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Related Experiment Videos

Elastase-like activity in cultured aortic endothelial cells.

S Menashi1, W Hornebeck, L Robert

  • 1INSERM U 150, CNRS UA 334, Hôpital St-Louis, Paris, France.

Thrombosis Research
|January 1, 1989
PubMed
Summary

Researchers investigated elastase activity in porcine aortic endothelial cells. A membrane-bound enzyme hydrolyzed synthetic substrates, while a separate, secreted enzyme degraded elastin, suggesting an inhibitor was present in the culture medium.

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Area of Science:

  • Cell biology
  • Biochemistry
  • Enzymology

Background:

  • Endothelial cells play crucial roles in vascular health.
  • Elastase activity is implicated in various physiological and pathological processes.
  • Understanding enzyme localization and activity is vital for vascular research.

Purpose of the Study:

  • To characterize cellular and secreted elastase activity in cultured porcine aortic endothelial cells.
  • To differentiate between enzymes acting on synthetic substrates and those degrading native elastin.
  • To investigate the presence and nature of potential inhibitors in the cell culture medium.

Main Methods:

  • Culturing porcine aortic endothelial cells.
  • Assaying enzyme activity using synthetic elastase substrates (succinyl(alanine)3 nitroanilide).

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  • Assessing elastin degradation using insoluble elastin.
  • Fractionating culture medium using gel filtration high-performance liquid chromatography (HPLC).

    • Main Results:

    • A membrane-located enzyme activity was identified, hydrolyzing synthetic substrates but not elastin.
    • A distinct neutral proteinase activity capable of degrading insoluble elastin was found in the fractionated culture medium.
    • Direct detection of elastinolytic activity in the conditioned medium was not observed.

    Conclusions:

    • Porcine aortic endothelial cells possess both membrane-bound and secreted enzymatic activities related to elastase.
    • The secreted enzyme responsible for elastin degradation may be masked by an endogenous inhibitor in the conditioned medium.
    • Further investigation is needed to isolate and characterize the secreted elastin-degrading proteinase and its inhibitor.