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Y Inui

Publications and source records attributed to Y Inui.

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Morphological and biochemical studies on the heart of the cardiomyopathic Syrian hamster.

Histological and ultrastructural observations of embryonic hearts and cultured cells from hamsters with inherited cardiomyopathy (BIO 14.6 line) showed a significant delay in maturation of the sarcomeric units in comparison with those of unrelated healthy control hamsters. Phase-contrast microscopic observation of the cultured cardiomyocytes revealed more rapid diminution of beating frequencies in the diseased hamsters than in the controls. Negatively stained ultrastructure and yield of the actomyosin extracted both from the cardiomyopathic and the control hamsters showed no fundamental differences. Disc electrophoresis of the erythrocyte ghosts revealed, at least, a quantitative difference in one of the composing proteins between these two groups.

Actomyosin

[Hematemesis].

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Gastrointestinal Diseases

Discrimination of single transport systems. The Na plus-sensitive transport of neutral amino acids in the Ehrlich cell.

Uptake of methionine, alpha-aminoisobutyric acid, and alpha-(methyl-amino)-isobutyric acid has been shown to occur by at least two transport systems, one sensitive and the other insensitive to the Na(+) concentration. For alpha-aminoisobutyric acid and its N-methyl derivative, the Na(+)-insensitive uptake is not concentrative and its rate increases almost linearly with concentration within the range examined. In contrast, the Na(+)-insensitive uptake of methionine is concentrative and subject to inhibition by such amino acids as phenylalanine, leucine, and valine, although not in a manner to indicate that the uptake is mediated by a single agency. This component is not produced by a residual operation of the Na(+)-requiring transport system, handicapped by the absence of Na(+) or by its having combined with alpha-aminoisobutyric acid. The increase in the rate of methionine uptake is linear with concentration only above about 16 mM methionine. The Na(+)-sensitive uptakes of methionine, alpha-aminoisobutyric, and alpha-(methylamino)-isobutyric acid appear to occur by the same population of transport-mediating sites. Both K(m) and V(max) of the Na(+)-sensitive uptake of these three amino acids change with changes in the concentration of Na(+), an effect which is shown to have a theoretical basis. A similarity in the values of Vmax for ten amino acids entering principally by the Na(+)-sensitive agency indicates that differences in their K(m) values probably measure differences in their affinities for that transport-mediating system.

Aminoisobutyric Acids

Cardiomyopathy in vitro.

Phase contrast microscopy of cultured embryonic heart cells showed the beating frequency decreased more rapidly and the regularity the rhythm of of the beating cells was lost sooner in heart cells from cardiomyopathic hamsters than from the control hamsters. Studies of cultured heart cells by differential interference contrast (with Nomarski's prism) and by electron microscopy revealed a significant impediment in the maturation of the sarcomeric units in the diseased animals compared to controls. The incorporation of [14C] leucine into acid-insoluble fractions was studied, and no significant difference in incorporation between the two groups was found. An analysis of polyacrylamide gel electrophoresis revealed the possible existence of a quantitative difference in one of the composing proteins of the erythrocyte membrane between the two groups. The protein kinase activity of ghosts from the control group was more sensitive to cAMP than that from the diseased animals. In addition, the binding of [3H] cAMP to the ghost was almost identical between the two. The morphological and biochemical observations lead one to the plausible supposition that there are some differences in the interaction of the so-called catalytic and regulatory subunits between the two groups and that there is an impairment of the higher arrangement of myofibrils from their building blocks in the diseased hamster. The significance of the existence of abundant corpuscles resembling neurosecretory granules was not established by this study. They may have an etiological significance or they may be related to a disturbed function in the cultured cells of the cardiomyopathic hamster.

Animals

Active immunization of human cancer with tumor cell-associated carbohydrate antigen.

The peanut agglutinin (PNA) receptors isolated from a tumor cell line could elicit antitumor activity by an active immunization. We report here the results of active immunization with a human PNA receptor glycoprotein on the tumor progression of cancer patients. A remarkable regression of cancer and a prolonged life span in patients were obtained after active immunization with a tumor cell-associated carbohydrate antigen.

Antibodies, Monoclonal

Characterization of cytochrome P-450 2B6 in human liver microsomes.

A cytochrome P-450 (P-450) enzyme of the CYP2B subfamily was partially purified from human liver microsomes and characterized with respect to immunochemical properties, N-terminal amino acid sequence, and catalytic activities toward typical P-450 substrates. P-450 enzymes were monitored in chromatographic fractions by immunoblotting analysis using antibodies raised against a monkey P-450 2B, as well as several purified human P-450 enzymes. The final P-450 2B preparation thus obtained was contaminated with P-450 3A4, but an N-terminal amino acid sequence matching the sequence predicted from the CYP2B6 cDNA was obtained. The apparent M(r) of this protein was 48 kDa, and the migration on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was the same as that of the P-450 2B6 protein expressed in a human lymphoblast cell line. Immunoblotting analysis of 50 human liver samples revealed that the protein band considered to be P-450 2B6 was detected in only 12 samples, with four of these having relatively high levels. Several activities toward typical P-450 substrates were determined in a reconstituted monooxygenase system containing partially purified P-450 2B6 and compared with those obtained using a highly purified preparation of P-450 3A4 enzyme; we found that most of the activities were similar in these preparations, except that the partially purified P-450 2B6 showed high rates of activation of the mutagens 6-aminochrysene and 3-methoxy-4-aminoazobenzene to genotoxic metabolites in Salmonella typhimurium NM2009 strain.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence