Roles of heat-shock protein 90 and its four domains (N, LR, M and C) in calcium oxalate stone-forming processes
Issued Date
2022-08-01
Resource Type
ISSN
1420682X
eISSN
14209071
Scopus ID
2-s2.0-85135086761
Pubmed ID
35900595
Journal Title
Cellular and Molecular Life Sciences
Volume
79
Issue
8
Rights Holder(s)
SCOPUS
Bibliographic Citation
Cellular and Molecular Life Sciences Vol.79 No.8 (2022)
Suggested Citation
Yoodee S., Peerapen P., Plumworasawat S., Thongboonkerd V. Roles of heat-shock protein 90 and its four domains (N, LR, M and C) in calcium oxalate stone-forming processes. Cellular and Molecular Life Sciences Vol.79 No.8 (2022). doi:10.1007/s00018-022-04483-z Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/83654
Title
Roles of heat-shock protein 90 and its four domains (N, LR, M and C) in calcium oxalate stone-forming processes
Author(s)
Author's Affiliation
Other Contributor(s)
Abstract
Human heat-shock protein 90 (HSP90) has four functional domains, including NH2-terminal (N), charged linker region (LR), middle (M) and COOH-terminal (C) domains. In kidney stone disease (or nephrolithiasis/urolithiasis), HSP90 serves as a receptor for calcium oxalate monohydrate (COM), which is the most common crystal to form kidney stones. Nevertheless, roles of HSP90 and its four domains in kidney stone formation remained unclear and under-investigated. We thus examined and compared their effects on COM crystals during physical (crystallization, growth and aggregation) and biological (crystal–cell adhesion and crystal invasion through extracellular matrix (ECM)) pathogenic processes of kidney stone formation. The analyses revealed that full-length (FL) HSP90 obviously increased COM crystal size and abundance during crystallization and markedly promoted crystal growth, aggregation, adhesion onto renal cells and ECM invasion. Comparing among four individual domains, N and C domains exhibited the strongest promoting effects, whereas LR domain had the weakest promoting effects on COM crystals. In summary, our findings indicate that FL-HSP90 and its four domains (N, LR, M and C) promote COM crystallization, crystal growth, aggregation, adhesion onto renal cells and invasion through the ECM, all of which are the important physical and biological pathogenic processes of kidney stone formation. Graphical abstract: [Figure not available: see fulltext.].