INTERACTION OF THE IMMUNOSUPPRESSANT DEOXYSPERGUALIN WITH A MEMBER OF THE HSP70 FAMILY OF HEAT-SHOCK PROTEINS
INTERACTION OF THE IMMUNOSUPPRESSANT DEOXYSPERGUALIN WITH A MEMBER OF THE HSP70 FAMILY OF HEAT-SHOCK PROTEINS
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DOI：
10.1126/science.1411548
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发表时间：
1992-10-16
期刊：
影响因子：
56.9
通讯作者：
MAZZUCCO, CE
中科院分区：
文献类型：
--
作者：
NADLER, SG;TEPPER, MA;MAZZUCCO, CE
脱氧桔果苷是一种有效的免疫抑制剂，其作用机制尚不清楚。为了阐明其作用机制，我们鉴定了一个胞内DSG结合蛋白。DSG现已被证明与Hsc70特异性结合，Hsc70是热休克蛋白70 （Hsp70）蛋白家族的组成或同源成员。热休克蛋白家族的成员对包括免疫反应在内的许多细胞过程都很重要，这一发现表明，热休克蛋白可能代表一类免疫抑制结合蛋白或亲免疫蛋白，不同于先前鉴定的顺式-反式脯氨酸异构酶。DSG可以为了解热休克蛋白在免疫过程中的功能提供工具。
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.