Abstract
Heat shock protein 90 (Hsp90), an ATP-dependent molecular chaperone, is a highly conserved and ubiquitously expressed stress protein in eukaryotes. It is responsible for activation of various proteins involved in signal transduction, cell cycle control, hormone signaling, and transcription. Anomalous expression of this family can be associated with several disease states. Current article focuses on the novel use of Hsp90 inhibitors as antimalarial agents. The present armamentarium of antimalarial therapy is not proving itself as an adequate treatment to eradicate malaria completely. This inadequacy is mainly due to the increasing drug resistance rate in Plasmodium species. The parasite Plasmodium falciparum requires Hsp90 (Pfhsp90) for regulating its development. Analysis of PfHsp90 function suggests that it regulates parasite development during the frequent febrile episodes that are characteristic of malaria. This crucial role of Hsp90 in the growth and development of the parasite has attracted many researchers as a potential target for malaria and other infectious diseases. Currently there are about seven antimalarial and more than thirty anticancer Hsp90 inhibitors in various phases of drug development. Addition of alternatives with novel mechanism to the current treatment armoury may eventually help improve the outcomes of malaria. It is prudent to remain optimistic as the research in this field continues to evolve.
Keywords: Heat shock protein, Hsp90, Hsp90 inhibitors, Plasmodium falciparum, PfHsp90, malaria.
Mini-Reviews in Medicinal Chemistry
Title:Targeting Heat Shock Protein 90 for Malaria
Volume: 13 Issue: 13
Author(s): Anup S. Ramdhave, Dhaval Patel, I. Ramya, Mukesh Nandave and Prashant S. Kharkar
Affiliation:
Keywords: Heat shock protein, Hsp90, Hsp90 inhibitors, Plasmodium falciparum, PfHsp90, malaria.
Abstract: Heat shock protein 90 (Hsp90), an ATP-dependent molecular chaperone, is a highly conserved and ubiquitously expressed stress protein in eukaryotes. It is responsible for activation of various proteins involved in signal transduction, cell cycle control, hormone signaling, and transcription. Anomalous expression of this family can be associated with several disease states. Current article focuses on the novel use of Hsp90 inhibitors as antimalarial agents. The present armamentarium of antimalarial therapy is not proving itself as an adequate treatment to eradicate malaria completely. This inadequacy is mainly due to the increasing drug resistance rate in Plasmodium species. The parasite Plasmodium falciparum requires Hsp90 (Pfhsp90) for regulating its development. Analysis of PfHsp90 function suggests that it regulates parasite development during the frequent febrile episodes that are characteristic of malaria. This crucial role of Hsp90 in the growth and development of the parasite has attracted many researchers as a potential target for malaria and other infectious diseases. Currently there are about seven antimalarial and more than thirty anticancer Hsp90 inhibitors in various phases of drug development. Addition of alternatives with novel mechanism to the current treatment armoury may eventually help improve the outcomes of malaria. It is prudent to remain optimistic as the research in this field continues to evolve.
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Cite this article as:
Ramdhave S. Anup, Patel Dhaval, Ramya I., Nandave Mukesh and Kharkar S. Prashant, Targeting Heat Shock Protein 90 for Malaria, Mini-Reviews in Medicinal Chemistry 2013; 13 (13) . https://dx.doi.org/10.2174/13895575113136660094
DOI https://dx.doi.org/10.2174/13895575113136660094 |
Print ISSN 1389-5575 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5607 |
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