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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antibodies, Blocking / pharmacology
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Benzoquinones
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CD28 Antigens / immunology
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CD28 Antigens / pharmacology*
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Enzyme Inhibitors / pharmacology*
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HSP90 Heat-Shock Proteins / antagonists & inhibitors*
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HSP90 Heat-Shock Proteins / physiology
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Humans
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Interleukin-2 / metabolism
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Lactams, Macrocyclic
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Lymphocyte Activation / drug effects
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Quinones / pharmacology*
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Receptors, Interleukin-2 / biosynthesis
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Signal Transduction
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T-Lymphocytes / immunology*
Substances
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Antibodies, Blocking
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Benzoquinones
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CD28 Antigens
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Enzyme Inhibitors
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HSP90 Heat-Shock Proteins
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Interleukin-2
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Lactams, Macrocyclic
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Quinones
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Receptors, Interleukin-2
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geldanamycin