Proteomic analysis of lipopolysaccharide-induced apoptosis in PC12 cells

Ya Hui Huang, Alice Y.W. Chang, Chun Ming Huang, Shiow Wen Huang, Samuel H.H. Chan*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

38 Scopus citations


We employed rat pheochromocytoma PC12 cells as our model system to identify cellular proteins that accompany Escherichia coli lipopolysaccharide (LPS)-induced apoptosis, based on a proteomic approach. Cell viability tests revealed that naïve PC12 cells underwent cell death in a dose-dependent manner after treatment with LPS. Flow cytometric analysis confirmed that apoptosis was primarily responsible for the observed cell death. Two-dimensional electrophoresis in conjunction with N-terminal sequencing, immunoblot, matrix-assisted laser desorption/ionization-time of flight analysis or computer matching with protein databases further revealed that the LPS-induced apoptosis is accompanied by an augmented level of calreticulin, calcium binding protein 50, endoplasmic reticulum protein 60 (ERP60), heat shock protein 60 (HSP60) or HSP90, and a reduced level of amphoterin, cytochrome c oxidase polypeptide Vla-liver or ERP29. These proteins are associated with endoplasmic reticulum, mitochondria or cell membrane, and are with known or potential roles in apoptosis. Their identification therefore provides an impetus for further delineation of the cellular and molecular basis of apoptotic cell death and sepsis based on proteomic profiling of PC12 cells.

Original languageEnglish
Pages (from-to)1220-1228
Number of pages9
Issue number9
StatePublished - 01 09 2002
Externally publishedYes


  • Apoptosis
  • Lipopolysaccharide
  • PC12 cells
  • Proteome map
  • Two-dimensional gel electrophoresis


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