90-kDa heat shock protein inhibition abrogates the topoisomerase I poison-induced G2/M checkpoint in p53-null tumor cells by depleting Chk1 and Wee1

The G(2)/M cell cycle checkpoint is regulated by a multitude of signaling pathways after genotoxic stress. Herein, we report that treatment with the 90-kDa heat shock protein (Hsp90) molecular chaperone inhibitor 17-allylamino-17-demethoxygeldanamycin (17AAG) selectively abrogates the G(2)/M checkpo...

Full description

Saved in:

Bibliographic Details
Published in:	Molecular pharmacology Vol. 75; no. 1; p. 124
Main Authors:	Tse, Archie N, Sheikh, Tahir N, Alan, Ho, Chou, Ting-Chao, Schwartz, Gary K
Format:	Journal Article
Language:	English
Published:	United States 01-01-2009
Subjects:	Apoptosis - drug effects Benzoquinones - pharmacology Camptothecin - analogs & derivatives Camptothecin - pharmacology Cell Cycle - drug effects Cell Cycle - physiology Cell Cycle Proteins - metabolism Cell Survival - drug effects Checkpoint Kinase 1 DNA Topoisomerases, Type I - metabolism DNA Topoisomerases, Type I - pharmacology Dose-Response Relationship, Drug Drug Interactions G2 Phase Gene Expression Regulation, Neoplastic - drug effects HCT116 Cells HSP90 Heat-Shock Proteins - antagonists & inhibitors Humans Lactams, Macrocyclic - pharmacology Nuclear Proteins - metabolism Protein Kinases - metabolism Protein-Tyrosine Kinases - metabolism Time Factors Topoisomerase I Inhibitors Tumor Suppressor Protein p53 - metabolism
Online Access:	Get more information
Tags:	Add Tag No Tags, Be the first to tag this record!

Be the first to leave a comment!