Evidence map›Paper›PMID 41759742›Full record

ArticleThe Journal of biological chemistry2026

SLC52A1 is a neofunctionalized primate urate transporter enabling intestinal urate secretion.

Syunsuke Yamamoto, Katsuhisa Inoue, Tomoya Yasujima, Hideki Takei, Takahiro Yamashiro, Keiko Asai, Isamu Matake, Sora Uchiyama, Kinya Ohta, Hisanao Kishimoto and 14 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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

24 authors.

Syunsuke YamamotoDepartment of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan; Drug Metabolism, Pharmacokinetics and Modeling, Research, Takeda Pharmaceutical Company Limited, Fujisawa, Japan.
Katsuhisa InoueDepartment of Biopharmaceutics, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Japan.
Tomoya YasujimaDepartment of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan.
Hideki TakeiDepartment of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan.
Takahiro YamashiroDepartment of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan.
Keiko AsaiDepartment of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan.
Isamu MatakeDepartment of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan.
Sora UchiyamaDepartment of Biopharmaceutics, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Japan.
Kinya OhtaCollege of Pharmacy, Kinjo Gakuin University, Nagoya, Japan.
Hisanao KishimotoDepartment of Biopharmaceutics, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Japan.
Kei HiguchiDepartment of Biopharmaceutics, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Japan; Faculty of Pharmaceutical Sciences, Department of Pharmacokinetics, Toho University, Funabashi, Japan.
Hisashi AnayamaDrug Safety Research and Evaluation, Research, Takeda Pharmaceutical Company Limited, Fujisawa, Japan.
Yuuko AsaoDrug Safety Research and Evaluation, Research, Takeda Pharmaceutical Company Limited, Fujisawa, Japan.
Hideki HirabayashiDrug Metabolism, Pharmacokinetics and Modeling, Research, Takeda Pharmaceutical Company Limited, Fujisawa, Japan.
Nobuyuki AmanoDrug Metabolism, Pharmacokinetics and Modeling, Research, Takeda Pharmaceutical Company Limited, Fujisawa, Japan.
Toru ShimizuMidorigaoka Hospital, Takatsuki, Japan; Kyoto Industrial Health Association, Kyoto, Japan.
Tappei TakadaDepartment of Pharmacy, The University of Tokyo Hospital, Tokyo, Japan.
Takashi TamuraDepartment of Preventive Medicine, Nagoya University Graduate School of Medicine, Nagoya, Japan.
Kenji WakaiDepartment of Preventive Medicine, Nagoya University Graduate School of Medicine, Nagoya, Japan.
Yusuke KawamuraDepartment of Integrative Physiology and Bio-Nano Medicine, National Defense Medical College, Tokorozawa, Japan.
Akiyoshi NakayamaDepartment of Integrative Physiology and Bio-Nano Medicine, National Defense Medical College, Tokorozawa, Japan.
Yu ToyodaDepartment of Integrative Physiology and Bio-Nano Medicine, National Defense Medical College, Tokorozawa, Japan.
Hirotaka MatsuoDepartment of Integrative Physiology and Bio-Nano Medicine, National Defense Medical College, Tokorozawa, Japan; Department of Bioinformation Management, National Defense Medical College Research Institute, Tokorozawa, Japan.
Hiroaki YuasaDepartment of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan. Electronic address: yuasa@phar.nagoya-cu.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serum urate levels are high in hominoids because of the evolutionary loss of uricase, an enzyme involved in purine metabolism during evolution. However, the mechanism underlying uricase loss remains unclear. We report the involvement of the neofunctionalized solute carrier family 52 member A1 (SLC52A1) in the evolutionary loss of uricase. Synteny analysis revealed that SLC52A1 was duplicated from SLC52A2, which encodes a riboflavin transporter and is conserved among primates. Functional studies demonstrated the ability of primate SLC52A1 to transport urate as well as riboflavin and the mediation of cellular uptake and efflux of urate by human SLC52A1 through facilitated diffusion. Transcellular transport studies demonstrated that SLC52A1, which is basolaterally localized in enterocytes, works synergistically with ABC subfamily G member 2, a luminally localized urate efflux transporter, to remove urate from the basolateral side. Before uricase loss, acquiring SLC52A1 may have provided primates with a novel intestinal urate transport system and allowed for evolutionary uricase loss in hominoids.

Indexed as

Evolution, MolecularIntestine, SmallPrimatesPurinesReceptors, G-Protein-CoupledUric AcidAmino Acid SequenceAnimalsGene DuplicationHumansHyperuricemiaUrate OxidasePurinesReceptors, G-Protein-CoupledSLC52A1 protein, humanUrate OxidaseUric AcidSLC52A1small intestinespecies differenceurate transporter

Identifiers

PMID41759742
PMCPMC13052076

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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.