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- W1964692821 abstract "In view of the importance of P i in the control of cell metabolism, it was of interest to study the mechanism and regulation of P i uptake by ascites tumor cells. For this purpose, the incorporation of 32 P i into Ehrlich Lettré cells was compared when competitive anions and inhibitors which alter cation movements were present. Anions such as sulfanilate (35 m m ) and succinate (30 m m ) decrease 32 P i uptake by ca. 35%, suggesting that transport is mediated by a protein similar to the 100,000 M r anion carrier isolated from erythrocyte membranes. Furosemide, a diuretic which bears a structural analogy to sulfanilate inhibitors of anion transport, also decreases 32 P i incorporation at concentrations as low as 2 × 10 −5 m . This inhibitor blocks cation exchange in ascites tumor cells, and from the present data, it is suggested that a possible function of the furosemidesensitive cation exchange protein is to facilitate anion transport. Ouabain, known to inhibit (Na + + K + )-ATPase and its dephosphorylation, stimulates the rate of incorporation of 32 P i into cells and also raises the net inorganic phosphate level. The stimulation of 32 P i incorporation is decreased by sulfanilate or succinate. In contrast to the effects of ouabain, addition of 10 m m K + , which is known to stimulate (Na + + K + )-ATPase and its dephosphorylation, decreases 32 P i incorporation. These observations suggest that anion transport and energy-dependent Na + and K + movements may be closely coupled to the intact cell." @default.
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- W1964692821 date "1977-03-01" @default.
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- W1964692821 title "Phosphate transport and its relationship to cation movements in Ehrlich Lettré ascites tumor cells" @default.
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- W1964692821 doi "https://doi.org/10.1016/0003-9861(77)90128-x" @default.
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