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001-es BibID:	BIBFORM050047
Első szerző:	Király Anna
Cím:	Hypoxia reduces the efficiency of elisidepsin by inhibiting hydroxylation and altering the structure of lipid rafts / Anna Király, Tímea Váradi, Tímea Hajdu, Ralph Rühl, Carlos M. Galmarini, János Szöllősi, Peter Nagy
Dátum:	2013
Megjegyzések:	The mechanism of action of elisidepsin (PM02734, Irvalec(R)) is assumed to involve membrane permeabilization via attacking lipid rafts and hydroxylated lipids. Here we investigate the role of hypoxia in the mechanism of action of elisidepsin. Culturing under hypoxic conditions increased the half-maximal inhibitory concentration and decreased the drug's binding to almost all cell lines which was reversed by incubation of cells with 2-hydroxy palmitic acid. The expression of fatty acid 2-hydroxylase was strongly correlated with the efficiency of the drug and inversely correlated with the effect of hypoxia. Number and brightness analysis and fluorescence anisotropy experiments showed that hypoxia decreased the clustering of lipid rafts and altered the structure of the plasma membrane. Although the binding of elisidepsin to the membrane is non-cooperative, its membrane permeabilizing effect is characterized by a Hill coefficient of ~3.3. The latter finding is in agreement with elisidepsin-induced clusters of lipid raft-anchored GFP visualized by confocal microscopy. We propose that the concentration of elisidepsin needs to reach a critical level in the membrane above which elisidepsin induces the disruption of the cell membrane. Testing for tumor hypoxia or the density of hydroxylated lipids could be an interesting strategy to increase the efficiency of elisidepsin
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban analysis Anisotropy article Biophysics cell biology Cell Line Cell Membrane Cells Confocal Confocal microscopy EXPRESSION Fluorescence FLUORESCENCE ANISOTROPY Hungary lipid raft LIPID RAFTS Lipids Microscopy Research Research Support Support
Megjelenés:	Marine Drugs. - 11 : 12 (2013), p. 4858-4875. -
További szerzők:	Váradi Tímea (1982-) (okleveles vegyész) Hajdu Tímea (1991-) (biomérnök) Rühl, Ralph (1969-) (vegyész) Galmarini, Carlos M. Szöllősi János (1953-) (biofizikus) Nagy Péter (1971-) (biofizikus)
Internet cím:	DOI Szerző által megadott URL Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM067230
035-os BibID:	(Cikkazonosító)41376 (WOS)000393137000001 (Scopus)85011264087
Első szerző:	Tarapcsák Szabolcs (Molekuláris biológus)
Cím:	Interactions of retinoids with the ABC transporters P-glycoprotein and Breast Cancer Resistance Protein / Szabolcs Tarapcsák, Gábor Szalóki, Ágnes Telbisz, Zsuzsanna Gyöngy, Krisztina Matúz, Éva Csősz, Péter Nagy, Imre J. Holb, Ralph Rühl, László Nagy, Gábor Szabó, Goda Katalin
Dátum:	2017
ISSN:	2045-2322
Megjegyzések:	Retinoids - derivatives of vitamin A - are important cell permeant signaling molecules that regulate gene expression through activation of nuclear receptors. P-glycoprotein (Pgp) and ABCG2 are plasma membrane efflux transporters affecting the tissue distribution of numerous structurally unrelated lipophilic compounds. In the present work we aimed to study the interaction of the above ABC transporters with retinoid derivatives. We have found that 13-cis-retinoic acid, retinol and retinyl-acetate inhibited the Pgp and ABCG2 mediated substrate transport as well as the substrate stimulated ATPase activity of these transporters. Interestingly, 9-cis-retinoic acid and ATRA (all-trans retinoic acid), both are stereoisomers of 13-cis-retinoic acid, did not have any effect on the transporters' activity. Our fluorescence anisotropy measurements revealed that 13-cis-retinoic acid, retinol and retinyl-acetate selectively increase the viscosity and packing density of the membrane. Thus, the mixed-type inhibition of both transporters by retinol and ABCG2 by 13-cis-retinoic acid may be the collective result of direct interactions of these retinoids with the substrate binding site(s) and of indirect interactions mediated by their membrane rigidifying effects.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk retinoid derivatives P-glycoprotein ABCG2 ABC transporter membrane fluidity intramembrane localization
Megjelenés:	Scientific Reports. - 7 : 41376 (2017), p. 1-31. -
További szerzők:	Szalóki Gábor (1986-) (molekuláris biológus) Telbisz Ágnes Gyöngy Zsuzsanna (1991-) (molekuláris biológus) Matúz Krisztina (1980-) (vegyész, biokémikus) Csősz Éva (1977-) (biokémikus, molekuláris biológus) Nagy Péter (1971-) (biofizikus) Holb Imre (1973-) (agrármérnök) Rühl, Ralph (1969-) (vegyész) Nagy László (1966-) (molekuláris sejtbiológus, biokémikus) Szabó Gábor (1953-) (biofizikus) Goda Katalin (1969-) (biofizikus)
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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