Dataset Information

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

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 13,620.9 Da 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-1?, IL-6 and TNF-?, probably due to mast cell degranulation.

SUBMITTER: Marques PP

PROVIDER: S-EPMC5668520 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

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

Marques Petrus Pires PP Esteves Alessandra A Lancellotti Marcelo M Ponce-Soto Luis Alberto LA Marangoni Sergio S

Biochemistry and biophysics reports 20150324

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 biochemicall ...[more]

PMID: 29124136

Similar Datasets

Project description:Lipoprotein-associated phospholipase A(2) (Lp-PLA(2)), also known as platelet-activating factor acetylhydrolase (PAF-AH), is a unique member of the phospholipase A(2) superfamily. This enzyme is characterized by its ability to specifically hydrolyze PAF as well as glycerophospholipids containing short, truncated, and/or oxidized fatty acyl groups at the sn-2 position of the glycerol backbone. In humans, Lp-PLA(2) circulates in active form as a complex with low- and high-density lipoproteins. Clinical studies have reported that plasma Lp-PLA(2) activity and mass are strongly associated with atherogenic lipids and vascular risk. These observations led to the hypothesis that Lp-PLA(2) activity and/or mass levels could be used as biomarkers of cardiovascular disease and that inhibition of the activity could offer an attractive therapeutic strategy. Darapladib, a compound that inhibits Lp-PLA(2) activity, is anti-atherogenic in mice and other animals, and it decreases atherosclerotic plaque expansion in humans. However, disagreement continues to exist regarding the validity of Lp-PLA(2) as an independent marker of atherosclerosis and a scientifically justified target for intervention. Circulating Lp-PLA(2) mass and activity are associated with vascular risk, but the strength of the association is reduced after adjustment for basal concentrations of the lipoprotein carriers with which the enzyme associates. Genetic studies in humans harboring an inactivating mutation at this locus indicate that loss of Lp-PLA(2) function is a risk factor for inflammatory and vascular conditions in Japanese cohorts. Consistently, overexpression of Lp-PLA(2) has anti-inflammatory and anti-atherogenic properties in animal models. This thematic review critically discusses results from laboratory and animal studies, analyzes genetic evidence, reviews clinical work demonstrating associations between Lp-PLA(2) and vascular disease, and summarizes results from animal and human clinical trials in which administration of darapladib was tested as a strategy for the management of atherosclerosis.

Dataset Information

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

Publications

Novel acidic phospholipase A<sub>2</sub> from <i>Porthidium hyoprora</i> causes inflammation with mast cell rich infiltrate.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets