Alcohols are inhibitors of Saccharomyces cerevisiae multidrug-resistance pumps Pdr5p and Snq2p

Abstract The effect of alcohols on cell membrane proteins has originally been assumed to be mediated by their primary action on membrane lipid matrix. Many studies carried out later on both animal and yeast cells have revealed that ethanol and other alcohols inhibit the functions of various membrane...

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Bibliographic Details
Published in:	FEMS yeast research Vol. 13; no. 8; pp. 782 - 795
Main Authors:	Gášková, Dana, Plášek, Jaromír, Zahumenský, Jakub, Benešová, Ivana, Buriánková, Ľuboslava, Sigler, Karel
Format:	Journal Article
Language:	English
Published:	Oxford, UK Blackwell Publishing Ltd 01-12-2013 Oxford University Press
Subjects:	Adenosine Triphosphate - metabolism Alcohol Alcohols Alcohols - pharmacology ATP-Binding Cassette Transporters - antagonists & inhibitors ATP-Binding Cassette Transporters - genetics ATP-Binding Cassette Transporters - metabolism Cell Membrane Permeability - drug effects Cell membranes Drug Resistance, Fungal - genetics Ethanol fluorescent probe diS‐C3 Hexanol Ions - metabolism Membrane channels membrane potential Membrane proteins Microbial Sensitivity Tests Multidrug resistant organisms Mutants Propanol Proteins pump inhibitor Saccharomyces cerevisiae Saccharomyces cerevisiae - drug effects Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - antagonists & inhibitors Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Structure-function relationships yeast MDR pump fluorescent probe diS-C yeast MDR pump alcohols pump inhibitor 3 membrane potential fluorescent probe diS-C3
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Summary:	Abstract The effect of alcohols on cell membrane proteins has originally been assumed to be mediated by their primary action on membrane lipid matrix. Many studies carried out later on both animal and yeast cells have revealed that ethanol and other alcohols inhibit the functions of various membrane channels, receptors and solute transport proteins, and a direct interaction of alcohols with these membrane proteins has been proposed. Using our fluorescence diS-C3(3) diagnostic assay for multidrug-resistance pump inhibitors in a set of isogenic yeast Pdr5p and Snq2p mutants, we found that n-alcohols (from ethanol to hexanol) variously affect the activity of both pumps. Beginning with propanol, these alcohols have an inhibitory effect that increases with increasing length of the alcohol acyl chain. While ethanol does not exert any inhibitory effect at any of the concentration used (up to 3%), hexanol exerts a strong inhibition at 0.1%. The alcohol-induced inhibition of MDR pumps was detected even in cells whose membrane functional and structural integrity were not compromised. This supports a notion that the inhibitory action does not necessarily involve only changes in the lipid matrix of the membrane but may entail a direct interaction of the alcohols with the pump proteins.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1
ISSN:	1567-1356 1567-1364
DOI:	10.1111/1567-1364.12088