Evidence map›Paper›PMID 30622215›Full record

ArticleMolecular pharmacology2019

Belinostat, at Its Clinically Relevant Concentrations, Inhibits Rifampicin-Induced CYP3A4 and MDR1 Gene Expression.

Kodye L Abbott, Chloe S Chaudhury, Aneesh Chandran, Saraswathi Vishveshwara, Zdenek Dvorak, Eva Jiskrova, Karolina Poulikova, Barbora Vyhlidalova, Sridhar Mani, Satyanarayana R Pondugula

Open access · bronzeAbstract read
In one paragraph

Article in Molecular pharmacology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Evaluation ofJournal of dietary supplements · 2026
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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

10 authors at 3 institutions in 3 countries.

Kodye L AbbottDepartment of Anatomy, Physiology and Pharmacology (K.L.A., C.S.C., S.R.P.) and Auburn University Research Initiative in Cancer (K.L.A., C.S.C., S.R.P.), Auburn University, Auburn, Alabama; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India (A.C., S.V.); Regional Centre of Advanced Technologies and Materials, Faculty of Science, Palacky University, Olomouc, Czech Republic (Z.D., E.J., K.P., B.V.); and Albert Einstein Cancer Center, Albert Einstein College of Medicine, New York, New York (S.M.).
Chloe S ChaudhuryDepartment of Anatomy, Physiology and Pharmacology (K.L.A., C.S.C., S.R.P.) and Auburn University Research Initiative in Cancer (K.L.A., C.S.C., S.R.P.), Auburn University, Auburn, Alabama; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India (A.C., S.V.); Regional Centre of Advanced Technologies and Materials, Faculty of Science, Palacky University, Olomouc, Czech Republic (Z.D., E.J., K.P., B.V.); and Albert Einstein Cancer Center, Albert Einstein College of Medicine, New York, New York (S.M.).
Aneesh ChandranDepartment of Anatomy, Physiology and Pharmacology (K.L.A., C.S.C., S.R.P.) and Auburn University Research Initiative in Cancer (K.L.A., C.S.C., S.R.P.), Auburn University, Auburn, Alabama; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India (A.C., S.V.); Regional Centre of Advanced Technologies and Materials, Faculty of Science, Palacky University, Olomouc, Czech Republic (Z.D., E.J., K.P., B.V.); and Albert Einstein Cancer Center, Albert Einstein College of Medicine, New York, New York (S.M.).
Saraswathi VishveshwaraDepartment of Anatomy, Physiology and Pharmacology (K.L.A., C.S.C., S.R.P.) and Auburn University Research Initiative in Cancer (K.L.A., C.S.C., S.R.P.), Auburn University, Auburn, Alabama; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India (A.C., S.V.); Regional Centre of Advanced Technologies and Materials, Faculty of Science, Palacky University, Olomouc, Czech Republic (Z.D., E.J., K.P., B.V.); and Albert Einstein Cancer Center, Albert Einstein College of Medicine, New York, New York (S.M.).
Zdenek DvorakDepartment of Anatomy, Physiology and Pharmacology (K.L.A., C.S.C., S.R.P.) and Auburn University Research Initiative in Cancer (K.L.A., C.S.C., S.R.P.), Auburn University, Auburn, Alabama; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India (A.C., S.V.); Regional Centre of Advanced Technologies and Materials, Faculty of Science, Palacky University, Olomouc, Czech Republic (Z.D., E.J., K.P., B.V.); and Albert Einstein Cancer Center, Albert Einstein College of Medicine, New York, New York (S.M.).
Eva JiskrovaDepartment of Anatomy, Physiology and Pharmacology (K.L.A., C.S.C., S.R.P.) and Auburn University Research Initiative in Cancer (K.L.A., C.S.C., S.R.P.), Auburn University, Auburn, Alabama; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India (A.C., S.V.); Regional Centre of Advanced Technologies and Materials, Faculty of Science, Palacky University, Olomouc, Czech Republic (Z.D., E.J., K.P., B.V.); and Albert Einstein Cancer Center, Albert Einstein College of Medicine, New York, New York (S.M.).
Karolina PoulikovaDepartment of Anatomy, Physiology and Pharmacology (K.L.A., C.S.C., S.R.P.) and Auburn University Research Initiative in Cancer (K.L.A., C.S.C., S.R.P.), Auburn University, Auburn, Alabama; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India (A.C., S.V.); Regional Centre of Advanced Technologies and Materials, Faculty of Science, Palacky University, Olomouc, Czech Republic (Z.D., E.J., K.P., B.V.); and Albert Einstein Cancer Center, Albert Einstein College of Medicine, New York, New York (S.M.).
Barbora VyhlidalovaDepartment of Anatomy, Physiology and Pharmacology (K.L.A., C.S.C., S.R.P.) and Auburn University Research Initiative in Cancer (K.L.A., C.S.C., S.R.P.), Auburn University, Auburn, Alabama; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India (A.C., S.V.); Regional Centre of Advanced Technologies and Materials, Faculty of Science, Palacky University, Olomouc, Czech Republic (Z.D., E.J., K.P., B.V.); and Albert Einstein Cancer Center, Albert Einstein College of Medicine, New York, New York (S.M.).
Sridhar ManiDepartment of Anatomy, Physiology and Pharmacology (K.L.A., C.S.C., S.R.P.) and Auburn University Research Initiative in Cancer (K.L.A., C.S.C., S.R.P.), Auburn University, Auburn, Alabama; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India (A.C., S.V.); Regional Centre of Advanced Technologies and Materials, Faculty of Science, Palacky University, Olomouc, Czech Republic (Z.D., E.J., K.P., B.V.); and Albert Einstein Cancer Center, Albert Einstein College of Medicine, New York, New York (S.M.) srp0010@auburn.edu sridhar.mani@einstein.yu.edu.
Satyanarayana R PondugulaDepartment of Anatomy, Physiology and Pharmacology (K.L.A., C.S.C., S.R.P.) and Auburn University Research Initiative in Cancer (K.L.A., C.S.C., S.R.P.), Auburn University, Auburn, Alabama; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India (A.C., S.V.); Regional Centre of Advanced Technologies and Materials, Faculty of Science, Palacky University, Olomouc, Czech Republic (Z.D., E.J., K.P., B.V.); and Albert Einstein Cancer Center, Albert Einstein College of Medicine, New York, New York (S.M.) srp0010@auburn.edu sridhar.mani@einstein.yu.edu.
Albert Einstein College of Medicine · USRegional Centre of Advanced Technologies and Materials · CZAuburn University · US

