Activation of the glycosylphosphatidylinositol-anchored membrane proteinase upon release from Herpetomonas samuelpessoai by phospholipase C

André Luis Souza Dos Santos, Celina Monteiro Abreu, Celuta Sales Alviano, Rosangela Maria De Araújo Soares

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

We have analyzed the effects of exogenous phospholipase C (PLC) on the cell-surface polypeptides and proteinases of Herpetomonas samuelpessoai grown in chemically defined conditions by SDS-PAGE gels. Live parasites treated with PLC released into the extracellular medium a complex profile of glycosylphosphatidylinositol (GPI)-anchored polypeptides ranging from 15 to 100 kDa, some of them with proteolytic activity. Two major metalloproteinases with apparent molecular masses of 63 and 115 kDa were observed after PLC hydrolysis. Interestingly, only the PLC-released soluble form of the 115-kDa metalloenzyme, and not the membrane-anchored form, displayed proteolytic activity, demonstrating that cleavage of the GPI anchor can lead to enzymatic activation.

Original languageEnglish (US)
Pages (from-to)293-298
Number of pages6
JournalCurrent Microbiology
Volume45
Issue number4
DOIs
StatePublished - Oct 1 2002
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Applied Microbiology and Biotechnology

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