Heat shock protein 90 and role of its chemical inhibitors in treatment of hematologic malignancies
Heat shock protein 90 (Hsp90) is a conserved and constitutively expressed molecular chaperone and it has been shown to stabilize oncoproteins and facilitate cancer development. Hsp90 has been considered as a therapeutic target for cancers and three classes of Hsp90 inhibitors have been developed: (1...
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Published in | Pharmaceuticals Vol. 5; no. 8; pp. 779 - 801 |
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Main Authors | , , , |
Format | Journal Article Book Review |
Language | English |
Published |
Switzerland
MDPI AG
25.07.2012
MDPI |
Subjects | |
Online Access | Get full text |
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Summary: | Heat shock protein 90 (Hsp90) is a conserved and constitutively expressed molecular chaperone and it has been shown to stabilize oncoproteins and facilitate cancer development. Hsp90 has been considered as a therapeutic target for cancers and three classes of Hsp90 inhibitors have been developed: (1) benzoquinone ansamycin and its derivatives, (2) radicicol and its derivates, and (3) small synthetic inhibitors. The roles of these inhibitors in cancer treatment have been studied in laboratories and clinical trials, and some encouraging results have been obtained. Interestingly, targeting of Hsp90 has been shown to be effective in inhibition of cancer stem cells responsible for leukemia initiation and progression, providing a strategy for finding a cure. Because cancer stem cells are well defined in some human leukemias, we will focus on hematologic malignancies in this review. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Adam Li is currently a high school student at Xaverian Brothers High School, 800 Clapboardtree Street, Westwood, MA 02090, USA |
ISSN: | 1424-8247 1424-8247 |
DOI: | 10.3390/ph5080779 |