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Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis
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Elastase secretion in Acanthamoeba polyphaga.

Gabriela A Ferreira1, Ana C M Magliano, Elizabeth M F Pral

  • 1Departamento de Parasitologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, CEP 05508-000 São Paulo, Brazil.

Acta Tropica
|July 28, 2009
PubMed
Summary

Acanthamoeba trophozoites secrete elastases, primarily high molecular weight serine peptidases. These enzymes contribute to tissue damage in Acanthamoeba infections, with activity observed across a broad pH range.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Parasitology

Background:

  • Acanthamoeba species are ubiquitous in soil and water.
  • Certain Acanthamoeba species cause human diseases like keratitis and opportunistic infections.
  • Secreted peptidases, especially serine peptidases, are implicated in Acanthamoeba-induced tissue damage.

Purpose of the Study:

  • To investigate elastase activity in Acanthamoeba-conditioned medium (ACM).
  • To characterize the types and properties of peptidases secreted by Acanthamoeba trophozoites.
  • To identify potential elastase candidates involved in pathogenicity.

Main Methods:

  • Enzyme activity assays using elastin-Congo red (ECR) and synthetic peptide p-nitroanilide substrates.
  • Inhibition studies with specific protease inhibitors (PMSF, antipain, chymostatin, EDTA, etc.).
  • Protein purification using ammonium sulfate precipitation, Fast Protein Liquid Chromatography (FPLC), and CM-sepharose chromatography.
  • Detection of enzyme activity using gelatin zymography.

Main Results:

  • ACM exhibited broad pH elastase activity, optimal at pH 7.5 and above, inhibited by serine and metallopeptidase inhibitors.
  • Synthetic substrate screening indicated significant serine peptidase activity, particularly against Suc-Ala(2)-Pro-Leu-pNA and Suc-Ala(2)-Pro-Phe-pNA.
  • Purification revealed that ECR-splitting activity, identified as serine peptidases, co-eluted with Suc-Ala(2)-Pro-Phe-pNA hydrolyzing activity.
  • Gelatin zymography detected serine peptidases in the 70-130kDa range in active FPLC fractions.

Conclusions:

  • Acanthamoeba trophozoites secrete active elastases.
  • High molecular weight serine peptidases are identified as likely candidates for elastase activity.
  • These secreted elastases may play a significant role in Acanthamoeba pathogenesis and tissue invasion.