Activation of the heat shock factor 1 by serine protease inhibitors. An effect associated with nuclear factor-kB inhibition. (Articolo in rivista)

Type
Label
  • Activation of the heat shock factor 1 by serine protease inhibitors. An effect associated with nuclear factor-kB inhibition. (Articolo in rivista) (literal)
Anno
  • 1998-01-01T00:00:00+01:00 (literal)
Alternative label
  • Rossi A.(1); Elia G.(1); Santoro M.G.(1,2) (1998)
    Activation of the heat shock factor 1 by serine protease inhibitors. An effect associated with nuclear factor-kB inhibition.
    in The Journal of biological chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Rossi A.(1); Elia G.(1); Santoro M.G.(1,2) (literal)
Pagina inizio
  • 16446 (literal)
Pagina fine
  • 16452 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 273 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1-Institute of Experimental Medicine, Consiglio Nazionale delle Ricerche, Rome, 2-Department of Biology, University of Rome Tor Vergata, Rome, Italy (literal)
Titolo
  • Activation of the heat shock factor 1 by serine protease inhibitors. An effect associated with nuclear factor-kB inhibition. (literal)
Abstract
  • Heat shock proteins (HSPs) have a cytoprotective role in several human diseases, including ischemia and viral infection. Nuclear factor-?B (NF-?B) is a critical regulator of inflammation and virus replication. Here we report that a class of serine protease inhibitors with NF-?B-inhibitory activity are potent HSP inducers via activation of heat shock transcription factor 1 (HSF1) in human cells. 3,4-Dichloroisocoumarin, the most effective compound, rapidly induces HSF1 DNA binding activity and phosphorylation, leading to transcription and translation of heat shock genes for a period of several hours. HSF1 activation is independent of de novo protein synthesis and is correlated in a concentration- and time-dependent manner with NF-?B inhibition. Cysteine protease inhibitors E64 and calpain inhibitor II, which do not block NF-?B activation, do not induce HSF DNA binding activity. HSP induction by 3,4-dichloroisocoumarin is associated with antiviral activity during rhabdovirus infection. These results identify a new class of HSP inducers and indicate a link between the regulatory pathways of HSF and NF-?B, suggesting novel strategies to simultaneously switch on cytoprotective genes and down-regulate inflammatory and viral genes. (literal)
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