Evidence map›Paper›PMID 40448544›Full record

ArticleFEBS letters2025

P-glycoprotein modulates the fluidity gradient of the plasma membrane of multidrug resistant CHO cells.

Roger Busche, John R Riordan, Burkhard Tümmler

Abstract read
In one paragraph

Article in FEBS letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Roger BuscheInstitute for Biophysical Chemistry and Structural Biochemistry, Fritz-Hartmann-Centre for Medical Research, Hannover Medical School, Germany.
John R RiordanDepartment of Biochemistry and Biophysics and Cystic Fibrosis Center, University of North Carolina-Chapel Hill, NC, USA.
Burkhard TümmlerInstitute for Biophysical Chemistry and Structural Biochemistry, Fritz-Hartmann-Centre for Medical Research, Hannover Medical School, Germany.ORCID https://orcid.org/0000-0002-2566-8758

Funding

Deutsche Forschungsgemeinschaft Tu-40/1-1 1-2
6 · The paper itself

Abstract

Cryo-electron microscopy has yielded high-resolution structural data of the multidrug efflux transporter P-glycoprotein (ABCB1), but its direct and indirect interactions within the native membrane environment have remained largely unexplored. Here, we compared the fluidity gradients of plasma membranes of the drug-sensitive CHO cell line AuxB1 and its P-glycoprotein overexpressing derivative B30 by fluorescence anisotropy of embedded n-(9-anthroyloxy) fatty acid probes (n = 2, 7, 9, 12, 16) in the temperature range of 10-50 °C. The shape of the temperature profiles of probe mobility was comparable in AuxB1 and B30 membranes, but did not match. Overexpression of P-glycoprotein smoothened the transversal gradient of the out-of-plane mode of rotation of the probes, which may facilitate the partitioning of hydrophobic drugs into the membrane and thereby increase the speed of P-glycoprotein to pump the drug out of the cell.

Indexed as

ATP Binding Cassette Transporter, Subfamily B, Member 1Cell MembraneDrug Resistance, MultipleMembrane FluidityAnimalsATP Binding Cassette Transporter, Subfamily BCHO CellsCricetinaeCricetulusATP Binding Cassette Transporter, Subfamily BATP Binding Cassette Transporter, Subfamily B, Member 1ABCB1ABC transportermembrane fluiditymultidrug resistancen‐(9‐anthroyloxy) fatty acidP‐glycoprotein

Identifiers

PMID40448544
PMCPMC12338861

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Registered trials

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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.