Evidence map›Paper›PMID 40133703›Full record

ArticleEuropean journal of human genetics : EJHG2026

A hypomorphic FLVCR2 variant resulting in moderate transport deficiency causes hydranencephaly syndrome with brain calcifications.

Marcello Scala, Nancy C P Leong, Thanh Nha Uyen Le, Yu Zhang, Yichang Wu, Mariasavina Severino, Francesca Madia, Mohammad Sadegh Shams Nosrati, Alireza Dostmohammadi, Valeria Capra and 8 more

Abstract readCase Reports
In one paragraph

Article in European journal of human genetics : EJHG, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Choline-An Essential Nutrient with Health Benefits and a Signaling Molecule.International journal of molecular sciences · 2025
    Review
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

18 authors.

Marcello ScalaDepartment of Neurosciences, Rehabilitation, Ophthalmology, Genetics, Maternal and Child Health, Università di Genova, Genoa, Italy. mscala.md@gmail.com.ORCID 0000-0003-2194-7239
Nancy C P LeongDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.ORCID 0009-0004-3818-8675
Thanh Nha Uyen LeDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.ORCID 0000-0003-1838-6100
Yu ZhangDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.
Yichang WuDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.
Mariasavina SeverinoNeuroradiology Unit, IRCCS Istituto Giannina Gaslini, Genoa, Italy.ORCID 0000-0003-4730-5322
Francesca MadiaMedical Genetics Unit, IRCSS Istituto Giannina Gaslini, Genoa, Italy.
Mohammad Sadegh Shams NosratiDepartment of Neurosciences, Rehabilitation, Ophthalmology, Genetics, Maternal and Child Health, Università di Genova, Genoa, Italy.ORCID 0000-0002-5762-0601
Alireza DostmohammadiDepartment of Bioinformatics and Computational Biophysics, Faculty of Biology and Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany.ORCID 0000-0003-4311-2056
Valeria CapraGenomics and Clinical Genetics Unit, IRCSS Istituto Giannina Gaslini, Genoa, Italy.ORCID 0000-0002-3097-0388
Dario PaladiniFetal Medicine and Surgery Unit, IRCCS Istituto Giannina Gaslini, Genoa, Italy.
Francesca BuffelliClinical Pathology Unit, IRCCS Istituto Giannina Gaslini, Genoa, Italy.
Ezio FulcheriClinical Pathology Unit, IRCCS Istituto Giannina Gaslini, Genoa, Italy.
Serena CappatoDepartment of Neurosciences, Rehabilitation, Ophthalmology, Genetics, Maternal and Child Health, Università di Genova, Genoa, Italy.
Ludovica MentaDepartment of Neurosciences, Rehabilitation, Ophthalmology, Genetics, Maternal and Child Health, Università di Genova, Genoa, Italy.
Renata BocciardiDepartment of Neurosciences, Rehabilitation, Ophthalmology, Genetics, Maternal and Child Health, Università di Genova, Genoa, Italy.
Federico ZaraDepartment of Neurosciences, Rehabilitation, Ophthalmology, Genetics, Maternal and Child Health, Università di Genova, Genoa, Italy.ORCID 0000-0001-9744-5222
Long N NguyenDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore. bchnnl@nus.edu.sg.ORCID 0000-0002-9857-2239

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FLVCR2 is a highly conserved member of the major facilitator superfamily (MFS), the largest superfamily of solute carriers that are involved in the transport of small molecules across lipid bilayers. The loss of the murine ortholog Mfsd7c, an endothelial transporter in brain blood vessels, causes brain angiogenic growth deficiency and lethality. Recessive FLVCR2 variants cause proliferative vasculopathy and hydranencephaly-hydrocephaly syndrome (PVHH), also known as Fowler syndrome. This often-lethal condition features microcephaly, skeletal deformities, and severe cerebrovascular defects. Although a number of cases have been reported, very limited evidence of the pathogenicity of FLVCR2 variants is available. In this study, we thoroughly investigated a new fetal case of Fowler syndrome. Through exome sequencing, we identified two compound heterozygous FLVCR2 variants: the maternal c.1124+3_1124+6del and the paternal p.(Arg492Trp). The effects of the c.1124+3_1124+6del variant were investigated through a minigene assay, which showed impaired splicing of the exon 5 of FLVCR2. To characterize the impact of the p.(Arg492Trp) substitution, we performed protein modeling using Rosetta and DynaMut2, that showed a highly destabilizing effect. Then, based on the very recent evidence that choline is a major FLVCR2 ligand, we performed a radiolabeled-choline or ethanolamine transport assays in HEK 293 cells and found that the p.(Arg492Trp) variant causes a 50-60% reduction of FLVCR2 transport activity, resulting in a net activity of 25-30%. Our findings suggest that FLVCR2 deficiency may be sufficient to cause PVHH even in the absence of a complete loss of transport activity, possibly involving extragenetic factors in the pathophysiology of this complex condition.

Indexed as

CalcinosisHydranencephalyMembrane Transport ProteinsReceptors, VirusSymportersBrainFemaleHEK293 CellsHumansMaleFLVCR2 protein, humanMembrane Transport ProteinsReceptors, VirusSymporters

Identifiers

PMID40133703
PMCPMC12963544

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.