Effects of lanthanum on the heart sarcolemmal ATPase and calcium binding activities

Abstract

Effects of lanthanum on Ca2+-ATPase, Mg2+-ATPase, Na+–K+-ATPase, and calcium binding activities were studied in rat heart sarcolemma. Ten to 100 μM lanthanum depressed significantly the Ca2+-ATPase activity and 50–200 μM lanthanum inhibited the calcium binding activity. Lineweaver–Burk plots of the Ca2+-ATPase activity showed that the inhibition by lanthanum was competitive with calcium concentration. Neither Mg2+-ATPase nor Na+–K+-ATPase activities were affected by lanthanum when the assay medium contained 1 mM EDTA; however, in the absence of EDTA, these enzyme activities were significantly decreased by 10–100 μM lanthanum. Rat hearts perfused with HEPES buffer containing 0.5 mM lanthanum showed electron-dense deposits restricted to the outer cell surface and the sarcolemma obtained from these hearts also had the deposits, indicating that the membrane fraction isolated by the hypotonic shock – LiBr treatment method is of sarcolemmal origin. The Ca2+-ATPase activity of the sarcolemma isolated from lanthanum-perfused hearts, unlike the Mg2+-ATPase, Na+–K+-ATPase, and calcium binding activities, was significantly less than the control value. From these observations it is suggested that lanthanum may influence calcium movement across the sarcolemma by affecting sarcolemmal ATPase and calcium binding activities.