Novel acidic phospholipase A2 from Porthidium hyoprora causes inflammation with mast cell rich infiltrate

Petrus Pires Marques, Alessandra Esteves, Marcelo Lancellotti, Luis Alberto Ponce-Soto, Sergio Marangoni

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

Phospholipases A2 (PLA2) are a group of enzymes that hydrolyze phospholipids at the sn-2 position, being present in all nature. In venomous animals, these proteins assume a special role, being able to exert diverse pharmacological effects. In this work, authors identified a new isoform of PLA2 in the venom of Porthidium hyoprora, which was isolated through sequential chromatographic steps and named PhTX-III. The enzyme was characterized biochemically and structurally. Structural studies using mass spectrometry confirmed an acidic secretory PLA2, family IIA, with molecular mass of 13,620.9Da and identification of 86% of its primary sequence. PhTX-III did not exhibit myotoxic, anticoagulant or antibacterial effects, often present in this class of enzymes. Although, it was capable of initiate inflammatory response, with local edema and release of cytokines IL-1α, IL-6 and TNF-α, probably due to mast cell degranulation.

Original languageEnglish
Pages (from-to)78-84
Number of pages7
JournalBiochemistry and Biophysics Reports
Volume1
Issue number1
DOIs
StatePublished - 2015
Externally publishedYes

Keywords

  • Edema forming activity
  • Inflammatory activity
  • PhTX-III
  • Pro-inflammatory cytokines

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