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Hepatocyte isolation stimulates formation of interferon stimulatory response element DNA-protein complexes

C L Varley1, A J Dickson

  • 1School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester, M13 9PT, United Kingdom. CVARLEY@FS1.SCG.MAN.AC.UK

Biochemical and Biophysical Research Communications
|October 8, 1999
PubMed

Insights

Hepatocyte isolation activates the interferon stimulatory response element (ISRE) pathway, involving interferon regulatory factor-1 (IRF-1) and p38 kinase. This pathway may contribute to the loss of differentiated function in cultured hepatocytes.

Area of Science:

  • Cell Biology
  • Hepatology
  • Molecular Biology

Background:

  • Primary hepatocytes lose differentiated function during isolation and culture.
  • Intracellular signaling pathways are implicated in this functional decline.

Purpose of the Study:

  • To investigate the relationship between intracellular signaling and loss of differentiated function in hepatocytes.
  • To identify specific signaling molecules involved in hepatocyte culture-induced changes.

Main Methods:

  • Hepatocyte isolation and culture.
  • Analysis of interferon stimulatory response element (ISRE) activation.
  • Electromobility shift assays and supershift assays to study Interferon regulatory factor-1 (IRF-1) binding.
  • Use of p38 kinase inhibitor (SB 203580).

Main Results:

  • Hepatocyte isolation transiently activated ISRE, peaking at 3 hours.
  • Interferon regulatory factor-1 (IRF-1) was crucial for ISRE complex formation and translocated to the nucleus.
  • p38 kinase inhibition reduced ISRE binding complex formation, suggesting its involvement.

Conclusions:

  • p38 kinase signaling pathway is involved in ISRE activation and IRF-1 binding in hepatocytes.
  • ISRE activation dynamics in cultured hepatocytes may impact primary hepatocyte differentiation and function.

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