Abstract

Heat shock protein (HSP) 90, an important component of the molecular chaperone network, is closely concerned with cellular signaling pathways and stress response by participating in the process of maturation and activation of client proteins, playing a crucial role both in the normal and abnormal operation of the organism. In functionally defective tissues, programmed cell death (PCD) is one of the regulable fundamental mechanisms mediated by HSP90, including apoptosis, autophagy, necroptosis, ferroptosis, and others. Here, we show the complex relationship between HSP90 and different types of PCD in various diseases, and discuss the possibility of HSP90 as the common regulatory nodal in multiple PCD, which would provide a new perspective for the therapeutic approaches in disease.

Details

Title
HSP90 mediates the connection of multiple programmed cell death in diseases
Author
Peng, Caiwang 1   VIAFID ORCID Logo  ; Zhao, Fengyan 1   VIAFID ORCID Logo  ; Li, Hengli 1   VIAFID ORCID Logo  ; Li, Ling 2 ; Yang, Yantao 3 ; Liu, Fang 1   VIAFID ORCID Logo 

 Hunan University of Chinese Medicine, College of Pharmacy, Changsha, China (GRID:grid.488482.a) (ISNI:0000 0004 1765 5169); Hunan Engineering Technology Center of Standardization and Function of Chinese Herbal Decoction Piece, Changsha, China (GRID:grid.488482.a); Key Laboratory of Modern Research of TCM, Education Department of Hunan Province, Changsha, China (GRID:grid.454772.7) (ISNI:0000 0004 5901 2284) 
 Hunan University of Chinese Medicine, College of Pharmacy, Changsha, China (GRID:grid.488482.a) (ISNI:0000 0004 1765 5169); Key Laboratory of Modern Research of TCM, Education Department of Hunan Province, Changsha, China (GRID:grid.454772.7) (ISNI:0000 0004 5901 2284) 
 Hunan University of Chinese Medicine, College of Pharmacy, Changsha, China (GRID:grid.488482.a) (ISNI:0000 0004 1765 5169); Hunan Engineering Technology Center of Standardization and Function of Chinese Herbal Decoction Piece, Changsha, China (GRID:grid.488482.a) 
Publication year
2022
Publication date
Nov 2022
Publisher
Springer Nature B.V.
e-ISSN
20414889
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2732139334
Copyright
© The Author(s) 2022. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.