ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026
Lipid Metabolic Dysregulation Driven by OSMR Mutations Underlies Amyloidogenesis in Primary Localized Cutaneous Amyloidosis.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
backgroundPrimary localized cutaneous amyloidosis (PLCA) is characterized by the deposition of amyloid material within the superficial dermis. Its origin and composition remain debated, including whether deposits derive from keratin filament degeneration or misfolded protein aggregation, and whether non-protein components contribute.
objectivesThis study aimed to re-examine the composition of PLCA deposits and elucidate how OSMR mutations drive their formation, focusing on protein aggregation and lipid metabolism.
methodsWe employed PROTEOSTAT staining, lipidomics, and Nile Red/Oil Red O staining in patient tissues, engineered HaCaT cells, and mouse models, together with mechanistic functional analyses.
resultsPLCA lesions contain abundant protein aggregates alongside significant lipid accumulation, indicating pathological protein-lipid complexes. As the common genetic defect in familial PLCA, OSMRβ deficiency significantly promoted both lipid accumulation and protein aggregation in cellular and animal models. Lipidomic profiling revealed alterations in unsaturated fatty acids (UFAs, C18:1/C18:2) and ceramides. Crucially, exogenous UFAs induced protein aggregation. Mechanistically, OSMRβ deficiency impairs STAT5 activation, leading to AKR1B10 upregulation and lipid dysregulation, whereas inhibition of this axis rescued both phenotypes.
conclusionsOSMR mutation drives amyloid deposition in PLCA through a STAT5-AKR1B10 lipid metabolic axis that promotes co-aggregation of lipids and misfolded proteins, providing potential therapeutic targets.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.