Evidence map›Paper›PMID 26026069›Full record

ArticleJournal of lipid research2015

α-Tocopherols modify the membrane dipole potential leading to modulation of ligand binding by P-glycoprotein.

Sterenn Davis, Benjamin M Davis, Joanna L Richens, Kelly-Ann Vere, Peter G Petrov, C Peter Winlove, Paul O'Shea

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.9field-weighted citation impact, top 29% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 25 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Sterenn DavisBiomedical Physics Group, School of Physics, University of Exeter, Exeter, United Kingdom.
Benjamin M DavisCell Biophysics Group, School of Life Sciences, University of Nottingham, Nottingham, United Kingdom.
Joanna L RichensCell Biophysics Group, School of Life Sciences, University of Nottingham, Nottingham, United Kingdom.
Kelly-Ann VereCell Biophysics Group, School of Life Sciences, University of Nottingham, Nottingham, United Kingdom.
Peter G PetrovBiomedical Physics Group, School of Physics, University of Exeter, Exeter, United Kingdom.
C Peter WinloveBiomedical Physics Group, School of Physics, University of Exeter, Exeter, United Kingdom.
Paul O'SheaCell Biophysics Group, School of Life Sciences, University of Nottingham, Nottingham, United Kingdom.
University of Nottingham · GBUniversity of Exeter · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Tocopherol (vitamin E) has attracted considerable attention as a potential protective or palliative agent. In vitro, its free radical-scavenging antioxidant action has been widely demonstrated. In vivo, however, vitamin E treatment exhibits negligible benefits against oxidative stress. α-Tocopherol influences lipid ordering within biological membranes and its derivatives have been suggested to inhibit the multi-drug efflux pump, P-glycoprotein (P-gp). This study employs the fluorescent membrane probe, 1-(3-sulfonatopropyl)-4-[β[2-(di-n-octylamino)-6-naphthyl]vinyl] pyridinium betaine, to investigate whether these effects are connected via influences on the membrane dipole potential (MDP), an intrinsic property of biological membranes previously demonstrated to modulate P-gp activity. α-Tocopherol and its non-free radical-scavenging succinate analog induced similar decreases in the MDP of phosphatidylcholine vesicles. α-Tocopherol succinate also reduced the MDP of T-lymphocytes, subsequently decreasing the binding affinity of saquinavir for P-gp. Additionally, α-tocopherol succinate demonstrated a preference for cholesterol-treated (membrane microdomain enriched) cells over membrane cholesterol-depleted cells. Microdomain disruption via cholesterol depletion decreased saquinavir's affinity for P-gp, potentially implicating these structures in the influence of α-tocopherol succinate on P-gp. This study provides evidence of a microdomain dipole potential-dependent mechanism by which α-tocopherol analogs influence P-gp activity. These findings have implications for the use of α-tocopherol derivatives for drug delivery across biological barriers.

Indexed as

alpha-TocopherolATP Binding Cassette Transporter, Subfamily B, Member 1Cell MembraneFluoresceinsFluorescent DyesHumansJurkat CellsKetocholesterolsLigandsMembrane PotentialsModels, MolecularMolecular ConformationPhosphatidylethanolaminesProtein BindingPyridinium CompoundsSaquinavir1-(3-sulfonatopropyl)-4-(beta-(2-(di-n-octylamino)-6-naphthyl)vinyl)pyridinium betaine7-ketocholesterolalpha-TocopherolATP Binding Cassette Transporter, Subfamily B, Member 1FluoresceinsFluorescent DyesKetocholesterolsLigandsN-fluoresceinylphosphatidylethanolaminePhosphatidylethanolaminesPyridinium CompoundsSaquinavirUnilamellar Liposomesantioxidantscholesterollipid raftssaquinavirvitamin E

Identifiers

PMID26026069
PMCPMC4513995
OpenAlexW2131420776

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.