Evidence map›Paper›PMID 42484988›Full record

ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2026

Functional characterization of a novel ZIP8 variant causing impaired manganese homeostasis and congenital disorders of glycosylation.

Hitomi Fujishiro, Naoya Morisada, Nao Mitani, Rina Nakayama, Natsuki Goto, Yukina Nishito, Taiho Kambe, Nobuhiko Okamoto, Yoshinao Wada, Yusuke Ishida and 5 more

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In one paragraph

Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 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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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

15 authors.

Hitomi Fujishiro *Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima, 770-8514, Japan. donai-do@ph.bunri-u.ac.jp.
Naoya Morisada *Department of Clinical Genetics, Hyogo Prefectural Kobe Children's Hospital, Kobe, Hyogo, 650-0047, Japan.
Nao MitaniFaculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima, 770-8514, Japan.
Rina NakayamaFaculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima, 770-8514, Japan.
Natsuki GotoDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.
Yukina NishitoDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.
Taiho KambeDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.
Nobuhiko OkamotoDepartment of Medical Genetics, Osaka Women's and Children's Hospital, Izumi, 594-1101, Japan.
Yoshinao WadaDepartment of Obstetric Medicine, Osaka Women's and Children's Hospital (OWCH), 840 Murodo-Cho, Izumi, Osaka, 594-1101, Japan.
Yusuke IshidaDepartment of Neurology, Hyogo Prefectural Kobe Children's Hospital, Kobe, Hyogo, 650-0047, Japan.
Hisato SuzukiDepartment of Pediatrics, University of Tsukuba Hospital, Ibaraki, 305-8575, Japan.
Kandai NozuDepartment of Pediatrics, Kobe University Graduate School of Medicine, Kobe, 650-0017, Japan.
Kenjiro KosakiCenter for Medical Genetics, Keio University School of Medicine, Tokyo, 160-8582, Japan.
Seiichiro HimenoFaculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima, 770-8514, Japan.
Daigo SumiFaculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima, 770-8514, Japan.

Funding

grant for the Initiative on Rare and Undiagnosed Diseases JP22ek0109549Grant-in-Aid for Scientific Research on Innovative Areas 19H05770JSPS KAKENHI Grant 18K06646
6 · The paper itself

Abstract

ZIP8, encoded by SLC39A8, mediates cellular uptake of divalent metal ions, including manganese (Mn). Mutations in SLC39A8 cause a congenital disorder of glycosylation (CDG) associated with Mn deficiency (SLC39A8-CDG). Here, we report a novel case of SLC39A8-CDG harboring a previously unreported mutation (p.F206I) in the transmembrane domain 3 (TMD3). The patient showed markedly low serum Mn levels and abnormal glycosylation. To evaluate the functional consequences of this variant, we generated cells expressing hZIP8-F206I. Mn, cadmium, and zinc uptake levels in cells expressing hZIP8-F206I were approximately half of those in cells expressing wild-type hZIP8. The mutant hZIP8 also showed reduced plasma membrane localization. These findings suggest that this previously unreported mutation in TMD3 significantly impairs ZIP8-mediated metal transport, leading to CDG.

Indexed as

Cation Transport ProteinsCongenital Disorders of GlycosylationManganeseZinc Transporter 8GlycosylationHomeostasisHumansMutationCation Transport ProteinsManganeseSLC39A8 protein, humanZinc Transporter 8Congenital disorder of glycosylationManganeseMetal transporterSLC39A8ZIP8

Identifiers

PMID42484988

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