Simvastatin functions as a heat shock protein 90 inhibitor against triple‐negative breast cancer

Acetylation plays an important role in regulating the chaperone activity of heat shock protein 90 (Hsp90) during malignant transformation through the stabilization and conformational maturation of oncogenic proteins. However, the functional acetylation sites, potential anticancer drug targets, are s...

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Veröffentlicht in:	Cancer science 2018-10, Vol.109 (10), p.3272-3284
Hauptverfasser:	Kou, Xinhui, Jiang, Xiaoxiao, Liu, Huijuan, Wang, Xuan, Sun, Fanghui, Han, Jiami, Fan, Jiaxing, Feng, Guize, Lin, Zhaohu, Jiang, Lan, Yang, Yonghua
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylation Acetylation - drug effects Adenosine Triphosphate - metabolism Animals Antineoplastic Combined Chemotherapy Protocols - pharmacology Antineoplastic Combined Chemotherapy Protocols - therapeutic use Apoptosis Apoptosis - drug effects Breast cancer Cdc37 Cell cycle Cell Cycle Proteins - metabolism Cell Line, Tumor Cell migration Chaperonins - metabolism Epidermal growth factor Female Heat Heat shock proteins Hsp90 HSP90 Heat-Shock Proteins - antagonists & inhibitors HSP90 Heat-Shock Proteins - metabolism Hsp90 protein Humans Hydroxamic Acids - pharmacology Hydroxamic Acids - therapeutic use Hydroxymethylglutaryl-CoA Reductase Inhibitors - pharmacology Hydroxymethylglutaryl-CoA Reductase Inhibitors - therapeutic use Immunoglobulins Indoles - pharmacology Indoles - therapeutic use Kinases LBH589 Lysine - metabolism Medical prognosis Mice Mice, Inbred BALB C Mice, Nude Mutation Original Panobinostat Plasmids Proteasomes Protein Binding - drug effects Simvastatin Simvastatin - pharmacology Simvastatin - therapeutic use Triple Negative Breast Neoplasms - drug therapy Triple Negative Breast Neoplasms - pathology Tumors Wound healing Xenograft Model Antitumor Assays Xenografts
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