Inhibition of the SERCA Ca2+ pumps by curcumin. Curcumin putatively stabilizes the interaction between the nucleotide-binding and phosphorylation domains in the absence of ATP.

Jonathan Bilmen, SZ Khan, MH Javed, Francesco Michelangeli

Research output: Contribution to journalArticle

125 Citations (Scopus)

Abstract

Curcumin is a compound derived from the spice, tumeric. It is a potent inhibitor of the SERCA Ca2+ pumps (all isoforms), inhibiting Ca2+-dependent ATPase activity with IC50 values of between 7 and 15 microm. It also inhibits ATP-dependent Ca2+-uptake in a variety of microsomal membranes, although for cerebellar and platelet microsomes, a stimulation in Ca2+ uptake is observed at low curcumin concentrations (
Original languageEnglish
Pages (from-to)6318-27
Number of pages10
JournalEuropean Journal of Biochemistry
Volume268
Issue number23
DOIs
Publication statusPublished - 1 Dec 2001

Keywords

  • fluorescence
  • phosphorylation
  • curcumin
  • SERCA
  • ATP binding

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