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Related Experiment Videos

Ceramide 1-phosphate phosphatase activity in brain

R Shinghal1, R H Scheller, S M Bajjalieh

  • 1Department of Molecular and Cellular Physiology, Stanford University, California 94305-5428.

Journal of Neurochemistry
|December 1, 1993
PubMed
Summary

This study identifies ceramide 1-phosphate phosphatase (CPPase) as a key enzyme in neurotransmitter release. CPPase regulates ceramide 1-phosphate metabolism at the synapse, impacting vesicle function.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Sphingolipids play crucial roles in intracellular signaling.
  • Ceramide kinase, found with neurotransmitter vesicles, suggests a role for ceramide metabolites in neurotransmitter release.

Purpose of the Study:

  • To investigate the metabolic fate of ceramide 1-phosphate, a product of ceramide kinase.
  • To understand the role of ceramide kinase in synaptic vesicle functioning.

Main Methods:

  • Enzyme assays to characterize ceramide 1-phosphate metabolism.
  • Subcellular fractionation to determine the localization of ceramide 1-phosphate phosphatase (CPPase).

Main Results:

  • Ceramide 1-phosphate is not deacylated by brain ceramidases.

Related Experiment Videos

  • A novel phosphatase activity, ceramide 1-phosphate phosphatase (CPPase), was identified.
  • CPPase is localized to synaptic terminals, associated with synaptic vesicle and plasma membranes.
  • Divalent cations, particularly calcium, inhibit CPPase activity.

    • Conclusions:

    • The presence of both ceramide kinase and CPPase at the synapse indicates a regulatory role for ceramide 1-phosphate metabolism in synaptic vesicle function.
    • Ceramide 1-phosphate production is a critical step in regulating neurotransmitter release.