pronounced among the seventy-three patients with atrophic thyroiditis (chi 1(2) = 8.80 corrected P less than 0.05). Because the haplotype ag was not significantly increase in this group, we conclude that homozygotes for Gm ag are at an increased risk of developing atrophic thyroiditis.