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A lipidomics-based LC/MS assay was used to define the specificity of cPLA2 (Montrer PLA2G4A Protéines), iPLA2 (Montrer PLA2G6 Protéines), 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 (Montrer ETV3 Protéines) 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 (Montrer INS Protéines) 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 (Montrer PNPLA2 Protéines)-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 (Montrer EGFR Protéines) family receptors and supports CSC properties via HER/ERBB (Montrer EGFR Protéines)-elicited signaling, which may contribute to resistance to therapy and cancer progression
the activity of human cPLA2alpha (Montrer PLA2G4A Protéines) towards a multitude of glycerophospholipids species present in micelles or bilayers, was investigated.
Mutational analysis of functional sites showed that both peroxidase and PLA2 (Montrer YWHAZ Protéines) active sites were necessary for mutant Prdx6 (Montrer PRDX6 Protéines) function, and that Prdx6 (Montrer PRDX6 Protéines) phosphorylation (at T177 residue) was essential for optimum PLA2 (Montrer YWHAZ Protéines) activity.Mutant Prdx6 (Montrer PRDX6 Protéines) at its Sumo1 (Montrer SUMO1 Protéines) sites escapes and abates this adverse process by maintaining its integrity and gaining function
sPLA2-IIA activates Integrin alphaVbeta3 (Montrer ITGAV Protéines) and Integrin alpha4beta1 in an allosteric manner. (Review)
transgenic mice overexpressing sPLA2 -IIA keratinocytes showed enhanced activation of EGFR (Montrer EGFR Protéines) and JNK1 (Montrer MAPK8 Protéines)/2 that led to c-Jun (Montrer JUN Protéines) activation.
PLA2 promotes pulmonary inflammation and systemic disease during Streptococcus pneumoniae infection.
secretory PLA2s have important functions as genetic modifiers of inflammation and colon cancer.
Dimethyl ester of bilirubin exhibits anti-inflammatory activity through inhibition of secretory phospholipase A2 (Montrer YWHAZ Protéines), lipoxygenase and cyclooxygenase.
Polyozellin might play an important role in the modulation of sPLA2-IIA expression and activity in response to the inflammatory diseases.
Progesterone-induced Acrosome Exocytosis Requires Sequential Involvement of Calcium-independent Phospholipase A2beta (iPLA2beta (Montrer PLA2G6 Protéines)) and Group X Secreted Phospholipase A2 (Montrer YWHAZ Protéines) (sPLA2).
Data show that the coordinated action of phospholipase A2 (Montrer YWHAZ Protéines) IIA (sPLA2-IIA) and 12-lipoxygenase (12-LO (Montrer ALOX15 Protéines)) promotes inflammatory arthritis.
Pla2g2a sequence varies between tumor resistant and sensitive mouse strains. Some of these variations in the promoter region affect Pla2g2a expression and nonsense-mediated RNA decay also contributes to reducing Pla2g2a mRNA in tumor-sensitive strains.
hydrolysis of the mitochondrial membrane by sPLA2-IIA yields inflammatory mediators (ie, lysophospholipids, fatty acids, and mtDNA) that promote leukocyte activation
Ionomycin causes susceptibility to phospholipase A2 while temperature-induced increases in membrane fluidity fail: possible involvement of actin fragmentation.
PLA2G2A production is induced by Pseudomonas aeruginosa.
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