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Related Experiment Videos

Rat brain synaptosomal ATP:AMP-phosphotransferase activity.

A K Nagy1, T A Shuster, A V Delgado-Escueta

  • 1Department of Neurology, UCLA Center for Health Sciences 90024.

Journal of Neurochemistry
|October 1, 1989
PubMed
Summary

Adenylate kinase, an enzyme crucial for cellular energy, was found in rat brain synaptosomes. This suggests a potential role for this enzyme on the cell surface, acting as an ecto-enzyme.

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Area of Science:

  • Neurochemistry
  • Enzymology
  • Cellular Biology

Background:

  • Adenylate kinase (ATP:AMP-phosphotransferase; EC 2.7.4.3) plays a key role in cellular energy homeostasis.
  • Investigating its localization and function in different subcellular fractions of brain tissue is essential for understanding neuronal energy metabolism.

Purpose of the Study:

  • To characterize adenylate kinase activity in various subcellular fractions of rat brain.
  • To determine the specific localization and potential ecto-enzymatic nature of adenylate kinase in synaptosomes.

Main Methods:

  • Adenylate kinase activity was assayed in forward and reverse directions using coupled enzyme systems and a specific inhibitor (P1,P5-di(adenosine-5') pentaphosphate).
  • Subcellular fractions, including cytosol and intact synaptosomes isolated via Percoll/sucrose gradients, were analyzed.

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  • Kinetic parameters of membrane-bound and cytosolic enzyme forms were compared.

    • Main Results:

    • The highest specific adenylate kinase activity was observed in the cytosolic fraction (2.89 μmol/min/mg protein).
    • Substantial activity (0.68 μmol/min/mg) was also detected in intact synaptosomes.
    • Synaptosomal adenylate kinase activity showed distinct kinetic parameters compared to the cytosolic form and adhered to synaptic plasma membranes, resisting release by isoosmotic sucrose washes.

    Conclusions:

    • Synaptosomal adenylate kinase activity is unlikely due to cytosolic contamination.
    • The enzyme's association with synaptic plasma membranes and its activity in intact synaptosomes suggest it may function as an ecto-enzyme.
    • Further investigation is warranted to confirm the ecto-enzymatic role of synaptosomal adenylate kinase.