HSP90 Inhibition and Modulation of the Proteome: Therapeutical Implications for Idiopathic Pulmonary Fibrosis (IPF)
Idiopathic Pulmonary fibrosis (IPF) is a catastrophic disease with poor outcomes and limited pharmacological approaches. Heat shock protein 90 (HSP90) has been recently involved in the wound-healing pathological response that leads to collagen deposition in patients with IPF and its inhibition repre...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-07-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/15/5286 |
| _version_ | 1797561301430435840 |
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| author | Ruben Manuel Luciano Colunga Biancatelli Pavel Solopov Betsy Gregory John D. Catravas |
| author_facet | Ruben Manuel Luciano Colunga Biancatelli Pavel Solopov Betsy Gregory John D. Catravas |
| author_sort | Ruben Manuel Luciano Colunga Biancatelli |
| collection | DOAJ |
| description | Idiopathic Pulmonary fibrosis (IPF) is a catastrophic disease with poor outcomes and limited pharmacological approaches. Heat shock protein 90 (HSP90) has been recently involved in the wound-healing pathological response that leads to collagen deposition in patients with IPF and its inhibition represents an exciting drug target against the development of pulmonary fibrosis. Under physiological conditions, HSP90 guarantees proteostasis through the refolding of damaged proteins and the degradation of irreversibly damaged ones. Additionally, its inhibition, by specific HSP90 inhibitors (e.g., 17 AAG, 17 DAG, and AUY-922) has proven beneficial in different preclinical models of human disease. HSP90 inhibition modulates a complex subset of kinases and interferes with intracellular signaling pathways and proteome regulation. In this review, we evaluated the current evidence and rationale for the use of HSP90 inhibitors in the treatment of pulmonary fibrosis, discussed the intracellular pathways involved, described the limitations of the current understanding and provided insights for future research. |
| first_indexed | 2024-03-10T18:12:57Z |
| format | Article |
| id | doaj.art-5a5ccfd97bec4937a67331b2abdb5621 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T18:12:57Z |
| publishDate | 2020-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-5a5ccfd97bec4937a67331b2abdb56212023-11-20T07:57:50ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-07-012115528610.3390/ijms21155286HSP90 Inhibition and Modulation of the Proteome: Therapeutical Implications for Idiopathic Pulmonary Fibrosis (IPF)Ruben Manuel Luciano Colunga Biancatelli0Pavel Solopov1Betsy Gregory2John D. Catravas3Frank Reidy Research Center for Bioelectrics, Old Dominion University, Norfolk, VA 23508, USAFrank Reidy Research Center for Bioelectrics, Old Dominion University, Norfolk, VA 23508, USAFrank Reidy Research Center for Bioelectrics, Old Dominion University, Norfolk, VA 23508, USAFrank Reidy Research Center for Bioelectrics, Old Dominion University, Norfolk, VA 23508, USAIdiopathic Pulmonary fibrosis (IPF) is a catastrophic disease with poor outcomes and limited pharmacological approaches. Heat shock protein 90 (HSP90) has been recently involved in the wound-healing pathological response that leads to collagen deposition in patients with IPF and its inhibition represents an exciting drug target against the development of pulmonary fibrosis. Under physiological conditions, HSP90 guarantees proteostasis through the refolding of damaged proteins and the degradation of irreversibly damaged ones. Additionally, its inhibition, by specific HSP90 inhibitors (e.g., 17 AAG, 17 DAG, and AUY-922) has proven beneficial in different preclinical models of human disease. HSP90 inhibition modulates a complex subset of kinases and interferes with intracellular signaling pathways and proteome regulation. In this review, we evaluated the current evidence and rationale for the use of HSP90 inhibitors in the treatment of pulmonary fibrosis, discussed the intracellular pathways involved, described the limitations of the current understanding and provided insights for future research.https://www.mdpi.com/1422-0067/21/15/5286Idiopathic Pulmonary FibrosisHSP90HSP90 inhibitorAUY-92217 AAGProteome |
| spellingShingle | Ruben Manuel Luciano Colunga Biancatelli Pavel Solopov Betsy Gregory John D. Catravas HSP90 Inhibition and Modulation of the Proteome: Therapeutical Implications for Idiopathic Pulmonary Fibrosis (IPF) International Journal of Molecular Sciences Idiopathic Pulmonary Fibrosis HSP90 HSP90 inhibitor AUY-922 17 AAG Proteome |
| title | HSP90 Inhibition and Modulation of the Proteome: Therapeutical Implications for Idiopathic Pulmonary Fibrosis (IPF) |
| title_full | HSP90 Inhibition and Modulation of the Proteome: Therapeutical Implications for Idiopathic Pulmonary Fibrosis (IPF) |
| title_fullStr | HSP90 Inhibition and Modulation of the Proteome: Therapeutical Implications for Idiopathic Pulmonary Fibrosis (IPF) |
| title_full_unstemmed | HSP90 Inhibition and Modulation of the Proteome: Therapeutical Implications for Idiopathic Pulmonary Fibrosis (IPF) |
| title_short | HSP90 Inhibition and Modulation of the Proteome: Therapeutical Implications for Idiopathic Pulmonary Fibrosis (IPF) |
| title_sort | hsp90 inhibition and modulation of the proteome therapeutical implications for idiopathic pulmonary fibrosis ipf |
| topic | Idiopathic Pulmonary Fibrosis HSP90 HSP90 inhibitor AUY-922 17 AAG Proteome |
| url | https://www.mdpi.com/1422-0067/21/15/5286 |
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