Redox factor 1 inhibits the apoptosis process after intracerebral hemorrhage

Neurol Res. 2011 Sep;33(7):681-5. doi: 10.1179/1743132810Y.0000000021.

Abstract

Objective: To determine the role of redox factor 1 (Ref-1) in the apoptotic process in perihematoma brain tissue from intracerebral hemorrhage (ICH) patients.

Methods: Thirty ICH patients were selected, and normal brain tissue, inevitably lost during surgery, was used as the control group, while the brain tissue from 1 cm around the hematoma was used as the experimental group. Experimental tissues were further divided according to the time from syndrome onset to the time of operation as follows: <6 hours (n = 6); 6-12 hours (n = 7); 12-24 hours (n = 5); 24-72 hours (n = 6); and >72 hours (n = 6). Apoptotic cells were observed by the terminal deoxynucleotidyl transferase-mediated deoxyuridine 5-triphosphate nick-end labeling (TUNEL) reaction. Protein and mRNA expression of Ref-1 and Bax were determined by immunohistochemistry and reverse transcription polymerase chain reaction (RT-PCR) respectively.

Results: Immunohistochemistry indicated that Ref-1 expression was the maximal in control tissue, while it slowly declined to a nadir between 12 and 72 hours in the experimental tissue. Bax expression was the lowest in the control tissue, and gradually increased from 12 to 72 hours in the experimental tissue. RT-PCR data showed that patterns of Ref-1 and Bax expression similar to the immunohistochemistry results. Correlation analysis demonstrated a negative correlation among Ref-1, apoptosis, and Bax.

Conclusion: Ref-1 may play an important role in protecting brain cells and may be able to inhibit apoptosis following ICH.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis / physiology*
  • Case-Control Studies
  • Cerebral Hemorrhage / metabolism*
  • Cerebral Hemorrhage / physiopathology
  • DNA-(Apurinic or Apyrimidinic Site) Lyase / biosynthesis*
  • Humans
  • In Situ Nick-End Labeling
  • Reverse Transcriptase Polymerase Chain Reaction
  • bcl-2-Associated X Protein / biosynthesis

Substances

  • bcl-2-Associated X Protein
  • APEX1 protein, human
  • DNA-(Apurinic or Apyrimidinic Site) Lyase