Evidence map›Paper›PMID 37184663›Full record

ArticleActa neuropathologica2023

SCA34 caused by ELOVL4 L168F mutation is a lysosomal lipid storage disease sharing pathology features with neuronal ceroid lipofuscinosis and peroxisomal disorders.

Benjamin Ellezam, Matsanga L Kaseka, Dang Khoa Nguyen, Jean Michaud

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Article in Acta neuropathologica, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 6 citations in OpenAlex.

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4 · The record

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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

4 authors at 3 institutions in 1 country.

Benjamin EllezamDivision of Pathology, CHU Sainte-Justine, 3175 Côte-Sainte-Catherine, Montréal, QC, H3T 1C5, Canada. benjamin.ellezam@umontreal.ca.ORCID 0000-0002-8716-7924
Matsanga L KasekaDivision of Neurology, CHU Sainte-Justine, Montréal, QC, Canada.
Dang Khoa NguyenDepartment of Neuroscience, Université de Montréal, Montréal, QC, Canada.
Jean MichaudDepartment of Pathology and Laboratory Medicine, University of Ottawa, Ottawa, ON, Canada.
Centre Hospitalier Universitaire Sainte-Justine · CACentre Hospitalier de l’Université de Montréal · CAUniversity of Ottawa · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Spinocerebellar ataxia 34 (SCA34) is a late-onset progressive ataxia caused by a mutation in ELOVL4, a gene involved in the biosynthesis of very long-chain fatty acids (VLCFAs). We performed post-mortem neuropathological examinations on four SCA34 patients with the ELOVL4 L168F mutation and compared the findings to age-matched controls. Specific gross findings of SCA34 were limited to pontocerebellar atrophy. On light microscopy, pontine base showed neuronal loss and storage of an autofluorescent lipopigment positive on oil red O, PAS and Hale's colloidal iron and negative on Alcian blue and Luxol fast blue (LFB). Among the swollen neurons were abundant CD68+ /CD163+ /IBA1- macrophages laden with a material with similar histochemical profile as in neurons except for the lack of autofluorescence and oil red O positivity and the presence of needle-like birefringent inclusions. Normal resting IBA1 + microglia were generally absent from pontine base nuclei but present in normal numbers elsewhere in the pons. In dentate nucleus neurons, atrophy was milder than in the pontine base and the coarser storage material was LFB-positive, closely resembling lipofuscin. On electron microscopy, dentate nucleus neurons showed neuronal storage of tridimensionally organized trilaminar spicules within otherwise normal lipofuscin, while in the more affected pontine base neurons, lipofuscin was almost completely replaced by the storage material. Storage macrophages were tightly packed with stacks of unorganized trilaminar spicules, reminiscent of the storage material seen in peroxisomal disorders and thought to represent VLCFAs incorporated in complex polar lipids. In summary, we provide histochemical and ultrastructural evidence that SCA34 is a lipid storage disease, the first among the currently known SCAs, and that the storage lipid is accumulating within neuronal lipofuscin. Our findings suggest that the storage lipid is similar to the one accumulating in non-neuronal cells in peroxisomal disorders and provide the first ultrastructural description of this type of material within neurons.

Indexed as

Lysosomal Storage DiseasesNeuronal Ceroid-LipofuscinosesPeroxisomal DisordersAtaxiaAzo CompoundsEye ProteinsHumansLipidsLipofuscinMembrane ProteinsMutationSkin Diseases, GeneticAzo CompoundsELOVL4 protein, humanEye ProteinsLipidsLipofuscinMembrane Proteinsoil red OAutopsyElectron microscopyLysosomal storage diseasesMicrogliaSpinocerebellar ataxiaVery long-chain fatty acids

Identifiers

PMID37184663
OpenAlexW4376617974

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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.