ArticleInternational journal of molecular sciences2020
Glycosylation Tunes Neuroserpin Physiological and Pathological Properties.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Immunomodulatory Effects of a Tick Salivary Serpin on Psoriasis-like Inflammation.Life (Basel, Switzerland) · 2026Article
- Innovative Non-PrP-Targeted Drug Strategy Designed to Enhance Prion Clearance.Journal of medicinal chemistry · 2022Article
- Neuroserpin, a crucial regulator for axogenesis, synaptic modelling and cell-cell interactions in the pathophysiology of neurological disease.Cellular and molecular life sciences : CMLS · 2022Review
- Mechanisms affecting brain remodeling in depression: do all roads lead to impaired fibrinolysis?Molecular psychiatry · 2022Review
- Neuroserpin and transthyretin are extracellular chaperones that preferentially inhibit amyloid formation.Science advances · 2021Article
- Neuroserpin: structure, function, physiology and pathology.Cellular and molecular life sciences : CMLS · 2021Review
- G392E neuroserpin causing the dementia FENIB is secreted from cells but is not synaptotoxic.Scientific reports · 2021Article
- Iripin-3, a New Salivary Protein Isolated FromFrontiers in immunology · 2021Article
- Embelin as Lead Compound for New Neuroserpin Polymerization Inhibitors.Life (Basel, Switzerland) · 2020Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
Neuroserpin (NS) is a member of the serine protease inhibitors superfamily. Specific point mutations are responsible for its accumulation in the endoplasmic reticulum of neurons that leads to a pathological condition named familial encephalopathy with neuroserpin inclusion bodies (FENIB). Wild-type NS presents two N-glycosylation chains and does not form polymers in vivo, while non-glycosylated NS causes aberrant polymer accumulation in cell models. To date, all in vitro studies have been conducted on bacterially expressed NS, de facto neglecting the role of glycosylation in the biochemical properties of NS. Here, we report the expression and purification of human glycosylated NS (gNS) using a novel eukaryotic expression system, LEXSY. Our results confirm the correct N-glycosylation of wild-type gNS. The fold and stability of gNS are not altered compared to bacterially expressed NS, as demonstrated by the circular dichroism and intrinsic tryptophan fluorescence assays. Intriguingly, gNS displays a remarkably reduced polymerisation propensity compared to non-glycosylated NS, in keeping with what was previously observed for wild-type NS in vivo and in cell models. Thus, our results support the relevance of gNS as a new in vitro tool to study the molecular bases of FENIB.
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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.