ArticleInternational journal of molecular sciences2019
Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of α-Synuclein.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Review
- Immunomodulatory Tissue Factors in the Gallbladder Walls of Pediatric Patients with Chronic Calculous Cholecystitis.Children (Basel, Switzerland) · 2025Article
- Heat shock proteins in osteoarthritis: molecular mechanisms, pathogenic roles, and therapeutic opportunities.Frontiers in immunology · 2025Review
- 8-Anilino-1-naphthalenesulfonate-Conjugated Carbon-Coated Ferrite Nanodots for Fluoromagnetic Imaging, Smart Drug Delivery, and Biomolecular Sensing.Pharmaceutics · 2024Article
- Oligomeric State and Holding Activity of Hsp60.International journal of molecular sciences · 2023Article
- Bioinformatics Analysis, Expression Profiling, and Functional Characterization of Heat Shock Proteins inBioengineering (Basel, Switzerland) · 2023Article
- Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases.International journal of molecular sciences · 2022Review
- Different α-synuclein prion strains cause dementia with Lewy bodies and multiple system atrophy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Mitochondrial chaperones in human health and disease.Free radical biology & medicine · 2022Review
- Review
- Spearmint Extract Containing Rosmarinic Acid Suppresses Amyloid Fibril Formation of Proteins Associated with Dementia.Nutrients · 2020Article
- Article
- Chaperones and Proteostasis: Role in Parkinson's Disease.Diseases (Basel, Switzerland) · 2020Review
- An α-synuclein decoy peptide prevents cytotoxic α-synuclein aggregation caused by fatty acid binding protein 3.The Journal of biological chemistryArticle
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Heat shock proteins play roles in assisting other proteins to fold correctly and in preventing the aggregation and accumulation of proteins in misfolded conformations. However, the process of aging significantly degrades this ability to maintain protein homeostasis. Consequently, proteins with incorrect conformations are prone to aggregate and accumulate in cells, and this aberrant aggregation of misfolded proteins may trigger various neurodegenerative diseases, such as Parkinson's disease. Here, we investigated the possibilities of suppressing α-synuclein aggregation by using a mutant form of human chaperonin Hsp60, and a derivative of the isolated apical domain of Hsp60 (Hsp60 AD(Cys)). In vitro measurements were used to detect the effects of chaperonin on amyloid fibril formation, and interactions between Hsp60 proteins and α-synuclein were probed by quartz crystal microbalance analysis. The ability of Hsp60 AD(Cys) to suppress α-synuclein intracellular aggregation and cytotoxicity was also demonstrated. We show that Hsp60 mutant and Hsp60 AD(Cys) both effectively suppress α-synuclein amyloid fibril formation, and also demonstrate for the first time the ability of Hsp60 AD(Cys) to function as a mini-chaperone inside cells. These results highlight the possibility of using Hsp60 AD as a method of prevention and treatment of neurodegenerative diseases.
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Registered trials
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