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Biomedical subjects

M Matsuda

Publications and source records attributed to M Matsuda.

At least 1,369 records · Page 76Linked to original sources

Morphologic and biochemical characteristics of human kidney cells in vitro.

In vitro cultivated cells derived from normal human renal cortex were characterized morphologically and biochemically. Although the epithelial monolayer was composed of heterogeneous cells, it included cells with a surface structure similar to microvilli as well as some resembling the desmosome between neighboring cells. Enzymatic studies revealed a marked decrease in alkaline phosphatase activity, and the activity of gamma-glutamyl transpeptidase was also reduced to about one-fifth of that in the original tissue. The electrophoretic mobility of the enzyme was not identical with that of normal kidney or of the novel enzyme in renal neoplastic tissue. Lactate dehydrogenase activity was similar to that of normal kidney tissue but the isozyme pattern was completely inverted. These cells responded to the addition of 10 ng per ml of parathyroid hormone in culture medium and there was a 33 fold increase in intracellular cyclic adenosine monophosphate. Estrogen specific binding protein was not detectable in the monolayer cells. These results clearly indicated that the biologic transformation observed in the cultivated normal cells was not attributable to simple fetalism or dedifferentiation, but was a more complicated process.

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Gamma-glutamyl transpeptidase in a newly established cell line from human renal carcinoma, OUR-10.

A newly established cell line, OUR-10, from human renal carcinoma seems to have the same gamma-glutamyl transpeptidase as the novel one which was found recently in renal carcinoma tissue; the enzymic properties such as electrophoretic mobility, Km value, molecular weight, thermostability, the effects of urea, sodium dodecyl sulfate and sulfhydryl reagents, the effects of amino acids, cations and EDTA, and the binding behavior to a concanavalin A-Sepharose column were the same as those of the novel gamma-glutamyl transpeptidase found in renal carcinoma tissue. The immunological properties of the gamma-glutamyl transpeptidase (GGTP) of OUR-10 examined by inhibition tests and tests of cross-reactivity with anti-normal kidney GGTP antibody were also the same as those of the novel gamma-glutamyl transpeptidase. These results may mean that the novel gamma-glutamyl transpeptidase originates from the cancer cells, and can be used as a marker for identification of this cell line, OUR-10.

Adult↗