
The Hsp90 inhibitor 17‐AAG represses calcium‐induced cytokeratin 1 and 10 expression in HaCaT keratinocytes
Author(s) -
Miyoshi Sadanori,
Yamazaki Shota,
Uchiumi Asato,
Katagata Yohtaro
Publication year - 2012
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2012.03.002
Subject(s) - hacat , involucrin , cytokeratin , hsp90 , downregulation and upregulation , keratinocyte , microbiology and biotechnology , signal transduction , function (biology) , biology , chemistry , biochemistry , immunology , in vitro , gene , heat shock protein , immunohistochemistry
Hsp90 is essential for maintaining the activity of numerous signaling factors, and plays a key role in cellular signal transduction networks. 17‐Allylamino‐17‐demethoxygeldanamycin (17‐AAG) is an ansamycin antibiotic that binds to Hsp90 and inhibits its function. HaCaT human keratinocytes were used to investigate the cellular and molecular functions of Hsp90 in keratinocyte differentiation. Inhibition of Hsp90 by 17‐AAG leads to downregulation of the differentiation markers cytokeratin 1 and cytokeratin 10 at the protein and mRNA levels.