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Titolo:
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
Autore:
Bilmen, JG; Khan, SZ; Javed, MUH; Michelangeli, F;
Indirizzi:
Univ Birmingham, Sch Biosci, Birmingham, W Midlands, England Univ Birmingham Birmingham W Midlands England ngham, W Midlands, England Shifa Coll Med, Islamabad, Pakistan Shifa Coll Med Islamabad PakistanShifa Coll Med, Islamabad, Pakistan
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 23, volume: 268, anno: 2001,
pagine: 6318 - 6327
SICI:
0014-2956(200112)268:23<6318:IOTSCP>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
+ MG-2+-ACTIVATED ATPASE; SARCOPLASMIC-RETICULUM; PLATELET-AGGREGATION; BLOOD-PLATELETS; FOOD SPICE; CELLS; CALCIUM; APOPTOSIS; SITES; MECHANISM;
Keywords:
SERCA; ATP binding; curcumin; phosphorylation; fluorescence;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Michelangeli, F Univ Birmingham, Sch Biosci, Birmingham, W Midlands, England Univ Birmingham Birmingham W Midlands England s, England
Citazione:
J.G. Bilmen et al., "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", EUR J BIOCH, 268(23), 2001, pp. 6318-6327

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 muM. 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 (<10 <mu>M). For the skeletal muscle isoform of the Ca2+ pump (SERCA1), the inhibition of curcumin is noncompetitive with respect to Ca2+, and competitive with respect to ATP at high curcumin concentrations (approximate to 10-25 muM). This was confirmed by ATP binding studies that showed inhibition in the presence of curcumin: ATP-dependentphosphorylation was also reduced. Experiments with fluorescein 5'-isothiocyanate (FITC)-labelled ATPase also suggest that curcumin stabilizes the El conformational state. The fact that FITC labels the nucleotide binding siteof the ATPase (precluding ATP from binding), and the fact that curcumin affects FITC fluorescence indicate that curcumin must be binding to another site within the ATPase that induces a conformational change to prevent ATP from binding. This observation is interpreted, with the aid of recent structural information, as curcumin stabilizing the interaction between the nucleotide-binding and phosphorylation domains, precluding ATP binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 10:47:48