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K Sudo

Publications and source records attributed to K Sudo.

At least 289 records · Page 16Linked to original sources

[The effect of anti-human AFP serum for AFP producing stomach cancer xenotransplanted nude mice].

The effect of anti-human alpha-fetoprotein (AFP) on growth, serum AFP levels and histological changes of two lines of AFP producing stomach cancer serially xenotransplanted in nude mice were examined. The efficacy of anti-human AFP antibody on tumor growth was observed specifically for the tumor producing AFP, but there was great difference on growth between two lines. The AFP levels of the serum disclosed a rapid decrease after administration of antibody and maintained as level of Ong/ml for a long period. On histopathologic examination, there were not observed any changes on the tumor cells and structure and necrotic change was not demonstrated. By the immunohistochemical examination (PAP method), anti-human AFP antibody was identified in tumor even 50 th days later after injection.

Adenocarcinoma↗

Estimation of the gene frequency of lactate dehydrogenase subunit deficiencies.

To detect the frequency of lactate dehydrogenase (LDH) subunit deficiency, screening for LDH subunit deficiency was performed on 3,776 blood samples from healthy individuals in Shizuoka Prefecture by means of electrophoresis. The frequency of heterozygote with LDH-A subunit deficiency was found to be 0.185%, and with LDH-B subunit deficiency, 0.159%. The frequencies of both subunit deficiencies were not significantly different. Gene frequencies of LDH subunit deficiencies were calculated by the simple counting procedure, and the results are as follows: gene frequency of LDH-A subunit deficiency was 11.9 X 10(-4), and that of LDH-B subunit deficiency, 7.9 X 10(-4). In addition, the second case in the world of a homozygous individual with LDH-A subunit deficiency was detected by this screening. This case with regard to the characteristics of LDH-A subunit deficiency are summarized herein.

Erythrocytes↗

Allotypes of murine factor B controlled by a locus within the S region of the H-2 complex.

Bf protein was directly precipitated from a mixture of EDTA-plasma from 13 different, inbred strains and rabbit IgG anti-mouse Bf, and was isolated by SDS-PAGE. The gel pieces containing Bf protein were digested by trypsin after labeling with 125I-Na, and then peptides of Bf protein with each mouse strain were compared by two-dimensional peptide mapping. The results for the peptide patterns with the standard B10 congenic strains (all of which Bf phenotypes had been already designated as Bf.1 because of the identical isoelectric point values) revealed two distinct peptide patterns. The peptide pattern of Bf protein appeared to be identical in each of the inbred strains, but only one of the 36 spots in the fingerprint observed either with B10 or B10.BR (designated tentatively as Bf.1 (b.k.) ) was not detected in that from B10.D2 and B10.S (designated tentatively as Bf.1 (d.s.) ). The results of peptide mapping with intra-H-2 recombinant inbred strains show that this structural variant was mapped to the S region, which is direct evidence that allotypes of murine Bf are encoded by a structural gene within the MHC.

Animals↗

Gastric- and intestinal-type properties of human gastric cancers transplanted into nude mice.

The gastric- and intestinal-type properties of 15 human gastric cancers, which were transplanted into nude mice, were studied biochemically and histologically. Enzyme activities were determined in the crude extracts of cancer tissues: pepsinogen isozymes as gastric marker enzymes; and sucrase, aminopeptidase (microsomal), and alkaline phosphatase as intestinal marker enzymes. By hematoxylin and eosin staining and paradoxical concanavalin A staining, gastric cancer tissues were classified into gastric type (pyloric gland cell type and surface mucous cell type) and intestinal type (goblet cell type and intestinal absorptive cell type). On the basis of their properties, human gastric cancers were classified into four types: (a) intestinal type; (b) gastric type; (c) intestinal plus gastric type; and (d) unclassified type, showing no gastric- or intestinal-type properties. Of six well-differentiated adenocarcinomas, four were of intestinal type, one of gastric type, and one of intestinal plus gastric type. All of the intestinal-type carcinomas showed sucrase activity. Of the three signet ring cell carcinomas, one was classified as a gastric type, one as an intestinal plus gastric type, and one as an unclassified type. Of the six poorly differentiated adenocarcinomas, five were of the intestinal type and one of the unclassified type. The present results clearly showed the appearance of intestinal-type properties in gastric cancer cells not only in so-called intestinal-type carcinomas, but also in diffuse-type carcinomas.

Adenocarcinoma↗

A specific kinetic assay for tripeptide aminopeptidase in serum.

This is a method for measuring tripeptide aminopeptidase (EC 3.4.11.4) activity in serum. L- Leucylglycylglycine is used as substrate, and the reaction is followed by monitoring the absorbance increase at 340 nm when NAD+ is reduced to NADH in the presence of an excess of leucine dehydrogenase. This principle allows kinetic determination of the enzyme without interference by carboxypeptidases. Amastatin is added to the reaction mixture to prevent nonspecific hydrolysis of the substrate catalyzed by other aminopeptidases. As final reaction concentrations we recommend (per liter): 100 mmol of Tris buffer (pH 8.2), 4.0 mmol of L- leucylglycylglycine , 10 kU of leucine dehydrogenase, 3.8 mmol of NAD+, and 85 mumol of amastatin . The assay is suited to modern enzyme analyzers and has high precision.

