Heat Shock Protein 90: Inhibitors in Clinical Trials

2010 ◽  
Vol 53 (1) ◽  
pp. 3-17 ◽  
Author(s):  
Marco A. Biamonte ◽  
Ryan Van de Water ◽  
Joseph W. Arndt ◽  
Robert H. Scannevin ◽  
Daniel Perret ◽  
...  
Keyword(s):  
Clinical Trials ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90

Corrections to Heat Shock Protein 90: Inhibitors in Clinical Trials

2010 ◽  
Vol 53 (5) ◽  
pp. 2332-2332 ◽  
Author(s):  
Marco A. Biamonte ◽  
Ryan Van de Water ◽  
Joseph W. Arndt ◽  
Robert H. Scannevin ◽  
Daniel Perret ◽  
...  
Keyword(s):  
Clinical Trials ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90

scholarly journals Kajian Heat Shock Protein 90 (HSP90) dalam Pencarian Kandidat Penghambatnya melalui Ekplorasi Bahan Alam Indonesia

2019 ◽  
Vol 5 (1) ◽  
pp. 1-11
Author(s):  
Rehmadanta Sitepu
Keyword(s):  
Clinical Trials ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Tyrosine Kinases ◽  
Glucocorticoid Receptors ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitor ◽  
Hsp90 Inhibitors ◽  
Protein Activity ◽  
Third Phase

Exploration on anticancer candidates on inhibition of Heat Shock Protein (HSP) activity are increasing in the past ten years. Some of HSP90 inhibitor candidates were in third phase of clinical trials. However, this issue is not followed by the emergency of HSP90 inhibitor research in Indonesia, not only study on natural source but also on synthetic candidates. This study aims to look the development of tracking HSP90 inhibitor candidates globally so that it can initiate the related research in Indonesia. Study of HSP90 and its inhibitors were taken from scientific articles in the range from 2009 to 2018. HSP90 and its inhibitors have important values in the dynamics of functions and stability of proteins to maintain survival of cells. This also include the oncogene proteins that involve in cell proliferation such as tyrosine kinases, transcription factors, and regulatory proteins that expression and interaction depend on HSP90. Expression of the transcription factor p53, Alk gene, Wnt gene, glucocorticoid receptors have also links with HSP90 protein activity. Some candidates for inhibitor of HSP90 have been entering clinical trials such as geldanamycin analogues, resorcinol derivatives, and purines analog. Candidates from natural sources that are also being developed such as luteolin, licochalcone A, oleochantal, novobiocin, epigallocathecin gallat, silybin, deguelin, and celastrol from terpenoid class, Apigenin from flavon class, Curcumin, and  Gambogat Acid. HSP90 inhibitors which are entering the third phase of clinical trial are ganetespib from the resorcinol derivative and retaspimycin from geldanamisin analog group. Exploration of HSP90 inhibitors from Indonesia natural resources still have great potential to be developed because they have high impact values as anticancer candidates.

scholarly journals Heat Shock Protein 90 (Hsp90)-Inhibitor-Luminespib-Loaded-Protein-Based Nanoformulation for Cancer Therapy

Polymers ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 1798
Author(s):  
Ankit K. Rochani ◽  
Sivakumar Balasubramanian ◽  
Aswathy Ravindran Girija ◽  
Toru Maekawa ◽  
Gagan Kaushal ◽  
...  
Keyword(s):  
Clinical Trials ◽  
Heat Shock ◽  
Cancer Therapy ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitor ◽  
Hsp90 Inhibitors ◽  
Delivery Platform ◽  
New Generation

Drugs targeting heat shock protein 90 (Hsp90) have been extensively explored for their anticancer potential in advanced clinical trials. Nanoformulations have been an important drug delivery platform for the anticancer molecules like Hsp90 inhibitors. It has been reported that bovine serum albumin (BSA) nanoparticles (NPs) serve as carriers for anticancer drugs, which have been extensively explored for their therapeutic efficacy against cancers. Luminespib (also known as NVP-AUY922) is a new generation Hsp90 inhibitor that was introduced recently. It is one of the most studied Hsp90 inhibitors for a variety of cancers in Phase I and II clinical trials and is similar to its predecessors such as the ansamycin class of molecules. To our knowledge, nanoformulations for luminespib remain unexplored for their anticancer potential. In the present study, we developed aqueous dispensable BSA NPs for controlled delivery of luminespib. The luminespib-loaded BSA NPs were characterized by SEM, TEM, FTIR, XPS, UV-visible spectroscopy and fluorescence spectroscopy. The results suggest that luminespib interacts by non-covalent reversible interactions with BSA to form drug-loaded BSA NPs (DNPs). Our in vitro evaluations suggest that DNP-based aqueous nanoformulations can be used in both pancreatic (MIA PaCa-2) and breast (MCF-7) cancer therapy.

scholarly journals In VitroActivity of Geldanamycin Derivatives againstSchistosoma japonicumandBrugia malayi

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
David Wenkert ◽  
Bernadette Ramirez ◽  
Yuehai Shen ◽  
Michael A. Kron
Keyword(s):  
Clinical Trials ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Peak Plasma ◽  
Plasma Concentrations ◽  
Heat Shock Protein 90 ◽  
Shock Proteins ◽  
Work Supports ◽  
Antiparasitic Agents

Geldanamycin (GA) is a benzoquinone-containing ansamycin that inhibits heat shock protein 90. GA derivatives are being evaluated as anti-neoplastic agents, but their utility against parasites whose heat shock proteins (Hsps) have homology with human Hsp90 is unknown. The activities of four synthetic GA derivatives were testedin vitrousing adultBrugia malayiandSchistosoma japonicum. Two of the derivatives, 17-N-allyl-17-demethoxygeldanamycin (17-AAG) and 17-N-(2-dimethylaminoethylamino)-17-demethoxygeldanamycin (DMAG), are currently in human clinical trials as anticancer drugs. Using concentrations considered safe peak plasma concentrations for these two derivatives, all four derivatives were active against both parasites. The less toxic derivative 17-AAG was as effective as GA in killingS. japonicum, and both DMAG and 5′-bromogeldanoxazinone were more active than 17-AAG againstB. malayi. This work supports continued evaluation of ansamycin derivatives as broad spectrum antiparasitic agents.

Glycyrrhizin effects rat hepatocytes via the reduction of heat shock protein 90 expression

2001 ◽  
Vol 120 (5) ◽  
pp. A357-A357
Author(s):  
T YOH ◽  
T NAKASHIMA ◽  
Y SUMIDA ◽  
Y KAKISAKA ◽  
H ISHIKAWA ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Rat Hepatocytes
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