Evidence map›Paper›PMID 33950190›Full record

ArticleJournal of biochemistry2021

Effects of genetic polymorphisms on the sulfation of doxorubicin by human SULT1C4 allozymes.

Saud A Gohal, Mohammed I Rasool, Ahsan F Bairam, Eid S Alatwi, Fatemah A Alherz, Maryam S Abunnaja, Amal A El Daibani, Katsuhisa Kurogi, Ming-Cheh Liu

Abstract read
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In one paragraph

Article in Journal of biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

9 authors.

Saud A GohalDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH 43614, USA.
Mohammed I RasoolDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH 43614, USA.
Ahsan F BairamDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH 43614, USA.
Eid S AlatwiDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH 43614, USA.
Fatemah A AlherzDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH 43614, USA.
Maryam S AbunnajaDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH 43614, USA.
Amal A El DaibaniDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH 43614, USA.
Katsuhisa KurogiDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH 43614, USA.
Ming-Cheh LiuDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH 43614, USA.

Funding

Ontogeny of the Phase II cytosolic sulfotransferases and adverse drug reactionsR03HD071146 · NICHD · UNIVERSITY OF TOLEDO HEALTH SCI CAMPUS · PI LIU, MING-CHEH · 2012 to 2013
$146k
NICHD NIH HHS R03 HD071146NIH HHS # R03HD071146
6 · The paper itself

Abstract

Doxorubicin is a chemotherapeutic drug widely utilized in cancer treatment. An enzyme critical to doxorubicin metabolism is the cytosolic sulfotransferase (SULT) SULT1C4. This study investigated the functional impact of SULT1C4 single nucleotide polymorphisms (SNPs) on the sulfation of doxorubicin by SULT1C4 allozymes. A comprehensive database search was performed to identify various SULT1C4 SNPs. Ten nonsynonymous SULT1C4 SNPs were selected, and the corresponding cDNAs, packaged in pGEX-2TK expression vector, were generated via site-directed mutagenesis. Respective SULT1C4 allozymes were bacterially expressed and purified by affinity chromatography. Purified SULT1C4 allozymes, in comparison with the wild-type enzyme, were analysed for sulphating activities towards doxorubicin and 4-nitrophenol, a prototype substrate. Results obtained showed clearly differential doxorubicin-sulphating activity of SULT1C4 allozymes, implying differential metabolism of doxorubicin through sulfation in individuals with distinct SULT1C4 genotypes.

Indexed as

Polymorphism, Single NucleotideCytosolDoxorubicinGenotypeHumansIsoenzymesKineticsMutagenesis, Site-DirectedNitrophenolsSulfatesSulfotransferases4-nitrophenolDoxorubicinIsoenzymesNitrophenolsSulfatesSulfotransferasesSULT1C4 protein, humancytosolic sulfotransferasedoxorubicinsingle nucleotide polymorphismsSNPssulfationSULTSULT1C4

Identifiers

PMID33950190
PMCPMC8510289

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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.