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Apoptosis induced by staurosporine alters chaperone and endoplasmic reticulum proteins: Identification by

Duncan M Short1, Ian D Heron, Jui-Lee A Birse-Archbold

  • 1Astellas CNS Research in Edinburgh (ACE), University of Edinburgh, Edinburgh, UK. Duncanshort1@googlemail.com

Proteomics
|August 7, 2007
PubMed

Insights

Staurosporine (STS) induces apoptosis in SH-SY5Y cells, altering 13 key proteins. This study reveals STS-induced apoptosis triggers an unfolded protein response, indicating endoplasmic reticulum stress.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Apoptosis plays a critical role in cell death following cerebral ischemia.
  • Understanding protein level alterations during apoptosis is crucial for neuroprotection strategies.

Purpose of the Study:

  • To quantitatively define protein level changes in staurosporine (STS)-induced apoptosis in human neuroblastoma SH-SY5Y cells.
  • To investigate the involvement of endoplasmic reticulum (ER) stress and unfolded protein response (UPR) in STS-induced apoptosis.

Main Methods:

  • Quantitative proteomics using 2D gel electrophoresis (2-DE).
  • Protein identification via MALDI-TOF Mass Spectrometry (MS).
  • Treatment of SH-SY5Y cells with 500 nM STS for 6 hours to induce apoptosis.

Main Results:

  • Analysis of 154 proteins revealed significant alterations in 13 proteins due to STS treatment.
  • Ten proteins increased, including heat shock cognate 71 (Hsc71), heat shock protein 70 (Hsp70) isoforms, glucose-regulated protein 78 (GRP78), and chromatin assembly factor 1 (CAF-1).
  • Three proteins decreased: tubulin, vimentin, and glucose-regulated protein 94 (GRP94).

Conclusions:

  • STS-induced apoptosis in SH-SY5Y cells involves significant changes in molecular chaperones, cochaperones, and structural proteins.
  • These protein alterations collectively suggest the induction of an unfolded protein response (UPR) and endoplasmic reticulum (ER) stress.

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