Document Type

Article

Publication Date

2020

Publication Title

International Journal of Molecular Sciences

Volume

21

Issue

15

Pages

5286 (1-15)

DOI

10.3390/ijms21155286

Abstract

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.

Comments

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Original Publication Citation

Colunga Biancatelli, R. M. L., Solopov, P., Gregory, B., & Catravas, J. D. (2020). HSP90 inhibition and modulation of the proteome: Therapeutical implications for idiopathic pulmonary fibrosis (IPF). International Journal of Molecular Sciences, 21(15), 1-15, Article 5286. https://doi.org/http://dx.doi.org/10.3390/ijms21155286

ORCID

0000-0002-1174-3876 (Colunga Biancatelli), 0000-0002-1705-027X (Solopov)

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