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• W2023202017 abstract "The effect of Ca2+-binding protein regucalcin on Ca2+-ATPase activity in isolated rat liver microsomes was investigated. The presence of regucalcin (0.1–1.0 μM) in the enzyme reaction mixture led to a significant increase in Ca2+-ATPase activity. Regucalcin significantly stimulated ATP-dependent 45Ca2+ uptake by the microsomes. Thapsigargin (10−6 M), a specific inhibitor of microsomal Ca2+ pump enzyme (Ca2+-ATPase), clearly inhibited regucalcin (0.5 μM)-increased microsomal Ca2+-ATPase activity. Liver microsomal Ca2+-ATPase activity was markedly decreased by N-ethylmaleimide (NEM; 2.5 mM), while the activity was clearly elevated by dithiothreitol (DTT; 2.5 mM), indicating that the sulfhydryl (SH) group of the enzyme is an active site. The effect of regucalcin (0.5 μM) in increasing Ca2+-ATPase activity was completely inhibited by the presence of NEM (2.5 mM) or digitonin (10−2 %), a solubilizing reagent of membranous lipids. Moreover, the effect of regucalcin on enzyme activity was seen in the presence of Ca2+ ionophore (A23187; 10−7 M). The present study demonstrates that regucalcin can stimulate Ca2+ pump activity in rat liver microsomes, and that the protein may act the SH groups of microsomal Ca2+-ATPase. J. Cell. Biochem. 74:663–669, 1999. © 1999 Wiley-Liss, Inc." @default.
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• W2023202017 date "1999-09-15" @default.
• W2023202017 modified "2023-09-23" @default.
• W2023202017 title "Role of regucalcin as an activator of Ca2+-ATPase activity in rat liver microsomes" @default.
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• W2023202017 doi "https://doi.org/10.1002/(sici)1097-4644(19990915)74:4<663::aid-jcb15>3.0.co;2-2" @default.
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