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Trehalose, the disaccharide of glucose, inhibits both initial rate and maximal capacity of ATP-dependent Ca 2+  transport in inside-out vesicles of basolateral membrane from kidney proximal tubules. This inhibition (I 0.5  = 60 mᴍ) cannot be attributed to an increase in Ca 2+  permeability, since the rate of EGTA-stimulated Ca 2+  efflux from preloaded vesicles is not modified by trehalose. In the presence of 600 mᴍ trehalose, Ca 2+  uptake was almost completely inhibited, but the Ca 2+ -stimulated ATPase activity was unaffected; thus trehalose uncouples the Ca 2+  transport from the ATPase activity. The Ca 2+  transport inhibition by trehalose is reversible, since the inhibition disappeared when the vesicles were pre-incubated with 600 mᴍ trehalose and then diluted in reaction medium to measure Ca 2+  accumulation. Other mono- and disaccharides such as glucose, fructose, galactose, sucrose, maltose and lactose were tested but were not so effective as trehalose. The uncoupling of Ca 2+  transport from hydrolysis can be explained by an interaction of trehalose with the phospholipid environment of the enzyme that induces conformational changes in specific domains of the enzyme so as to impair the coupling process.

Uncoupling by Trehalose of Ca 2+ Transport and ATP Hydrolysis by the Plasma Membrane (Ca 2+ +Mg 2+ ) ATPase of Kidney Tubules