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Related Experiment Videos

Mn2+-stimulated ATPase in rat brain.

J D Doherty, N Salem, C J Lauter

    Neurochemical Research
    |April 1, 1983
    PubMed
    Summary
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    Divalent cation ATPases in rat brain synaptic vesicles were optimally stimulated by manganese (Mn2+), while plasma membranes from various brain regions and nerves preferred magnesium (Mg2+). This suggests Mn2+ may play a key role in cellular metabolism and toxicity.

    Area of Science:

    • Neuroscience
    • Biochemistry
    • Cell Biology

    Background:

    • Divalent cations like manganese (Mn2+), magnesium (Mg2+), and calcium (Ca2+) are crucial for numerous cellular processes.
    • Adenosine triphosphatases (ATPases) are enzymes that hydrolyze ATP, utilizing divalent cations as cofactors.
    • Understanding the specific cation requirements of different ATPases is vital for elucidating their physiological roles.

    Purpose of the Study:

    • To investigate the optimal divalent cation stimulation (Mn2+, Mg2+, or Ca2+) for ATPases in distinct rat neural preparations.
    • To differentiate between Mn2+- and Mg2+-dependent ATPases in synaptic vesicles and plasma membranes.
    • To explore the potential physiological and toxicological significance of Mn2+ interaction with ATPases.

    Main Methods:

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  • Preparation of ATPase-rich fractions from rat brain synaptic vesicles, synaptosomal plasma membranes, and brain stem/sciatic nerve plasma membranes.
  • Assay of ATPase activity under varying concentrations of Mn2+, Mg2+, and Ca2+ to determine optimal cation stimulation.
  • Analysis of enzyme properties, including chemical inactivation and substrate preferences, to distinguish between different ATPase activities.

    • Main Results:

    • ATPase activity in the synaptic vesicle subfraction showed optimal stimulation by Mn2+.
    • All plasma membrane preparations, including those from synaptosomes, brain stem, and sciatic nerve, were optimally stimulated by Mg2+.
    • No distinct Mn2+- and Mg2+-ATPases could be identified based on chemical inactivation or substrate specificity.

    Conclusions:

    • Synaptic vesicle ATPases exhibit a preference for Mn2+ stimulation, distinct from the Mg2+ preference of plasma membrane ATPases.
    • The study suggests a potential physiological or toxicological role for Mn2+ in cellular metabolism due to its interaction with ATPases at micromolar concentrations.
    • Further research is warranted to fully elucidate the biological significance of Mn2+-ATPase interactions.