Increased expression of co-chaperone HOP with HSP90 and HSC70 and complex formation in human colonic carcinoma
| Autor: | Hiroshi Nanjo, Hiroshi Kubota, Hirotaka Okada, Hideaki Itoh, Soh Yamamoto, Yuzo Yamamoto, Yukina Izumi, Asami Nakamura, Yuki Abe, Masatake Iida, Eri Itoh |
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| Rok vydání: | 2010 |
| Předmět: |
Original Paper
Protein Folding Immunoprecipitation Lactams Macrocyclic Carcinoma Cell Biology Plasma protein binding Biology Biochemistry Hsp90 Molecular biology Hsp70 Co-chaperone Tetratricopeptide Heat shock protein Chaperone (protein) Colonic Neoplasms Benzoquinones biology.protein Humans HSP70 Heat-Shock Proteins HSP90 Heat-Shock Proteins Heat-Shock Proteins Protein Binding |
| Zdroj: | Cell Stress and Chaperones. 15:1003-1011 |
| ISSN: | 1466-1268 1355-8145 |
| Popis: | Co-chaperone HOP (also called stress-inducible protein 1) is a co-chaperone that interacts with the cytosolic 70-kDa heat shock protein (HSP70) and 90-kDa heat shock protein (HSP90) families using different tetratricopeptide repeat domains. HOP plays crucial roles in the productive folding of substrate proteins by controlling the chaperone activities of HSP70 and HSP90. Here, we examined the levels of HOP, HSC70 (cognate of HSP70, also called HSP73), and HSP90 in the tumor tissues from colon cancer patients, in comparison with the non-tumor tissues from the same patients. Expression level of HOP was significantly increased in the tumor tissues (68% of patients, n = 19). Levels of HSC70 and HSP90 were also increased in the tumor tissues (95% and 74% of patients, respectively), and the HOP level was highly correlated with those of HSP90 (r = 0.77, p |
| Databáze: | OpenAIRE |
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