ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2014
Heparin binding confers prion stability and impairs its aggregation.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 62 citations in OpenAlex.
- Practical Real-Time Quaking-Induced Conversion for Detecting Classical Bovine Spongiform Encephalopathy and Classical and Atypical Scrapie Prions.Pathogens (Basel, Switzerland) · 2026Article
- Identification of Chlorogenic Acids fromACS omega · 2025Article
- Extension of the SUGRES-1P Coarse-Grained Model of Polysaccharides to Heparin.Journal of chemical theory and computation · 2023Article
- Full-length prion protein incorporated into prion aggregates is a marker for prion strain-specific destabilization of aggregate structure following cellular uptake.Journal of biochemistry · 2023Article
- Cell biology of prion strains in vivo and in vitro.Cell and tissue research · 2023Review
- Aminoquinolones and Their Benzoquinone Dimer Hybrids as Modulators of Prion Protein Conversion.Molecules (Basel, Switzerland) · 2022Article
- Phase separation of p53 precedes aggregation and is affected by oncogenic mutations and ligands.Chemical science · 2021Article
- Comparative analysis of heparin affecting the biochemical properties of chicken and murine prion proteins.PloS one · 2021Article
- Rabbit PrP Is Partially Resistant toFrontiers in neuroscience · 2021Article
- Advances in the preparation and synthesis of heparin and related products.Drug discovery today · 2020Review
- Enzymatic degradation of RNA causes widespread protein aggregation in cell and tissue lysates.EMBO reports · 2020Article
- Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins.International journal of molecular sciences · 2020Review
- Shortening heparan sulfate chains prolongs survival and reduces parenchymal plaques in prion disease caused by mobile, ADAM10-cleaved prions.Acta neuropathologica · 2020Article
- Cellulose ether treatment in vivo generates chronic wasting disease prions with reduced protease resistance and delayed disease progression.Journal of neurochemistry · 2020Article
- p53 reactivation with induction of massive apoptosis-1 (PRIMA-1) inhibits amyloid aggregation of mutant p53 in cancer cells.The Journal of biological chemistry · 2019Article
- Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils.The Journal of biological chemistry · 2018Article
- A Promising Antiprion Trimethoxychalcone Binds to the Globular Domain of the Cellular Prion Protein and Changes Its Cellular Location.Antimicrobial agents and chemotherapy · 2018Article
- Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Pathogens (Basel, Switzerland) · 2017Review
- Article
- Lessons learned from protein aggregation: toward technological and biomedical applications.Biophysical reviews · 2017Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The conversion of the prion protein (PrP) into scrapie PrP (PrP(Sc)) is a central event in prion diseases. Several molecules work as cofactors in the conversion process, including glycosaminoglycans (GAGs). GAGs exhibit a paradoxical effect, as they convert PrP into protease-resistant PrP (PrP-res) but also exert protective activity. We compared the stability and aggregation propensity of PrP and the heparin-PrP complex through the application of different in vitro aggregation approaches, including real-time quaking-induced conversion (RT-QuIC). Transmissible spongiform encephalopathy-associated forms from mouse and hamster brain homogenates were used to seed RT-QuIC-induced fibrillization. In our study, interaction between heparin and cellular PrP (PrP(C)) increased thermal PrP stability, leading to an 8-fold decrease in temperature-induced aggregation. The interaction of low-molecular-weight heparin (LMWHep) with the PrP N- or C-terminal domain affected not only the extent of PrP fibrillization but also its kinetics, lowering the reaction rate constant from 1.04 to 0.29 s(-1) and increasing the lag phase from 12 to 19 h in RT-QuIC experiments. Our findings explain the protective effect of heparin in different models of prion and prion-like neurodegenerative diseases and establish the groundwork for the development of therapeutic strategies based on GAGs.
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Registered trials
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