scholarly journals Heat Shock Protein 90 as a Prognostic Marker and Therapeutic Target for Adrenocortical Carcinoma

2019 ◽  
Vol 10 ◽  
Author(s):  
Claudia Siebert ◽  
Denis Ciato ◽  
Masanori Murakami ◽  
Ludwig Frei-Stuber ◽  
Luis Gustavo Perez-Rivas ◽  
...  
2015 ◽  
Vol 14 (9) ◽  
pp. 1985-1993 ◽  
Author(s):  
Tomoki Shirota ◽  
Hidenori Ojima ◽  
Nobuyoshi Hiraoka ◽  
Kazuaki Shimada ◽  
Hirofumi Rokutan ◽  
...  

Surgery ◽  
2020 ◽  
Vol 167 (1) ◽  
pp. 233-240 ◽  
Author(s):  
Ton Wang ◽  
Chitra Subramanian ◽  
Brian S.J. Blagg ◽  
Mark S. Cohen

2016 ◽  
Vol 136 (9) ◽  
pp. S239
Author(s):  
S. Yamada-Kanazawa ◽  
I. Kajihara ◽  
S. Fukushima ◽  
M. Jinnin ◽  
M. Masuzawa ◽  
...  

2008 ◽  
Vol 8 (6) ◽  
pp. 522-535 ◽  
Author(s):  
M. Barginear ◽  
C. Van Poznak ◽  
N. Rosen ◽  
S. Modi ◽  
C. Hudis ◽  
...  

2008 ◽  
pp. 291-308
Author(s):  
Constantine S. Mitsiades ◽  
Teru Hideshima ◽  
Nikhil C. Munshi ◽  
Paul G. Richardson ◽  
Kenneth C. Anderson

2020 ◽  
Vol 14 (1) ◽  
pp. 30-37
Author(s):  
Chiranjib Bhattacharjee ◽  
Lokesh Deb

In human cells, Heat Shock Protein-90 (HSP-90) is present in the cytosol, nucleoplasm, endoplasmic reticulum, and mitochondria. The eukaryotic HSP-90 is multifunctionary and essential for cell viability, signal transduction, cell-cycle control as well as transcriptional regulation. The intracellular environment does not restrict HSP-90. It has a vital role in all types of inflammatory disorders, including cancer, autoimmune diseases, infectious inflammatory conditions. Hence, pharmacological inhibition of HSP-90 is currently a choice of therapeutic target for the treatment of autoimmune diseases, cancer, and infectious diseases. Based on the biology of HSP-90, several COOH-terminal ATPase sites of HSP-90, NH2-terminal ATPase sites of HSP-90, and Histone deacetylase inhibitors are evaluated and classified under various groups. For the treatment of different inflammatory disorders, HSP-90 identified as a promising therapeutic target. The present review may guide researchers for evaluating the HSP-90 targeted pathway as a useful therapeutic target for inflammatory diseases, including cancers.


2001 ◽  
Vol 382 (3) ◽  
pp. 499-504 ◽  
Author(s):  
Marcus C. Rosenhagen ◽  
Jason C. Young ◽  
Gabriela M. Wochnik ◽  
Alexandra S. Herr ◽  
Ulrike Schmidt ◽  
...  

Abstract Radicicol (RAD) and the benzoquinone ansamycin geldanamycin (GA) are potential anticancer drugs known to inhibit heat shock protein 90 (hsp90) and, therefore, the activation of proteins dependent on its function such as protooncogenic kinases and nuclear receptors. Using the glucocorticoid receptor (GR) as a model system we analysed the effects of RAD and various benzoquinone ansamycins. All compounds efficiently abolished GRdependent transactivation. Surprisingly, whenever one of the ansamycins was applied in combination with RAD, synergistic inhibition of GRdependent transcription and of hormone binding of GR was observed. In contrast, combination of two ansamycins showed no synergy. These findings suggest synergism within the hsp90 dimer and may open new ways to explore hsp90 as therapeutic target.


Sign in / Sign up

Export Citation Format

Share Document