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Titolo:
DISSOCIATION OF PHOSPHOLAMBAN REGULATION OF CARDIAC SARCOPLASMIC-RETICULUM CA2+ ATPASE BY QUERCETIN
Autore:
MCKENNA E; SMITH JS; COLL KE; MAZACK EK; MAYER EJ; ANTANAVAGE J; WIEDMANN RT; JOHNSON RG;
Indirizzi:
MERCK RES LABS,DEPT PHARMACOL,WP44-B124 W POINT PA 19486
Titolo Testata:
The Journal of biological chemistry
fascicolo: 40, volume: 271, anno: 1996,
pagine: 24517 - 24525
SICI:
0021-9258(1996)271:40<24517:DOPROC>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
CALCIUM-UPTAKE; ADENOSINE 5'-TRIPHOSPHATE; FUNCTIONAL ASSOCIATION; BINDING; CA2+-ATPASE; MECHANISM; CA-2+-ATPASE; STIMULATION; MODULATION; PUMP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
E. Mckenna et al., "DISSOCIATION OF PHOSPHOLAMBAN REGULATION OF CARDIAC SARCOPLASMIC-RETICULUM CA2+ ATPASE BY QUERCETIN", The Journal of biological chemistry, 271(40), 1996, pp. 24517-24525

Abstract

Quercetin had a biphasic effect on Ca2+ uptake and calcium-stimulatedATP hydrolysis in isolated cardiac sarcoplasmic reticulum (SR). Stimulation of Ca(2+)ATPase was observed at low quercetin concentrations (<25 mu M) followed by inhibition at higher concentrations. The effects were dependent upon the SR protein concentration, the MgATP concentration, and intact phospholamban regulation of cardiac Ca(2+)ATPase. Onlythe inhibitory effects at higher quercetin concentrations were observed in skeletal muscle SR which lacks phospholamban and in cardiac SR treated to remove phospholamban regulation, Stimulation was additive with monoclonal antibody 1D11 (directed against phospholamban) at submaximal antibody concentrations; however, the maximal antibody and quercetin stimulation were identical. Quercetin increased the calcium sensitivity of the Ca(2+)ATPase like that observed with phosphorylation of phospholamban or treatment with monoclonal antibody 1D11. In addition, low concentrations of quercetin increased the steady-state formation of phosphoenzyme from ATP or P-i, but higher quercetin decreased phosphoenzyme levels. Quercetin, even under stimulatory conditions, was a competitive inhibitor of ATP, but ap pears to relieve the Ca(2+)ATPase from phospholamban inhibition, thereby, producing an activation. The subsequent inhibitory action of higher quercetin concentrations results from competition of quercetin with the nucleotide binding site of the Ca(2+)ATPase. The data suggest that quercetin interacts with the nucleotide binding site to mask phospholamban's inhibition of the SR Ca(2+)ATPase and suggests that phospholamban may interact at or near the nucleotide binding site.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 09:59:29