Changes in the regulation of heat shock gene expression in neuronal cell differentiation

Jay Oza, Jingxian Yang, Kuang Yu Chen, Alice Liu

Research output: Contribution to journalArticle

24 Scopus citations


Neuronal differentiation of the NG108-15 neuroblastoma-glioma hybrid cells is accompanied by a marked attenuation in the heat shock induction of the Hsp70-firefly luciferase reporter gene activity. Analysis of the amount and activation of heat shock factor 1, induction of mRNAhsp, and the synthesis and accumulation of heat shock proteins (HSPs) in the undifferentiated and differentiated cells suggest a transcriptional mechanism for this attenuation. Concomitant with a decreased induction of the 72-kDa Hsp70 protein in the differentiated cells, there is an increased abundance of the constitutive 73-kDa Hsc70, a protein known to function in vesicle trafficking. Assessment of sensitivity of the undifferentiated and differentiated cells against stressinduced cell death reveals a significantly greater vulnerability of the differentiated cells toward the cytotoxic effects of arsenite and glutamate/glycine. This study shows that changes in regulation of the HSP and HSC proteins are components of the neuronal cell differentiation program and that the attenuated induction of HSPs likely contributes to neuronal vulnerability whereas the increased expression of Hsc70 likely has a role in neural-specific functions.

Original languageEnglish (US)
Pages (from-to)73-84
Number of pages12
JournalCell Stress and Chaperones
Issue number1
StatePublished - Mar 1 2008

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cell Biology


  • Heat shock gene expression
  • Heat shock protein
  • Neuronal cell differentiation

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