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Science 16 October 1992:
Vol. 258. no. 5081, pp. 484 - 486
DOI: 10.1126/science.1411548
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Articles

Science, Vol 258, Issue 5081, 484-486
Copyright © 1992 by American Association for the Advancement of Science

articles

Interaction of the immunosuppressant deoxyspergualin with a member of the Hsp70 family of heat shock proteins

SG Nadler, MA Tepper, B Schacter, and CE Mazzucco

Bristol-Myers Squibb Pharmaceutical Research Institute, Wallingford, CT 06492.

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.


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