Binding of Proteases to Fibrillar Amyloid-β Protein and its Inhibition by Congo Red
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Summary
It is reported that fAβ also binds to neprilysin and insulysin, which results in the inhibition of their proteolytic activities, suggesting that clearance of soluble Aβ may be defective in AD because of binding of proteases to amyloid plaques, leading to inactivation of proteases that are required for catabolism of Aβ.
- Type
- article
- Published
- 2007-11-19
- Cited by
- 14
- References
- 55
- OpenAlex
- https://openalex.org/W1776631372
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:2626899
Keywords
Congo red, Proteases, Trypsin, Thioflavin, Biochemistry
References
- The toxicity in vitro of beta-amyloid protein.
- Amyloid deposits and amyloidosis. The beta-fibrilloses (first of two parts).
- Staining methods for identification of amyloid in tissue.
- Degradation of Soluble Amyloid β-Peptides 1–40, 1–42, and the Dutch Variant 1–40Q by Insulin Degrading Enzyme from Alzheimer Disease and Control Brains
- The conformation of Alzheimer's beta peptide determines the rate of amyloid formation and its resistance to proteolysis.
- Fibrillar amyloid beta-protein inhibits the activity of high molecular weight brain protease and trypsin
- Neuronal neprilysin overexpression is associated with attenuation of Abeta-related spatial memory deficit.
- Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
- Amyloid β-peptide is produced by cultured cells during normal metabolism
- Congo red and protein aggregation in neurodegenerative diseases.
- Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
- Cathepsin D is involved in the clearance of Alzheimer's beta-amyloid protein.
- Sulfonated dyes attenuate the toxic effects of β-amyloid in a structure-specific fashion
- Alzheimer's Disease β-Amyloid Peptide Is Increased in Mice Deficient in Endothelin-converting Enzyme*
- Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red.
- Fibrillar amyloid beta-protein forms a membrane-like hydrophobic domain.
- Insulin, insulin-degrading enzyme and amyloid-beta peptide in Alzheimer's disease: review and hypothesis.
- Congo red protects against toxicity of beta-amyloid peptides on rat hippocampal neurones.
- CONGO RED AS A STAIN FOR FLUORESCENCE MICROSCOPY OF AMYLOID
- Translating cell biology into therapeutic advances in Alzheimer's disease
Cited by
- Promoting α‐secretase cleavage of beta‐amyloid with engineered proteolytic antibody fragments
- Plasma insulin-degrading enzyme: Characterisation and evaluation as a potential biomarker for Alzheimer's disease
- Effects of Congo red on aβ(1-40) fibril formation process and morphology.
- Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status
- Biochemical studies in Normal Pressure Hydrocephalus (NPH) patients: Change in CSF levels of amyloid precursor protein (APP), amyloid-beta (Aβ) peptide and phospho-tau
- Detection of oligomers and fibrils of α-synuclein by AIEgen with strong fluorescence.
- Advances in the pathogenesis of Alzheimer’s disease: a re-evaluation of amyloid cascade hypothesis
- Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform
- A Comparison of Three Fluorophores for the Detection of Amyloid Fibers and Prefibrillar Oligomeric Assemblies. ThT (Thioflavin T); ANS (1-Anilinonaphthalene-8-sulfonic Acid); and bisANS (4,4'-Dianilino-1,1'-binaphthyl-5,5'-disulfonic Acid).
- Microfluidic approaches for probing amyloid assembly and behaviour.
- Effects of Zn2+ Ions and Environmental Conditions on the Fibrillization of Insulin. Zn2+ ioonide ja keskkonnatingimuste mõju insuliini fibrillisatsioonile
- Structure and Aggregation Mechanisms in Amyloids
- Understanding Osaka mutation polymorphic Aβ fibril response to static and oscillating electric fields: insights from computational modeling
- Current status of fluid biomarkers for early Alzheimer's disease and FDA regulation implications.
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