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

Result code in 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>

Alternative codes found

RIV/61989592:15110/10:10212344

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

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

Original language description

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

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

BO - Biophysics

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

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

Publication year

2010

Confidentiality

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

Name of the periodical

Toxicology Letters

ISSN

0378-4274

e-ISSN

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Volume of the periodical

2010

Issue of the periodical within the volume

196

Country of publishing house

IE - IRELAND

Number of pages

4

Pages from-to

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UT code for WoS article

000278754100008

EID of the result in the Scopus database

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