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Related Experiment Videos

PACE4: a subtilisin-like endoprotease with unique properties

R E Mains1, C A Berard, J B Denault

  • 1Department of Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185, U.S.A.

The Biochemical Journal
|February 1, 1997
PubMed
Summary

PACE4, a neuroendocrine-specific protease, is synthesized and secreted differently than other prohormone convertases. Its unique properties suggest roles beyond peptide biosynthesis in neuroendocrine cells.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Neuroendocrinology

Background:

  • PACE4 is a neuroendocrine-specific mammalian subtilisin-related endoprotease involved in the secretory pathway.
  • Its biosynthesis and secretion are crucial for understanding neuroendocrine function.

Purpose of the Study:

  • To investigate the biosynthesis, secretion, and enzymatic properties of PACE4.
  • To compare PACE4 with other prohormone convertases and determine its unique characteristics.

Main Methods:

  • Studied PACE4 using transfected neuroendocrine and fibroblast cell lines, and primary pituitary cultures.
  • Analyzed pro-PACE4 cleavage, secretion kinetics, and enzyme inhibition profiles.

Main Results:

  • ProPACE4 cleavage is accelerated in a truncated form (PACE4s).

Related Experiment Videos

  • PACE4 and PACE4s are not stored in regulated neuroendocrine secretory granules.
  • PACE4 exhibits distinct enzyme activity, sensitive to leupeptin but not Ca2+ chelators or dithiothreitol, and resistant to alpha1-antitrypsin Portland variant.

    • Conclusions:

    • PACE4's unique biosynthetic and enzymatic profile suggests a role outside classical peptide biosynthesis pathways.
    • PACE4 functions distinctly from furin and other prohormone convertases in neuroendocrine systems.