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Related Experiment Videos

Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and functional characterization

D B Constam1, A R Tobler, A Rensing-Ehl

  • 1University Hospital of Zürich, Department of Internal Medicine, Switzerland.

The Journal of Biological Chemistry
|November 10, 1995
PubMed
Summary

Puromycin-sensitive aminopeptidase (PSA) is a novel enzyme involved in cell cycle regulation. Inhibiting PSA with puromycin or bestatin arrests cell division and induces apoptosis, highlighting its role in cell viability.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Proteolysis is crucial for regulating the cell division cycle.
  • The 26S proteasome is a key enzyme complex involved in proteolysis.
  • Understanding novel proteases is essential for cell cycle control research.

Purpose of the Study:

  • To analyze a novel mouse cDNA encoding puromycin-sensitive aminopeptidase (PSA).
  • To investigate the expression and localization of PSA in mammalian cells.
  • To determine the role of PSA in cell cycle progression and viability.

Main Methods:

  • cDNA cloning and expression analysis in COS cells and 3T3 fibroblasts.
  • Immunohistochemical analysis for PSA localization.
  • Cell cycle arrest and apoptosis assays using puromycin and bestatin.

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Main Results:

  • A novel mouse cDNA for puromycin-sensitive aminopeptidase (PSA) was identified and expressed.
  • PSA localizes to the cytoplasm, nucleus, and spindle apparatus during mitosis.
  • Inhibition of PSA by puromycin or bestatin induced G2/M phase arrest and apoptosis.

Conclusions:

  • PSA is a novel aminopeptidase implicated in cell cycle regulation.
  • PSA plays a critical role in cell growth and viability through proteolytic events.
  • Targeting PSA may offer new strategies for controlling cell division and inducing apoptosis.