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sPLA2 appears to play an important role in the pathogenesis of dengue. We found that sPLA2 activity was significantly higher in patients with dengue haemorrhagic fever when compared to those with dengue fever, during the first 120 h of clinical illness.
The findings of this study showed that maslinic acid inhibit inflammatory effects induced by sPLA2-IIA, including foam cells formation and PGE2 production.
High PLA2 activity is associated with West Nile virus infection.
A lipidomics-based LC/MS assay was used to define the specificity of cPLA2, iPLA2, and sPLA2 toward a variety of phospholipids. A unique hydrophobic binding site for the cleaved fatty acid dominates each enzyme's specificity rather than its catalytic residues and polar headgroup binding site.
demonstration of an independent association between early-stage atherosclerosis and increased levels of sPLA2-IIa, implying that increased sPLA2-IIa may have a role in early-stage atherosclerosis in MetS patients
these results suggest that PLA2G2A polymorphisms are involved in the risk of developing metabolic syndrome and type 2 diabetes mellitus and are associated with subclinical atherosclerosis in this group of patients
PLA2G2A has a previously undiscovered impact on insulin sensitivity and metabolism
lipidomic analyses revealed that sequestration of PUFAs in LDs by sPLA2-induced TAG remodelling and retention of PUFAs in LDs by inhibition of ATGL-mediated TAG lipolysis protect from PUFA lipotoxicity.
This report provides the first demonstration that Phosphatidylcholine-Isoprostanes are readily hydrolyzed by group IIA, V and X Secretory Phospholipases A2.
Given an aberrant high level of sPLA2IIa in the tumor microenvironment that should be much higher than that in the blood, our findings support the notion that sPLA2IIa functions as a ligand for EGFR family receptors and supports CSC properties via HER/ERBB-elicited signaling, which may contribute to resistance to therapy and cancer progression
the activity of human cPLA2alpha towards a multitude of glycerophospholipids species present in micelles or bilayers, was investigated.
Mutational analysis of functional sites showed that both peroxidase and PLA2 active sites were necessary for mutant Prdx6 function, and that Prdx6 phosphorylation (at T177 residue) was essential for optimum PLA2 activity.Mutant Prdx6 at its Sumo1 sites escapes and abates this adverse process by maintaining its integrity and gaining function
sPLA2-IIA activates Integrin alphaVbeta3 and Integrin alpha4beta1 in an allosteric manner. (Review)
Leptin, at concentrations with minimal or no activating effects on astrocytoma cells, enhanced growth and migration promoted by low doses of sPLA2-IIA. sPLA2-IIA alone induced a transient phosphorylation pattern in the Src/ERK/Akt/mTOR/p70S6K/rS6 pathway through EGFR transactivation
Molecular dynamics simulations reveal structural insights into inhibitor binding modes and functionality in human PLA2G2A.
Hepatitis B virus can upregulate the expression of PLA2G2A, and serum levels of PLA2G2A are associated with the progression of hepatitis to liver cirrhosis and hepatocellular carcinoma.
Dimethyl ester of bilirubin exhibits anti-inflammatory activity through inhibition of secretory phospholipase A2, lipoxygenase and cyclooxygenase.
High expression of PLA2G2A was associated with poor therapeutic response and worse survival in patients with rectal cancer receiving neoadjuvant concurrent cheomoradiotherapy (CCRT).
Data show that phospholipase A2 group IIA, V and X have different target/function related activity.
Polyozellin might play an important role in the modulation of sPLA2-IIA expression and activity in response to the inflammatory diseases.
The protein encoded by this gene is a member of the phospholipase A2 family (PLA2). PLA2s constitute a diverse family of enzymes with respect to sequence, function, localization, and divalent cation requirements. This gene product belongs to group II, which contains secreted form of PLA2, an extracellular enzyme that has a low molecular mass and requires calcium ions for catalysis. It catalyzes the hydrolysis of the sn-2 fatty acid acyl ester bond of phosphoglycerides, releasing free fatty acids and lysophospholipids, and thought to participate in the regulation of the phospholipid metabolism in biomembranes. Several alternatively spliced transcript variants with different 5' UTRs have been found for this gene.
, group IIA phospholipase A2
, non-pancreatic secretory phospholipase A2
, phosphatidylcholine 2-acylhydrolase 2A
, phospholipase A2, membrane associated
, eted enzyme type IIA phospholipase A2
, platelet phospholipase A2
, enhancing factor
, modifier of Min1
, non-pancreatic secreted type II phospholipase A2
, secretory group II phospholipase A2
, typeII phospholipase A2