Linked Life Data

8384787

Source:http://linkedlifedata.com/resource/pubmed/id/8384787

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pubmed-article:8384787pubmed:abstractTextCytochrome P-450 has been proposed to underlie the mechanism of regulation of the plasma membrane Ca2+ permeability by the Ca2+ content of the inositol 1,4,5-trisphosphate-sensitive Ca2+ pool. We have investigated the effects on divalent cation uptake in rat thymic lymphocytes of three structurally related imidazole reagents reported to inhibit redox mechanisms. Changes in intracellular Ca2+ concentration and intracellular Mn2+ concentration were measured fluorimetrically with indo-1 and/or quin-2. Econazole, miconazole, and SKF 96365 were found to be potent blockers of Ca2+ and Mn2+ uptake activated by release of Ca2+ from intracellular stores induced by thapsigargin. Additionally, we found that concentrations of these agents required to abolish divalent cation uptake also released Ca2+ from the thapsigargin-sensitive intracellular stores, consistent with inhibition of the endosomal Ca(2+)-ATPase. In agreement with this suggestion, we have found that all three of these agents are potent inhibitors of isolated sarcoplasmic reticulum Ca(2+)-ATPase. We conclude that econazole, miconazole, and SKF 96365 inhibit cytochrome P-450-independent filling of intracellular Ca2+ pools, as well as store-regulated Ca2+ entry, and caution against the use of these compounds as selective inhibitors of cytochrome P-450.lld:pubmed
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pubmed-article:8384787pubmed:articleTitleInhibition of Ca2+ transport pathways in thymic lymphocytes by econazole, miconazole, and SKF 96365.lld:pubmed
pubmed-article:8384787pubmed:affiliationDepartment of Physiology, Tulane University, New Orleans, Louisiana 70112.lld:pubmed
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pubmed-article:8384787pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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