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Acetylcholinesterase isozymes in developing mouse tissues

N S Henderson

    The Journal of Experimental Zoology
    |January 1, 1977
    PubMed
    Summary
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    Two acetylcholinesterase isozymes in mouse tissues change activity during development. A faster isozyme dominates embryonic stages, while a slower one prevails in adults, indicating developmental shifts in enzyme function.

    Area of Science:

    • Biochemistry
    • Developmental Biology
    • Neuroscience

    Background:

    • Acetylcholinesterase (AChE) is crucial for neurotransmission.
    • Multiple AChE isozymes exist with varying tissue distribution and developmental profiles.
    • Understanding AChE isozyme dynamics is key to comprehending neurological development and function.

    Purpose of the Study:

    • To characterize acetylcholinesterase (AChE) isozymes in mouse tissues.
    • To investigate developmental changes in AChE isozyme activity and distribution.
    • To identify specific AChE isozymes based on electrophoretic mobility and substrate specificity.

    Main Methods:

    • 10% acrylamide gel electrophoresis was used to separate AChE isozymes.
    • Mouse tissues including blood, brain, heart, muscle, and tongue were analyzed.

    Related Experiment Videos

  • Substrate specificity was assessed using acetylthiocholine iodide and butyrylthiocholine iodide.

    • Main Results:

    • Two major AChE isozymes migrating near the origin were identified.
    • A faster isozyme, specific for acetylthiocholine iodide, was prominent in embryonic tissues.
    • A slower isozyme, showing cross-reactivity with butyrylthiocholine iodide, predominated in adult tissues.
    • A developmental shift from the faster to the slower isozyme was observed from embryonic to postnatal stages.

    Conclusions:

    • Mouse tissues exhibit distinct developmental patterns of acetylcholinesterase (AChE) isozymes.
    • The identified isozymes show specific substrate preferences and electrophoretic mobilities.
    • These findings highlight the dynamic regulation of AChE during development, impacting cholinergic signaling.