A cryptic protease activity from Trypanosoma cruzi revealed by preincubation with kininogen at low temperatures

Mark F. Wiser, John D. Lonsdale-Eccles, Antonio D'Alessandro, Dennis J. Grab

Research output: Contribution to journalArticlepeer-review

Abstract

Cysteine proteases have been identified in parasitic protozoa including the causative agent of Chagas' disease Trypanosoma cruzi. T. cruzi lysates subjected to substrate containing SDS-polyacrylamide gel electrophoresis exhibit major bands of proteolytic activity in the 45-55 kDa molecular mass range (cruzipain activity). Paradoxically, addition of kininogen (a cystatin-like protease inhibitor) to the lysates before electrophoresis results in the appearance of additional bands of proteolytic activity in the 160-190 kDa molecular mass range. This inhibitor-activated protease activity depends upon the reaction conditions and exhibits novel properties. For example, a 24-48 hour preincubation at low temperature (-20°C optimum) greatly enhances the proteolytic activity. The results suggest that a metastable complex forms between kininogen and a cryptic 30 kDa cysteine protease from T. cruzi and that this complex participates in the activation of proteolytic activity.

Original languageEnglish (US)
Pages (from-to)540-544
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume240
Issue number3
DOIs
StatePublished - Nov 26 1997
Externally publishedYes

Keywords

  • Cysteine protease
  • Kinetoplastid
  • Kininogen
  • Trypanosoma cruzi

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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