Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease
The review describes correlations between impaired functioning of chaperones and co-chaperones in Alzheimer’s disease (AD) pathogenesis. The study aims to highlight significant lines of research in this field. Chaperones like Hsp90 or Hsp70 are critical agents in regulating cell homeostasis. Due to...
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| Format: | Article |
| Language: | English |
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MDPI AG
2024-03-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/25/6/3401 |
| _version_ | 1797240697665880064 |
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| author | Joanna Batko Katarzyna Antosz Weronika Miśków Magdalena Pszczołowska Kamil Walczak Jerzy Leszek |
| author_facet | Joanna Batko Katarzyna Antosz Weronika Miśków Magdalena Pszczołowska Kamil Walczak Jerzy Leszek |
| author_sort | Joanna Batko |
| collection | DOAJ |
| description | The review describes correlations between impaired functioning of chaperones and co-chaperones in Alzheimer’s disease (AD) pathogenesis. The study aims to highlight significant lines of research in this field. Chaperones like Hsp90 or Hsp70 are critical agents in regulating cell homeostasis. Due to some conditions, like aging, their activity is damaged, resulting in β-amyloid and tau aggregation. This leads to the development of neurocognitive impairment. Dysregulation of co-chaperones is one of the causes of this condition. Disorders in the functioning of molecules like PP5, Cdc37, CacyBP/SIPTRAP1, CHIP protein, FKBP52, or STIP1 play a key role in AD pathogenesis. PP5, Cdc37, CacyBP/SIPTRAP1, and FKBP52 are Hsp90 co-chaperones. CHIP protein is a co-chaperone that switches Hsp70/Hsp90 complexes, and STIP1 binds to Hsp70. Recognition of precise processes allows for the invention of effective treatment methods. Potential drugs may either reduce tau levels or inhibit tau accumulation and aggregation. Some substances neuroprotect from Aβ toxicity. Further studies on chaperones and co-chaperones are required to understand the fundamental tenets of this topic more entirely and improve the prevention and treatment of AD. |
| first_indexed | 2024-04-24T18:11:33Z |
| format | Article |
| id | doaj.art-9b1e7f09dc434e9aa04432cfe09b41bf |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-04-24T18:11:33Z |
| publishDate | 2024-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-9b1e7f09dc434e9aa04432cfe09b41bf2024-03-27T13:45:59ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672024-03-01256340110.3390/ijms25063401Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s DiseaseJoanna Batko0Katarzyna Antosz1Weronika Miśków2Magdalena Pszczołowska3Kamil Walczak4Jerzy Leszek5Faculty of Medicine, Wroclaw Medical University, Ludwika Pasteura 1, 50-367 Wrocław, PolandFaculty of Medicine, Wroclaw Medical University, Ludwika Pasteura 1, 50-367 Wrocław, PolandFaculty of Medicine, Wroclaw Medical University, Ludwika Pasteura 1, 50-367 Wrocław, PolandFaculty of Medicine, Wroclaw Medical University, Ludwika Pasteura 1, 50-367 Wrocław, PolandFaculty of Medicine, Wroclaw Medical University, Ludwika Pasteura 1, 50-367 Wrocław, PolandClinic of Psychiatry, Department of Psychiatry, Wroclaw Medical University, Ludwika Pasteura 10, 50-367 Wrocław, PolandThe review describes correlations between impaired functioning of chaperones and co-chaperones in Alzheimer’s disease (AD) pathogenesis. The study aims to highlight significant lines of research in this field. Chaperones like Hsp90 or Hsp70 are critical agents in regulating cell homeostasis. Due to some conditions, like aging, their activity is damaged, resulting in β-amyloid and tau aggregation. This leads to the development of neurocognitive impairment. Dysregulation of co-chaperones is one of the causes of this condition. Disorders in the functioning of molecules like PP5, Cdc37, CacyBP/SIPTRAP1, CHIP protein, FKBP52, or STIP1 play a key role in AD pathogenesis. PP5, Cdc37, CacyBP/SIPTRAP1, and FKBP52 are Hsp90 co-chaperones. CHIP protein is a co-chaperone that switches Hsp70/Hsp90 complexes, and STIP1 binds to Hsp70. Recognition of precise processes allows for the invention of effective treatment methods. Potential drugs may either reduce tau levels or inhibit tau accumulation and aggregation. Some substances neuroprotect from Aβ toxicity. Further studies on chaperones and co-chaperones are required to understand the fundamental tenets of this topic more entirely and improve the prevention and treatment of AD.https://www.mdpi.com/1422-0067/25/6/3401Alzheimer’s diseasedementiachaperonesHsp90Hsp60Hsp70 |
| spellingShingle | Joanna Batko Katarzyna Antosz Weronika Miśków Magdalena Pszczołowska Kamil Walczak Jerzy Leszek Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease International Journal of Molecular Sciences Alzheimer’s disease dementia chaperones Hsp90 Hsp60 Hsp70 |
| title | Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease |
| title_full | Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease |
| title_fullStr | Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease |
| title_full_unstemmed | Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease |
| title_short | Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease |
| title_sort | chaperones a new class of potential therapeutic targets in alzheimer s disease |
| topic | Alzheimer’s disease dementia chaperones Hsp90 Hsp60 Hsp70 |
| url | https://www.mdpi.com/1422-0067/25/6/3401 |
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