The Hsp90-specific inhibitor, geldanamycin, blocks CD28-mediated activation of human T lymphocytes

Tamás Schnaider, János Somogyi, Péter Csermely, Marta Szamel

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The 90 kDa heat shock protein (Hsp90) is a molecular chaperone aiding the folding of nuclear hormone receptors and protein kinases. Hsp90-mediated folding can be disrupted by the Hsp90-specific drug, geldanamycin. Here we provide evidence for the inhibition of the CD28-specific BW 828 antibody- mediated activation of human T lymphocyte proliferation, IL-2 secretion and IL-2 receptor expression by geldanamycin. Our results suggest that the major cytoplasmic chaperone, Hsp90, plays an important role in CD28-mediated T lymphocyte activation.

Original languageEnglish
Pages (from-to)949-954
Number of pages6
JournalLife Sciences
Volume63
Issue number11
DOIs
Publication statusPublished - Aug 7 1998

Keywords

  • CD28
  • Geldamycin
  • Hsp90
  • IL-2 receptor expression
  • IL-2 secretion
  • Molecular chaperones
  • T lymphocyte activation

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

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