Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs
| Autor: | Blagosklonny Mv |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Cancer Research
Lactams Macrocyclic Context (language use) Biology chemistry.chemical_compound Growth factor receptor Neoplasms medicine Benzoquinones Animals Humans Receptors Growth Factor HSP90 Heat-Shock Proteins Receptor Oncogene Proteins Clinical Trials as Topic Antibiotics Antineoplastic Quinones Hematology Geldanamycin Hsp90 Growth Inhibitors Radicicol Cell biology Oncology Mechanism of action chemistry Immunology biology.protein medicine.symptom Signal transduction Protein Kinases Signal Transduction Transcription Factors |
| Zdroj: | Leukemia. 16(4) |
| ISSN: | 0887-6924 |
| Popis: | Geldanamycin (GA), herbimycin A and radicicol bind heat-shock protein-90 (Hsp90) and destabilize its client proteins including v-Src, Bcr-Abl, Raf-1, ErbB2, some growth factor receptors and steroid receptors. Thus, Hsp90-active agents induce ubiquitination and proteasomal degradation of numerous oncoproteins. Depending on the cellular context, HSP90-active agents cause growth arrest, differentiation and apoptosis, or can prevent apoptosis. HSP-active agents are undergoing clinical trials. Like targets of most chemotherapeutics, Hsp90 is not a cancer-specific protein. By attacking a nonspecific target, HSP-90-active compounds still may preferentially kill certain tumor cells. How can this be achieved? How can therapeutic potentials be exploited? This article starts the discussion. |
| Databáze: | OpenAIRE |
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