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Related Experiment Videos

Processing and sorting of the prohormone convertase 2 propeptide.

L Muller1, A Cameron, Y Fortenberry

  • 1Department of Biochemistry and Molecular Biology, LSU Health Sciences Center, New Orleans, Louisiana 70112, USA.

The Journal of Biological Chemistry
|September 21, 2000
PubMed
Summary

The prohormone convertase 2 (PC2) propeptide is crucial for catalytic site folding and activity. Its cleavage site, not internal processing, is key for PC2 activation and function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Prohormone convertases (PCs) are essential proteases synthesized as inactive zymogens.
  • PC zymogens feature propeptides with multibasic cleavage sites, crucial for maturation and activity regulation.

Purpose of the Study:

  • Investigate the processing of the prohormone convertase 2 (PC2) propeptide.
  • Determine the role of PC2 propeptide processing in regulating PC2 activity and catalytic site folding.

Main Methods:

  • Purified pro-PC2 and directed mutagenesis were employed to study propeptide cleavage.
  • Synthetic peptides were used to identify inhibitory sequences within the PC2 propeptide.

Main Results:

  • PC2 propeptide undergoes primary cleavage, followed by sequential internal processing, but internal cleavage is not required for activation.

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  • A mutation at the primary cleavage site yielded inactive PC2, indicating its role in catalytic site folding.
  • PC2 propeptide fragments inhibit PC2 activity, with inhibition localized to the carboxyl terminus of the primary cleavage site.
  • PC2 propeptide is processed within secretory granules, and fragments can be released upon stimulated secretion.

    • Conclusions:

    • PC2 propeptide cleavage, particularly at the primary site, is essential for proper catalytic site folding and enzyme activity.
    • The PC2 propeptide acts as an inhibitor, with its carboxyl-terminal region being the inhibitory domain.
    • Prohormone convertase 2 processing and intracellular fate occur within secretory granules, with potential implications for secretion regulation.