Adult↗

Intestinal alkaline phosphatase linked to immunoglobulin G of the kappa type.

An electrophoretically slow-moving alkaline phosphatase(orthophosphoric-monoester phosphohydrolase, EC 3.1.3.1, alkaline optimum, ALP) isoenzyme was found in the serum of a patient with osteomalacia. Molecular mass of this ALP was estimated to be 500 000 daltons. Inhibitor studies revealed that the abnormal ALP, which formed a macromolecular complex, was an intestinal isoenzyme. Immunofixation following electrophoresis demonstrated that the macromolecular ALP was a complex composed of intestinal ALP and immunoglobulin G of the kappa type. This isotype specificity of immunoglobulin suggested that the ALP immunoglobulin complex is a specific antigen-antibody complex in circulation.

Aged↗

Cytotoxic action of prostaglandin D2 on mouse neuroblastoma cells.

Addition to the culture medium of prostaglandin (PG) D2 resulted in the degeneration in a dose- and time-dependent manner of N18TG-2 cells cloned from mouse neuroblastoma. The ED50 for PGD2-induced cytotoxicity was about 10 microM. The degenerative changes were irreversible when the cells were exposed for more than 10 h. Scanning and transmission electron microscopic examination revealed that treatment with PGD2 resulted in appearance of numerous blebs of various sizes along the cell surface and also in destruction of surface membrane and of cytoplasmic organelles. Tumor weight of N18TG-2 neuroblastoma inoculated subcutaneously on the backs of A/J mice was about 35-70% less than that of controls after 14 days of single daily i.p. or s.c. injections of 0.5-1 mg/kg of PGD2. The results indicate that PGD2 has growth-inhibitory effects on mouse neuroblastoma cells in vitro and in vivo.

Animals↗

Structural polymorphism of murine factor B controlled by a locus closely linked to the H-2 complex and demonstration of multiple alleles.

New alleles of murine factor B (Bf) protein were demonstrated. When ethylenediaminetetraacetic acid (EDTA)-plasmas from inbred and wild mice were analyzed by isoelectrofocusing (IEF) and immunofixation, murine Bf proteins were visualized as distinct protein bands in all mice tested. Four variants of murine Bf could be demonstrated in a large number of tested mice: Bf 1 (isoelectrofocusing point (P.I.) range of 5.8-6.1) exemplified by B10 and B10.BR, Bf 2 (P.I. range of 5.8-6.0) exemplified by B10.MOL (OHM), Bf 3 (P.I. range of 5.6-5.9) exemplified by B10.MOL (TEN2) and Mus musculus (Mus m.) subspecies Chc, Bf 4 (P.I. range of 6.0-6.3) exemplified by Mus m. subspecies Shh. The genetic linkage between S locus and Bf locus was studied with two backcross progenies--[B10.BR X (B10.BR X Mus m. subspecies Chc)F1] and [B10.BR X (B10.BR X Mus m. subspecies Shh)F1]. Totally, 256 backcross progenies were typed for Bf type and for Ss type (plasma level of the fourth complement protein regulated by S locus). The results indicated that murine Bf was controlled by a single codominant locus located close to the H-2 complex because no mouse showing recombination between Bf locus and S locus was found.

Alleles↗

Effects of branched chain amino acid infusion on glucose metabolism in cirrhotic patients with encephalopathy.

An amino acid solution enriched in branched chain amino acids (BCAA) was administered to cirrhotic patients with encephalopathy and serial determinations of serum glucose, IRI and IRG were performed. Slight decrease of serum glucose was observed when only BCAA was given. On the other hand, when BCAA was infused with glucose, the serum glucose level decreased significantly after infusion (-77.5 +/- 26.2 mg/dl, p less than 0.01) and two cases of hypoglycemic shock were observed. Although both serum insulin and glucagon increased in these cases, the IRI/IRG molar ratio which was 8.9 at the start of infusion increased to 20.6 at the end of infusion. It was suggested that administration of BCAA with glucose caused hypoglycemia in cirrhotics with encephalopathy, possibly by synergistic action of BCAA and glucose on serum insulin level.

Amino Acids↗

Genetic regulation of GM2 expression in liver of mouse.

GM2 containing NeuGc was found to be a major ganglioside in the liver of most inbred strains of mouse we have examined so far. They were DBA/2, C3H/He, C57BL/6, BALB/c, and CBA mice. However, WHT/Ht mouse does not contain a detectable amount of GM2 (NeuGc) but has GM3 containing NeuGc as the major ganglioside in the liver. The positive expression of GM2 (NeuGc) was demonstrated in the liver of F1 hybrids between WHT/Ht and DBA/2 mice, as one of the possible combinations. Moreover, the expression of GM2 (NeuGc) in the liver was proved to be an autosomal dominant trait by ganglioside analysis of 34 individual mice of the F2 and backcross generations. WHT/Ht mouse was demonstrated to be a recessive homozygote lacking GM2 (NeuGc) expression. During the analysis, interestingly enough, the enhanced elongation of the sugar chain in the gangliosides from GM2 (NeuGc) to GM1 (NeuGc) and GD1 was observed in the liver of F1 mice and this elongation was segregated only in half members of F2 and backcross generations.

Animals↗