Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury
The 70 kDa heat shock protein (HSP70) is a stress-inducible protein that has been shown to protect the brain from various nervous system injuries. It allows cells to withstand potentially lethal insults through its chaperone functions. Its chaperone properties can assist in protein folding and preve...
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MDPI AG
2020-09-01
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| Series: | Cells |
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| Online Access: | https://www.mdpi.com/2073-4409/9/9/2020 |
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| author | Jong Youl Kim Sumit Barua Mei Ying Huang Joohyun Park Midori A. Yenari Jong Eun Lee |
| author_facet | Jong Youl Kim Sumit Barua Mei Ying Huang Joohyun Park Midori A. Yenari Jong Eun Lee |
| author_sort | Jong Youl Kim |
| collection | DOAJ |
| description | The 70 kDa heat shock protein (HSP70) is a stress-inducible protein that has been shown to protect the brain from various nervous system injuries. It allows cells to withstand potentially lethal insults through its chaperone functions. Its chaperone properties can assist in protein folding and prevent protein aggregation following several of these insults. Although its neuroprotective properties have been largely attributed to its chaperone functions, HSP70 may interact directly with proteins involved in cell death and inflammatory pathways following injury. Through the use of mutant animal models, gene transfer, or heat stress, a number of studies have now reported positive outcomes of HSP70 induction. However, these approaches are not practical for clinical translation. Thus, pharmaceutical compounds that can induce HSP70, mostly by inhibiting HSP90, have been investigated as potential therapies to mitigate neurological disease and lead to neuroprotection. This review summarizes the neuroprotective mechanisms of HSP70 and discusses potential ways in which this endogenous therapeutic molecule could be practically induced by pharmacological means to ultimately improve neurological outcomes in acute neurological disease. |
| first_indexed | 2024-03-10T16:37:32Z |
| format | Article |
| id | doaj.art-233898c0246c44cb835a2dfc6d7a8c27 |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-10T16:37:32Z |
| publishDate | 2020-09-01 |
| publisher | MDPI AG |
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| series | Cells |
| spelling | doaj.art-233898c0246c44cb835a2dfc6d7a8c272023-11-20T12:17:54ZengMDPI AGCells2073-44092020-09-0199202010.3390/cells9092020Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain InjuryJong Youl Kim0Sumit Barua1Mei Ying Huang2Joohyun Park3Midori A. Yenari4Jong Eun Lee5Department of Anatomy, Yonsei University College of Medicine, Seoul 03722, KoreaDepartment of Anatomy, Yonsei University College of Medicine, Seoul 03722, KoreaDepartment of Anatomy, Yonsei University College of Medicine, Seoul 03722, KoreaDepartment of Anatomy, Yonsei University College of Medicine, Seoul 03722, KoreaDepartment of Neurology, University of California, San Francisco & the San Francisco Veterans Affairs Medical Center, Neurology (127) VAMC 4150 Clement St., San Francisco, CA 94121, USADepartment of Anatomy, Yonsei University College of Medicine, Seoul 03722, KoreaThe 70 kDa heat shock protein (HSP70) is a stress-inducible protein that has been shown to protect the brain from various nervous system injuries. It allows cells to withstand potentially lethal insults through its chaperone functions. Its chaperone properties can assist in protein folding and prevent protein aggregation following several of these insults. Although its neuroprotective properties have been largely attributed to its chaperone functions, HSP70 may interact directly with proteins involved in cell death and inflammatory pathways following injury. Through the use of mutant animal models, gene transfer, or heat stress, a number of studies have now reported positive outcomes of HSP70 induction. However, these approaches are not practical for clinical translation. Thus, pharmaceutical compounds that can induce HSP70, mostly by inhibiting HSP90, have been investigated as potential therapies to mitigate neurological disease and lead to neuroprotection. This review summarizes the neuroprotective mechanisms of HSP70 and discusses potential ways in which this endogenous therapeutic molecule could be practically induced by pharmacological means to ultimately improve neurological outcomes in acute neurological disease.https://www.mdpi.com/2073-4409/9/9/2020heat shock protein 70brain injurychaperone neuroprotectionpharmacological induction |
| spellingShingle | Jong Youl Kim Sumit Barua Mei Ying Huang Joohyun Park Midori A. Yenari Jong Eun Lee Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury Cells heat shock protein 70 brain injury chaperone neuroprotection pharmacological induction |
| title | Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury |
| title_full | Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury |
| title_fullStr | Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury |
| title_full_unstemmed | Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury |
| title_short | Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury |
| title_sort | heat shock protein 70 hsp70 induction chaperonotherapy for neuroprotection after brain injury |
| topic | heat shock protein 70 brain injury chaperone neuroprotection pharmacological induction |
| url | https://www.mdpi.com/2073-4409/9/9/2020 |
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