Interaction of sanguinarine and its dihydroderivative with the Na+/K+-ATPase. Complex view on the old problem

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F10%3A10212344" target="_blank" >RIV/61989592:15310/10:10212344 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15110/10:10212344

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Interaction of sanguinarine and its dihydroderivative with the Na+/K+-ATPase. Complex view on the old problem

Popis výsledku v původním jazyce

The effects of sanguinarine (SG) and its metabolite dihydrosanguinarine (DHSG) on Na+/K+-ATPase were investigated using fluorescence spectroscopy. The results showed that the enzyme in E1 conformation can bind both charged and neutral (pseudobase) formsof SG with a KD = 7.2+-2.0Mor 11.7+-0.9M, while the enzyme in E2 conformation binds only the charged form of SG with a KD = 4.7+-1.1M. Fluorescence quenching experiments suggest that the binding site in E1 conformation is located on the surface of the enzyme for both forms but the binding site in E2 conformation is protected from the solvent. We found no evidence for interaction of Na+/K+-ATPase and DHSG. This implies that any in vivo effect of SG attributable to inhibition of Na+/K+-ATPase can be considered only prior to SG?DHSG transformation in the gastro-intestinal tract and/or blood. Hence, Na+/K+-ATPase inhibition will be effective in SG topical application but its duration will be very limited in SG oral or parenteral administrat

Název v anglickém jazyce

Interaction of sanguinarine and its dihydroderivative with the Na+/K+-ATPase. Complex view on the old problem

Popis výsledku anglicky

The effects of sanguinarine (SG) and its metabolite dihydrosanguinarine (DHSG) on Na+/K+-ATPase were investigated using fluorescence spectroscopy. The results showed that the enzyme in E1 conformation can bind both charged and neutral (pseudobase) formsof SG with a KD = 7.2+-2.0Mor 11.7+-0.9M, while the enzyme in E2 conformation binds only the charged form of SG with a KD = 4.7+-1.1M. Fluorescence quenching experiments suggest that the binding site in E1 conformation is located on the surface of the enzyme for both forms but the binding site in E2 conformation is protected from the solvent. We found no evidence for interaction of Na+/K+-ATPase and DHSG. This implies that any in vivo effect of SG attributable to inhibition of Na+/K+-ATPase can be considered only prior to SG?DHSG transformation in the gastro-intestinal tract and/or blood. Hence, Na+/K+-ATPase inhibition will be effective in SG topical application but its duration will be very limited in SG oral or parenteral administrat

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2010

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Toxicology Letters

ISSN

0378-4274

e-ISSN

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Svazek periodika

2010

Číslo periodika v rámci svazku

196

Stát vydavatele periodika

IE - Irsko

Počet stran výsledku

4

Strana od-do

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Kód UT WoS článku

000278754100008

EID výsledku v databázi Scopus

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