Evidence map›Paper›PMID 27557898›Full record

ArticleArchives of toxicology2017

Impact of genetic modulation of SULT1A enzymes on DNA adduct formation by aristolochic acids and 3-nitrobenzanthrone.

Volker M Arlt, Walter Meinl, Simone Florian, Eszter Nagy, Frantisek Barta, Marlies Thomann, Iveta Mrizova, Annette M Krais, Maggie Liu, Meirion Richards and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Archives of toxicology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 25 citations in OpenAlex.

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  10. The Impact of p53 on Aristolochic Acid I-Induced Gene Expression In Vivo.International journal of molecular sciences · 2019
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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

16 authors at 6 institutions in 4 countries.

Volker M ArltAnalytical and Environmental Sciences Division, MRC-PHE Centre for Environment and Health, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London, SE1 9NH, UK. volker.arlt@kcl.ac.uk.ORCID http://orcid.org/0000-0003-4314-9318
Walter MeinlDepartment of Nutritional Toxicology, German Institute of Human Nutrition (DIfE) Potsdam-Rehbrücke, 14558, Nuthetal, Germany.
Simone FlorianDepartment of Nutritional Toxicology, German Institute of Human Nutrition (DIfE) Potsdam-Rehbrücke, 14558, Nuthetal, Germany.
Eszter NagyAnalytical and Environmental Sciences Division, MRC-PHE Centre for Environment and Health, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London, SE1 9NH, UK.
Frantisek BartaDepartment of Biochemistry, Faculty of Science, Charles University, Albertov 2030, 12840, Prague 2, Czech Republic.
Marlies ThomannAnalytical and Environmental Sciences Division, MRC-PHE Centre for Environment and Health, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London, SE1 9NH, UK.
Iveta MrizovaDepartment of Biochemistry, Faculty of Science, Charles University, Albertov 2030, 12840, Prague 2, Czech Republic.
Annette M KraisAnalytical and Environmental Sciences Division, MRC-PHE Centre for Environment and Health, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London, SE1 9NH, UK.
Maggie LiuDivision of Cancer Therapeutics, Institute of Cancer Research, Sutton, Surrey, SM2 5NG, UK.
Meirion RichardsDivision of Cancer Therapeutics, Institute of Cancer Research, Sutton, Surrey, SM2 5NG, UK.
Amin MirzaDivision of Cancer Therapeutics, Institute of Cancer Research, Sutton, Surrey, SM2 5NG, UK.
Klaus KopkaDivision of Radiopharmaceutical Chemistry, German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120, Heidelberg, Germany.
David H PhillipsAnalytical and Environmental Sciences Division, MRC-PHE Centre for Environment and Health, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London, SE1 9NH, UK.
Hansruedi GlattDepartment of Nutritional Toxicology, German Institute of Human Nutrition (DIfE) Potsdam-Rehbrücke, 14558, Nuthetal, Germany.
Marie StiborovaDepartment of Biochemistry, Faculty of Science, Charles University, Albertov 2030, 12840, Prague 2, Czech Republic.
Heinz H SchmeiserDivision of Radiopharmaceutical Chemistry, German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120, Heidelberg, Germany.
King's College London · GBCharles University · CZInstitute of Cancer Research · GBGerman Cancer Research Center · DEGerman Institute of Human Nutrition · DEFederal Institute for Risk Assessment · DE

Funding

Cancer Research UK 14329
6 · The paper itself

Abstract

Exposure to aristolochic acid (AA) causes aristolochic acid nephropathy (AAN) and Balkan endemic nephropathy (BEN). Conflicting results have been found for the role of human sulfotransferase 1A1 (SULT1A1) contributing to the metabolic activation of aristolochic acid I (AAI) in vitro. We evaluated the role of human SULT1A1 in AA bioactivation in vivo after treatment of transgenic mice carrying a functional human SULT1A1-SULT1A2 gene cluster (i.e. hSULT1A1/2 mice) and Sult1a1(-/-) mice with AAI and aristolochic acid II (AAII). Both compounds formed characteristic DNA adducts in the intact mouse and in cytosolic incubations in vitro. However, we did not find differences in AAI-/AAII-DNA adduct levels between hSULT1A1/2 and wild-type (WT) mice in all tissues analysed including kidney and liver despite strong enhancement of sulfotransferase activity in both kidney and liver of hSULT1A1/2 mice relative to WT, kidney and liver being major organs involved in AA metabolism. In contrast, DNA adduct formation was strongly increased in hSULT1A1/2 mice compared to WT after treatment with 3-nitrobenzanthrone (3-NBA), another carcinogenic aromatic nitro compound where human SULT1A1/2 is known to contribute to genotoxicity. We found no differences in AAI-/AAII-DNA adduct formation in Sult1a1(-/-) and WT mice in vivo. Using renal and hepatic cytosolic fractions of hSULT1A1/2, Sult1a1(-/-) and WT mice, we investigated AAI-DNA adduct formation in vitro but failed to find a contribution of human SULT1A1/2 or murine Sult1a1 to AAI bioactivation. Our results indicate that sulfo-conjugation catalysed by human SULT1A1 does not play a role in the activation pathways of AAI and AAII in vivo, but is important in 3-NBA bioactivation.

Indexed as

AnimalsAristolochic AcidsArylsulfotransferaseBenz(a)AnthracenesCarcinogensCytosolDNA AdductsHumansKidneyLiverMaleMiceMice, KnockoutMice, TransgenicMultigene Family3-nitrobenzanthroneAristolochic AcidsArylsulfotransferaseBenz(a)AnthracenesCarcinogensDNA AdductsSULT1A1 protein, humanSULT1A2 protein, human3-NitrobenzanthroneAristolochic acid nephropathyBalkan endemic nephropathyCarcinogen metabolismDNA adductsSulfotransferase 1A1

Identifiers

PMID27557898
PMCPMC5364269
OpenAlexW2517160513

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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.