ArticleiScience2025
Extracellular ERp57 promotes fibronectin fibril formation during matrix assembly of articular cartilage.
Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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
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Who cites it
1 citing paper in PubMed.
- Cytological Performance Evaluation of a Novel Skin-Repair Agent: Recombinant Protein Disulfide Bond Isomerase.Bioengineering (Basel, Switzerland) · 2026Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fibronectin 1 (FN1), a general organizer of extracellular matrix (ECM) in various connective tissues, contains disulfide bridges formed by protein disulfide isomerases (PDIs). ERp57 (PDIA3), an ER resident glycoprotein-specific PDI, is also detectable in cartilage extracellular matrix (ECM). Here, we analyzed the extracellular role of ERp57 in FN1 fibrillogenesis in cartilage. ERp57 KO mice exhibited reduced ECM density. Isolated chondrocytes thereof and C28/I2 ERp57 KO chondrocytes formed fewer and shorter FN1 fibrils than WT cells. Significantly, cell membrane-impermeable thiol blockers reduced FN1 assembly in WT cells, while active recombinant ERp57 protein increased it only in the absence of thiol blockers, emphasizing the necessity of ERp57-mediated disulfide bridge formation for FN1 fibrillogenesis. Co-immunofluorescence and proximity ligation assays revealed a direct interaction between ERp57 and FN1. This study highlights a key role for extracellular ERp57 PDI activity in cartilage and further explains phenotypic changes in ERp57 KO animals.
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