Endogenous Human Proteins Interfering with Amyloid Formation.
BRICHOS
IAPP
alpha-synuclein
amyloid inhibition
amyloid-beta
apolipoprotein E
clusterin
endogenous proteins
transthyretin
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
14 03 2022
14 03 2022
Historique:
received:
15
02
2022
revised:
08
03
2022
accepted:
11
03
2022
entrez:
25
3
2022
pubmed:
26
3
2022
medline:
23
4
2022
Statut:
epublish
Résumé
Amyloid formation is a pathological process associated with a wide range of degenerative disorders, including Alzheimer's disease, Parkinson's disease, and diabetes mellitus type 2. During disease progression, abnormal accumulation and deposition of proteinaceous material are accompanied by tissue degradation, inflammation, and dysfunction. Agents that can interfere with the process of amyloid formation or target already formed amyloid assemblies are consequently of therapeutic interest. In this context, a few endogenous proteins have been associated with an anti-amyloidogenic activity. Here, we review the properties of transthyretin, apolipoprotein E, clusterin, and BRICHOS protein domain which all effectively interfere with amyloid in vitro, as well as displaying a clinical impact in humans or animal models. Their involvement in the amyloid formation process is discussed, which may aid and inspire new strategies for therapeutic interventions.
Identifiants
pubmed: 35327638
pii: biom12030446
doi: 10.3390/biom12030446
pmc: PMC8946693
pii:
doi:
Substances chimiques
Amyloid
0
Amyloid beta-Peptides
0
Amyloidogenic Proteins
0
alpha-Synuclein
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
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