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Related Experiment Videos

An increase in smooth endoplasmic reticulum and a decrease in Golgi apparatus occur with ionic conditions that block

J D Lindsey, R Hammerschlag, M H Ellisman

    Brain Research
    |February 2, 1981
    PubMed
    Summary

    Calcium and cobalt alter bullfrog spinal ganglia ultrastructure, increasing smooth endoplasmic reticulum (SER) and decreasing Golgi apparatus (GA) stacks. This correlates with inhibited protein transport, suggesting a calcium-dependent step in axonal transport initiation.

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    Area of Science:

    • Neuroscience
    • Cell Biology
    • Biochemistry

    Background:

    • Neuronal function relies on efficient axonal transport of proteins from the soma.
    • The precise cellular mechanisms and calcium-dependent steps initiating axonal transport remain incompletely understood.

    Purpose of the Study:

    • To investigate the ultrastructural changes in bullfrog spinal ganglia under conditions known to inhibit protein export.
    • To correlate these morphological alterations with the biochemical inhibition of fast axonal transport.

    Main Methods:

    • Analysis of bullfrog spinal ganglia ultrastructure via electron microscopy.
    • Incubation of ganglia in calcium-free medium (CFM) and/or cobalt-supplemented medium (NM--Co, CFM--Co).
    • Assessment of [3H]protein transport inhibition in dorsal root ganglion neurons.

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    Main Results:

    • Incubation with CFM, NM--Co, and CFM--Co progressively increased smooth endoplasmic reticulum (SER) volume.
    • These conditions led to a dose-dependent decrease in Golgi apparatus (GA) stack density.
    • The extent of morphological changes in SER and GA correlated directly with the inhibition of fast axonal transport.

    Conclusions:

    • The calcium-dependent step(s) in initiating axonal transport are likely localized within the neuronal soma.
    • SER and GA undergo significant morphological changes in response to altered calcium and cobalt levels, impacting protein export.
    • These findings provide insights into the cellular basis of axonal transport regulation.