A monoallelic UXS1 variant associated with short-limbed short stature.


Journal

Molecular genetics & genomic medicine
ISSN: 2324-9269
Titre abrégé: Mol Genet Genomic Med
Pays: United States
ID NLM: 101603758

Informations de publication

Date de publication:
Jun 2024
Historique:
revised: 15 04 2024
received: 19 01 2024
accepted: 14 05 2024
medline: 11 6 2024
pubmed: 11 6 2024
entrez: 11 6 2024
Statut: ppublish

Résumé

Serine residues in the protein backbone of heavily glycosylated proteoglycans are bound to glycosaminoglycans through a tetrasaccharide linker. UXS1 encodes UDP-glucuronate decarboxylase 1, which catalyzes synthesis of UDP-xylose, the donor of the first building block in the linker. Defects in other enzymes involved in formation of the tetrasaccharide linker cause so-called linkeropathies, characterized by short stature, radio-ulnar synostosis, decreased bone density, congenital contractures, dislocations, and more. Whole exome sequencing was performed in a father and son who presented with a mild skeletal dysplasia, as well as the father's unaffected parents. Wild-type and mutant UXS1 were recombinantly expressed in Escherichia coli and purified. Enzyme activity was evaluated by LC-MS/MS. In vivo effects were studied using HeparinRed assay and metabolomics. The son had short long bones, normal epiphysis, and subtle metaphyseal changes especially in his legs. The likely pathogenic heterozygous variant NM_001253875.1(UXS1):c.557T>A p.(Ile186Asn) detected in the son was de novo in the father. Purified Ile186Asn-UXS1, in contrast to the wild-type, was not able to convert UDP-glucuronic acid to UDP-xylose. Plasma glycosaminoglycan levels were decreased in both son and father. This is the first report linking UXS1 to short-limbed short stature in humans.

Sections du résumé

BACKGROUND BACKGROUND
Serine residues in the protein backbone of heavily glycosylated proteoglycans are bound to glycosaminoglycans through a tetrasaccharide linker. UXS1 encodes UDP-glucuronate decarboxylase 1, which catalyzes synthesis of UDP-xylose, the donor of the first building block in the linker. Defects in other enzymes involved in formation of the tetrasaccharide linker cause so-called linkeropathies, characterized by short stature, radio-ulnar synostosis, decreased bone density, congenital contractures, dislocations, and more.
METHODS METHODS
Whole exome sequencing was performed in a father and son who presented with a mild skeletal dysplasia, as well as the father's unaffected parents. Wild-type and mutant UXS1 were recombinantly expressed in Escherichia coli and purified. Enzyme activity was evaluated by LC-MS/MS. In vivo effects were studied using HeparinRed assay and metabolomics.
RESULTS RESULTS
The son had short long bones, normal epiphysis, and subtle metaphyseal changes especially in his legs. The likely pathogenic heterozygous variant NM_001253875.1(UXS1):c.557T>A p.(Ile186Asn) detected in the son was de novo in the father. Purified Ile186Asn-UXS1, in contrast to the wild-type, was not able to convert UDP-glucuronic acid to UDP-xylose. Plasma glycosaminoglycan levels were decreased in both son and father.
CONCLUSION CONCLUSIONS
This is the first report linking UXS1 to short-limbed short stature in humans.

Identifiants

pubmed: 38860481
doi: 10.1002/mgg3.2472
doi:

Substances chimiques

Carboxy-Lyases EC 4.1.1.-

Types de publication

Journal Article Case Reports

Langues

eng

Sous-ensembles de citation

IM

Pagination

e2472

Subventions

Organisme : storbyuniversitetet
Organisme : H2020 Marie Skłodowska-Curie Actions
ID : 101107665
Organisme : Helse Sør-Øst RHF
ID : 2015095
Organisme : Science for Life Laboratory

Informations de copyright

© 2024 The Author(s). Molecular Genetics & Genomic Medicine published by Wiley Periodicals LLC.

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Auteurs

Cecilie F Rustad (CF)

Centre for Rare Disorders, Oslo University Hospital, Oslo, Norway.

Paul Hoff Backe (PH)

Department of Microbiology, Oslo University Hospital HF, Rikshospitalet, Oslo, Norway.
Department of Medical Biochemistry, Institute of Clinical Medicine, University of Oslo, Oslo, Norway.

Chunsheng Jin (C)

Proteomics Core Facility at Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.

Else Merckoll (E)

Unilabs Radiology Norway, Oslo, Norway.

Kristian Tveten (K)

Department of Medical Genetics, Telemark Hospital Trust, Skien, Norway.

Marissa Lucy Maciej-Hulme (ML)

Department of Life Sciences and Health, Oslo Metropolitan University, Oslo, Norway.

Niclas Karlsson (N)

Department of Life Sciences and Health, Oslo Metropolitan University, Oslo, Norway.
Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.

Trine Prescott (T)

Department of Medical Genetics, Telemark Hospital Trust, Skien, Norway.

Elise Sandås Sand (ES)

Department of Medical Biochemistry, Oslo University Hospital, Oslo, Norway.

Berit Woldseth (B)

Department of Medical Biochemistry, Oslo University Hospital, Oslo, Norway.

Katja Benedikte Prestø Elgstøen (KBP)

Department of Medical Biochemistry, Oslo University Hospital, Oslo, Norway.

Øystein L Holla (ØL)

Department of Medical Genetics, Telemark Hospital Trust, Skien, Norway.

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