Cellular signalling after in vivo heat shock in the liver

Paola Maroni, Paola Bendinelli, Cinzia Zuccorononno, Luisa Schiaffonati, Roberta Piccoletti

Research output: Contribution to journalArticle

Abstract

In an experimental model of in vivo hyperthermia, we investigated the involvement of a number of signalling events in rat liver. We report that in vivo heat shock causes a powerful activation of c-Jun N-terminal kinase and p38 kinase but does not trigger poly(ADP-ribose) polymerase cleavage, a signature event of apoptosis. Among the upstream regulators of the kinases, we show that stress-activated protein kinase/extracellular signal-regulated kinase/nitrogen-activated protein kinase kinase 4 SEK1/MKK4 is not involved whereas MKK3 and/or MKK6 are activated. PAK activity displays a transient rise, whereas GCK does not change. PI3-kinase activity increases in anti-phosphotyrosine immunoprecipitates, suggesting a tyrosine kinase-dependent induction mechanism, and the co-immunoprecipitation of PI3-kinase with p60 Src kinase supports the involvement of this latter. GSK3, which may act downstream to PI3-kinase through AKT, undergoes hyperphosphorylation, thus playing a possible role in the protection from apoptosis and in the modulation of heat-shock transcription factor activity. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)145-152
Number of pages8
JournalCell Biology International
Volume24
Issue number3
DOIs
Publication statusPublished - 2000

Keywords

  • Heat shock
  • Rat liver
  • Signal transduction
  • Stress-activated protein kinases

ASJC Scopus subject areas

  • Cell Biology

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  • Cite this

    Maroni, P., Bendinelli, P., Zuccorononno, C., Schiaffonati, L., & Piccoletti, R. (2000). Cellular signalling after in vivo heat shock in the liver. Cell Biology International, 24(3), 145-152. https://doi.org/10.1006/cbir.1999.0493