Evidence map›Paper›PMID 9677321›Full record

ArticleThe Biochemical journal1998

Linear and cyclic peptides as substrates and modulators of P-glycoprotein: peptide binding and effects on drug transport and accumulation.

F J Sharom, P Lu, R Liu, X Yu

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

19 citing papers in PubMed, 79 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Influence of quaternary cation compound on the size of theBiochemistry and biophysics reports · 2018
    Article
  7. Beauvericin counteracted multi-drug resistantSynthetic and systems biotechnology · 2016
    Article
  8. Article
  9. Review
  10. Mass spectrometry reveals synergistic effects of nucleotides, lipids, and drugs binding to a multidrug resistance efflux pump.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  11. Article
  12. Article
  13. Preface: the concept and consequences of multidrug resistance.Pflugers Archiv : European journal of physiology · 2007
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The hexapeptide immunofan inhibits the MRP-dependent multidrug resistance of tumor cells.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections
    Article
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

4 authors at 1 institution in 1 country.

F J SharomGuelph-Waterloo Centre for Graduate Work in Chemistry and Biochemistry, Department of Chemistry and Biochemistry, University of Guelph, Guelph, Ontario, Canada N1G 2W1. sharom@chembio.uoguelph.ca
P Lu
R Liu
X Yu
University of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One cause of multidrug resistance (MDR) in human cancers is the overexpression of the P-glycoprotein multidrug transporter, a member of the ABC superfamily of membrane proteins. Natural products and chemotherapeutic drugs are pumped out of the cell by P-glycoprotein in an ATP-dependent fashion. There is growing evidence that many hydrophobic peptides are also P-glycoprotein substrates. With the use of a fluorescence-quenching assay, we have shown that some linear and cyclic hydrophobic peptides interact with P-glycoprotein, whereas others do not. The measured values of the quenching constant, Kq, for interaction of peptides with P-glycoprotein ranged from 200 nM for cyclosporine A to 138 microM for the tripeptide N-acetyl-leucyl-leucyl-norleucinal. Peptides that interacted with P-glycoprotein in the fluorescence assay also blocked colchicine transport into plasma membrane vesicles from MDR cells. The values of Dm, the peptide concentration causing 50% inhibition of drug uptake, were highly correlated with the values of Kq, over three orders of magnitude. The P-glycoprotein ATPase stimulation/inhibition profile of the peptides was not helpful in making a quantitative assessment of the ability of a peptide to interact with P-glycoprotein or to block drug transport. Some hydrophobic peptides were able to restore accumulation in MDR cells of the chemotherapeutic drug daunorubicin and the fluorescent dye rhodamine 123 to the levels observed in the drug-sensitive parent. Peptides that interacted with P-glycoprotein also displayed a relatively low overall toxicity to intact MDR cells, and inhibited drug transport at concentrations below the toxic range. Hydrophobic peptides should be given serious consideration for development as clinical chemosensitizing agents.

Indexed as

Adenosine TriphosphatasesAnimalsAntibiotics, AntineoplasticAntimetabolites, AntineoplasticATP Binding Cassette Transporter, Subfamily B, Member 1Biological TransportCell MembraneCHO CellsCricetinaeDaunorubicinDrug Resistance, MultipleIonophoresKineticsOligopeptidesPeptides, CyclicProtein BindingAdenosine TriphosphatasesAntibiotics, AntineoplasticAntimetabolites, AntineoplasticATP Binding Cassette Transporter, Subfamily B, Member 1DaunorubicinIonophoresOligopeptidesPeptides, CyclicRhodamine 123Rhodamines

Identifiers

PMID9677321
PMCPMC1219625
OpenAlexW1871508751

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.