Interaction of the Immunosuppressant Deoxyspergualin with a Member of the Hsp70 Family of Heat Shock Proteins
| Autor: | Charles E. Mazzucco, Mark A. Tepper, Steven G. Nadler, Bernice Z. Schacter |
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| Rok vydání: | 1992 |
| Předmět: |
Multidisciplinary
HSPA12A Protein family Binding protein Molecular Sequence Data Biology Guanidines DNA-binding protein Hsp70 Mechanism of action Biochemistry Immunophilins Heat shock protein Tumor Cells Cultured medicine Humans Amino Acid Sequence medicine.symptom Heat-Shock Proteins Immunosuppressive Agents Protein Binding |
| Zdroj: | Science. 258:484-486 |
| ISSN: | 1095-9203 0036-8075 |
| Popis: | Deoxyspergualin (DSG) is a potent immunosuppressant whose mechanism of action remains unknown. To elucidate its mechanism of action, an intracellular DSG binding protein was identified. DSG has now been shown to bind specifically to Hsc70, the constitutive or cognate member of the heat shock protein 70 (Hsp70) protein family. The members of the Hsp70 family of heat shock proteins are important for many cellular processes, including immune responses, and this finding suggests that heat shock proteins may represent a class of immunosuppressant binding proteins, or immunophilins, distinct from the previously identified cis-trans proline isomerases. DSG may provide a tool for understanding the function of heat shock proteins in immunological processes. |
| Databáze: | OpenAIRE |
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