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

Tamás Schnaider, János Somogyi, P. 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

Fingerprint

T-cells
Chemical activation
T-Lymphocytes
HSP90 Heat-Shock Proteins
Molecular Chaperones
Interleukin-2 Receptors
Cytoplasmic and Nuclear Receptors
Lymphocyte Activation
Nuclear Proteins
Heat-Shock Proteins
Protein Kinases
Interleukin-2
Antibodies
Pharmaceutical Preparations
geldanamycin

Keywords

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

ASJC Scopus subject areas

  • Pharmacology

Cite this

The Hsp90-specific inhibitor, geldanamycin, blocks CD28-mediated activation of human T lymphocytes. / Schnaider, Tamás; Somogyi, János; Csermely, P.; Szamel, Marta.

In: Life Sciences, Vol. 63, No. 11, 07.08.1998, p. 949-954.

Research output: Contribution to journalArticle

Schnaider, Tamás ; Somogyi, János ; Csermely, P. ; Szamel, Marta. / The Hsp90-specific inhibitor, geldanamycin, blocks CD28-mediated activation of human T lymphocytes. In: Life Sciences. 1998 ; Vol. 63, No. 11. pp. 949-954.
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