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Biomedical subjects

M Goldstein

Publications and source records attributed to M Goldstein.

At least 775 records · Page 43Linked to original sources
PubMed1972

Dopamine- -hydroxylase activity in mouse neuroblastoma tumors and in cell cultures.

Dopamine-beta-hydroxylase activity is present in mouse neuroblastoma C-1300 tumors. The activity is proportional to the weight of the tumor. Serum activity is markedly increased in mice that bear the tumors. Treatment of mice with 5-bromodeoxyuridine causes marked inhibition of tumor growth and decrease of dopamine-beta-hydroxylase activity in the serum. The histochemical studies reveal that 1-5% of the cells in mouse C-1300 neuroblastoma tumors contain catecholamines and that catecholamine-containing processes terminate mainly around blood vessels of the tumor. Dopamine-beta-hydroxylase is present in clonal neuroblastoma cell lines. The cell line with the greater tendency to form axon-like processes has a higher activity of this enzyme.

Animals↗
PubMed1972

Tyrosine hydroxylase in human adrenal and pheochromocytoma: localization, kinetics, and catecholamine inhibition.

The properties of partially purified tyrosine hydroxylase from six pheochromocytomas were compared with partially purified normal human and bovine adrenal medulla enzyme. Substrate and inhibition kinetics, cofactor requirements, and intracellular localization of the enzyme from normal and tumor chromaffin tissue of humans were similar, as was the amount of enzyme activity per gram of tissue. Contrary to previous reports, the sensitivity to catecholamine inhibition of the pheochromocytoma enzyme from the six tumors studied was similar to that of both human and bovine adrenal medulla tyrosine hydroxylase. These results suggest that the excessive synthesis and secretion of catecholamines in some pheochromocytomas is not the result of a reduced sensitivity of tyrosine hydroxylase to catecholamine inhibition.

Adrenal Medulla↗