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Related Experiment Videos

Rapid postmortem decrease in the ectocellular acetylcholinesterase activity in rat striatum as assessed by in vivo

G Testylier1, P Gourmelon, D Clarençon

  • 1Centre de Recherches du Service de Santé des Armées, Grenoble, France.

Brain Research
|December 6, 1991
PubMed
Summary
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Acetylcholinesterase (AChE) activity in rat striatum drastically decreases postmortem. This rapid enzymatic decline, observed using in vivo microspectrophotometry, suggests localized cellular regulation rather than just temperature or pH changes.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Enzymology

Background:

  • Acetylcholinesterase (AChE) is a key enzyme in cholinergic neurotransmission.
  • Understanding AChE activity regulation is crucial for neuroscience research.
  • Postmortem changes in enzyme activity can complicate experimental interpretations.

Purpose of the Study:

  • To investigate the rapid postmortem changes in acetylcholinesterase (AChE) activity in the rat striatum.
  • To determine the extent and potential causes of this postmortem decline.
  • To explore the possibility of endogenous regulation of AChE activity in vivo.

Main Methods:

  • In vivo microspectrophotometry was employed to monitor AChE activity in the rat striatum.
  • The Ellman colorimetric reaction was measured directly within the brain using an implanted optical probe.

Related Experiment Videos

  • Local cyanide injections were used to assess cellular-level effects on enzymatic activity.

    • Main Results:

    • A significant postmortem decrease in AChE activity (35-50%) was observed within 10 minutes after death.
    • Changes in brain temperature, pH, and optical properties accounted for only a small fraction (16%) of the observed activity fall.
    • Local cyanide administration induced a substantial decrease in AChE activity (40%), comparable to postmortem levels.

    Conclusions:

    • The rapid postmortem decline in striatal AChE activity is primarily due to localized cellular events, not solely physical or chemical changes.
    • The findings suggest the existence of an endogenous regulatory mechanism for AChE activity in vivo that ceases shortly after death.
    • In vivo microspectrophotometry provides a valuable tool for studying dynamic changes in enzyme activity within the brain.