PubMed · 5866142
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J Huxley, E Mayr, H Osmond. 1965-06-12. Schizophrenia.. https://doi.org/10.1038/2061112a0
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This study investigated the effect of carbazochrome sodium sulphonate (AC-17) on the accumulation of tissue-type plasminogen activator antigen (t-PA:Ag) and plasminogen activator inhibitor-1 antigen (PAI-1:Ag) in culture medium of human umbilical vein endothelial cells (HUVEC). HUVEC were cultured in the presence of AC-17, and the concentration of t-PA:Ag and PAI-1:Ag in the medium was measured by an enzyme-linked immunoassay. AC-17, after 48 and 72 h incubation, significantly decreased the t-PA:Ag in the culture medium, while it had no significant effect on the PAI-1:Ag. The result of fibrin zymography was consistent with the result obtained by ELISA. It also revealed that all of the t-PA present in the culture medium formed complexes with PAI-1, indicating that AC-17 did not interfere with t-PA/PAI-1 complex formation. Furthermore, AC-17 did not inhibit the activities of t-PA and plasmin when measured by a fibrin plate method. These results suggest that AC-17 may modulate the fibrinolytic balance of blood through changing the function of endothelial cells, a new aspect of action of AC-17 as a haemostatic drug.
The effects of adrenochrome and epinephrine were investigated in cultured human umbilical arterial endothelial cells. The cells were exposed to either adrenochrome or epinephrine at levels of 50 and 200 microM, respectively, up to 24 hrs. At 3, 5, 7 and 24 hrs of the designed harvesting time, [3H]thymidine incorporation, protein content, [3H]cholesterol uptake, prostacyclin production and lipid peroxidation were measured. We found that adrenochrome at a level of 200 microM inhibited [3H]thymidine incorporation, decreased protein content, stimulated [3H]cholesterol uptake, and decreased prostacyclin production after 3, 5, 24 and 5 hrs of exposure, respectively, compared with control. It took 24 hrs however for epinephrine at a level of 200 microM to inhibit [3H]thymidine incorporation and prostacyclin production. When the concentration was reduced to 50 microM, only adrenochrome inhibited [3H]thymidine incorporation after 24 hrs of treatment. Both adrenochrome and epinephrine had no effect on lipid peroxidation. We suggest that atherogenic changes found in severe hypertension may be due to abnormal high concentration of epinephrine, especially oxidized epinephrine, on endothelial cell functions, such as DNA synthesis, cholesterol uptake and prostacyclin production.
Binding of [3H]serotonin and [3H]dopamine to serotonin-binding proteins (SBP) from soluble extracts of bovine frontal cortex is increased by Fe2+. This group recently attributed this effect of Fe2+ to its ability to enhance the oxidation of [3H]serotonin and [3H]dopamine in the presence of dissolved molecular oxygen, and to the ability of the formed oxidation products to bind covalently to cysteine residues of SBP. In this study it is shown that the binding of both ligands is potently inhibited by dopamine as well as by several catecholamine-and serotonin-related neurotoxins: adrenochrome, 5,6-dihydroxytryptamine, 5,7-dihydroxytryptamine, 6-hydroxydopamine and 6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline. In contrast, serotonin can only potently inhibit part (36%) of the [3H]dopamine binding, while 1,2,3,4-tetrahydroisoquinoline is only a weak competitor for both ligands. Potent inhibition by the toxins is associated with the presence of electrophilic centres at the aromatic ring, either of the products themselves (adrenochrome) or of their oxidation products (all other competitors). These findings suggest that "SBP" represent an important target for the Fe(2+)-mediated binding of [3H]-serotonin, [3H]dopamine and related neurotoxins.