Publication Date:
1992-10-16
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nadler, S G -- Tepper, M A -- Schacter, B -- Mazzucco, C E -- New York, N.Y. -- Science. 1992 Oct 16;258(5081):484-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bristol-Myers Squibb Pharmaceutical Research Institute, Wallingford, CT 06492.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411548" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Guanidines/*metabolism
;
Heat-Shock Proteins/*metabolism
;
Humans
;
Immunosuppressive Agents/*metabolism
;
Molecular Sequence Data
;
Protein Binding
;
Tumor Cells, Cultured
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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