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI STEVEN C. ALMO · 1985 to 2026
$111.2M
Microbial Metabolite Mimics, PXR and Colitis-Induced Colorectal CancerR01CA222469 · NCI · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI MANI, SRIDHAR · 2018 to 2022
$2.3M
Development of Novel Drugs to Alleviate CPT-11 ToxicityR01CA161879 · NCI · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI MANI, SRIDHAR, REDINBO, MATTHEW R · 2012 to 2016
$1.6M
NCI NIH HHS P30 CA013330NCI NIH HHS R01 CA161879NCI NIH HHS R01 CA222469
6 · The paper itself

Abstract

Activation of human pregnane X receptor (hPXR) has been associated with induction of chemoresistance. It has been proposed that such chemoresistance via cytochrome P450/drug transporters can be reversed with the use of antagonists that specifically abrogate agonist-mediated hPXR activation. Unfortunately, proposed antagonists lack the specificity and appropriate pharmacological characteristics that allow these features to be active in the clinic. We propose that, ideally, an hPXR antagonist would be a cancer drug itself that is part of a "cancer drug cocktail" and effective as an hPXR antagonist at therapeutic concentrations. Belinostat (BEL), a histone deacetylase inhibitor approved for the treatment of relapsed/refractory peripheral T-cell lymphoma, and often used in combination with chemotherapy, is an attractive candidate based on its hPXR ligand-like features. We sought to determine whether these features of BEL might allow it to behave as an antagonist in combination chemotherapy regimens that include hPXR activators. BEL represses agonist-activated hPXR target gene expression at its therapeutic concentrations in human primary hepatocytes and LS174T human colon cancer cells. BEL repressed rifampicin-induced gene expression of CYP3A4 and multidrug resistance protein 1, as well as their respective protein activities. BEL decreased rifampicin-induced resistance to SN-38, the active metabolite of irinotecan, in LS174T cells. This finding indicates that BEL could suppress hPXR agonist-induced chemoresistance. BEL attenuated the agonist-induced steroid receptor coactivator-1 interaction with hPXR, and, together with molecular docking studies, the study suggests that BEL directly interacts with multiple sites on hPXR. Taken together, our results suggest that BEL, at its clinically relevant therapeutic concentration, can antagonize hPXR agonist-induced gene expression and chemoresistance.

Indexed as

AdultATP Binding Cassette Transporter, Subfamily BCell Line, TumorCytochrome P-450 CYP3AFemaleGene ExpressionHepatocytesHumansHydroxamic AcidsIrinotecanMaleMiddle AgedMolecular Docking SimulationPregnane X ReceptorReceptors, SteroidRifampinABCB1 protein, humanATP Binding Cassette Transporter, Subfamily BbelinostatCYP3A4 protein, humanCytochrome P-450 CYP3AHydroxamic AcidsIrinotecanPregnane X ReceptorReceptors, SteroidRifampinSulfonamides

Identifiers

PMID30622215
PMCPMC6362450
OpenAlexW2910534780

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.