Exploring the Role of Hsp60 in Alzheimer’s Disease and Type 2 Diabetes: Suggestion for Common Drug Targeting
Heat shock protein 60 (Hsp60) is a member of the chaperonin family of heat shock proteins (HSPs), primarily found in the mitochondrial matrix. As a molecular chaperone, Hsp60 plays an essential role in mediating protein folding and assembly, and together with the co-chaperon Hsp10, it is thought to...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-08-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/15/12456 |
| _version_ | 1797586600980381696 |
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| author | Stefania Zimbone Maria Carmela Di Rosa Santina Chiechio Maria Laura Giuffrida |
| author_facet | Stefania Zimbone Maria Carmela Di Rosa Santina Chiechio Maria Laura Giuffrida |
| author_sort | Stefania Zimbone |
| collection | DOAJ |
| description | Heat shock protein 60 (Hsp60) is a member of the chaperonin family of heat shock proteins (HSPs), primarily found in the mitochondrial matrix. As a molecular chaperone, Hsp60 plays an essential role in mediating protein folding and assembly, and together with the co-chaperon Hsp10, it is thought to maintain protein homeostasis. Recently, it has been found to localize in non-canonical, extra-mitochondrial sites such as cell membranes or extracellular fluids, particularly in pathological conditions. Starting from its biological function, this review aims to provide a comprehensive understanding of the potential involvement of Hsp60 in Alzheimer’s disease (AD) and Type II Diabetes Mellitus (T2DM), which are known to share impaired key pathways and molecular dysfunctions. Fragmentary data reported in the literature reveal interesting links between the altered expression level or localization of this chaperonin and several disease conditions. The present work offers an overview of the past and more recent knowledge about Hsp60 and its role in the most important cellular processes to shed light on neuronal Hsp60 as a potential common target for both pathologies. The absence of any effective cure for AD patients makes the identification of a new molecular target a promising path by which to move forward in the development of new drugs and/or repositioning of therapies already used for T2DM. |
| first_indexed | 2024-03-11T00:24:22Z |
| format | Article |
| id | doaj.art-5de32e2ac82e45ae949e9706c70b0d5d |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T00:24:22Z |
| publishDate | 2023-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-5de32e2ac82e45ae949e9706c70b0d5d2023-11-18T23:05:18ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-08-0124151245610.3390/ijms241512456Exploring the Role of Hsp60 in Alzheimer’s Disease and Type 2 Diabetes: Suggestion for Common Drug TargetingStefania Zimbone0Maria Carmela Di Rosa1Santina Chiechio2Maria Laura Giuffrida3Institute of Crystallography, National Research Council (CNR-IC), 95126 Catania, ItalyInstitute of Crystallography, National Research Council (CNR-IC), 95126 Catania, ItalyDepartment of Drug and Health Sciences, University of Catania, 95125 Catania, ItalyInstitute of Crystallography, National Research Council (CNR-IC), 95126 Catania, ItalyHeat shock protein 60 (Hsp60) is a member of the chaperonin family of heat shock proteins (HSPs), primarily found in the mitochondrial matrix. As a molecular chaperone, Hsp60 plays an essential role in mediating protein folding and assembly, and together with the co-chaperon Hsp10, it is thought to maintain protein homeostasis. Recently, it has been found to localize in non-canonical, extra-mitochondrial sites such as cell membranes or extracellular fluids, particularly in pathological conditions. Starting from its biological function, this review aims to provide a comprehensive understanding of the potential involvement of Hsp60 in Alzheimer’s disease (AD) and Type II Diabetes Mellitus (T2DM), which are known to share impaired key pathways and molecular dysfunctions. Fragmentary data reported in the literature reveal interesting links between the altered expression level or localization of this chaperonin and several disease conditions. The present work offers an overview of the past and more recent knowledge about Hsp60 and its role in the most important cellular processes to shed light on neuronal Hsp60 as a potential common target for both pathologies. The absence of any effective cure for AD patients makes the identification of a new molecular target a promising path by which to move forward in the development of new drugs and/or repositioning of therapies already used for T2DM.https://www.mdpi.com/1422-0067/24/15/12456Hsp60Alzheimer’s diseasetype 2 diabetes mellitusIGF-IR |
| spellingShingle | Stefania Zimbone Maria Carmela Di Rosa Santina Chiechio Maria Laura Giuffrida Exploring the Role of Hsp60 in Alzheimer’s Disease and Type 2 Diabetes: Suggestion for Common Drug Targeting International Journal of Molecular Sciences Hsp60 Alzheimer’s disease type 2 diabetes mellitus IGF-IR |
| title | Exploring the Role of Hsp60 in Alzheimer’s Disease and Type 2 Diabetes: Suggestion for Common Drug Targeting |
| title_full | Exploring the Role of Hsp60 in Alzheimer’s Disease and Type 2 Diabetes: Suggestion for Common Drug Targeting |
| title_fullStr | Exploring the Role of Hsp60 in Alzheimer’s Disease and Type 2 Diabetes: Suggestion for Common Drug Targeting |
| title_full_unstemmed | Exploring the Role of Hsp60 in Alzheimer’s Disease and Type 2 Diabetes: Suggestion for Common Drug Targeting |
| title_short | Exploring the Role of Hsp60 in Alzheimer’s Disease and Type 2 Diabetes: Suggestion for Common Drug Targeting |
| title_sort | exploring the role of hsp60 in alzheimer s disease and type 2 diabetes suggestion for common drug targeting |
| topic | Hsp60 Alzheimer’s disease type 2 diabetes mellitus IGF-IR |
| url | https://www.mdpi.com/1422-0067/24/15/12456 |
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