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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 (show EGFR Proteins) family receptors and supports CSC properties via HER/ERBB (show EGFR Proteins)-elicited signaling, which may contribute to resistance to therapy and cancer progression
the activity of human cPLA2alpha (show PLA2G4A Proteins) towards a multitude of glycerophospholipids species present in micelles or bilayers, was investigated.
Mutational analysis of functional sites showed that both peroxidase and PLA2 (show YWHAZ Proteins) active sites were necessary for mutant Prdx6 (show PRDX6 Proteins) function, and that Prdx6 (show PRDX6 Proteins) phosphorylation (at T177 residue) was essential for optimum PLA2 (show YWHAZ Proteins) activity.Mutant Prdx6 (show PRDX6 Proteins) at its Sumo1 (show SUMO1 Proteins) sites escapes and abates this adverse process by maintaining its integrity and gaining function
sPLA2-IIA activates Integrin alphaVbeta3 (show ITGAV Proteins) and Integrin alpha4beta1 in an allosteric manner. (Review)
Leptin (show LEP Proteins), 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 (show SRC Proteins)/ERK (show EPHB2 Proteins)/Akt (show AKT1 Proteins)/mTOR (show FRAP1 Proteins)/p70S6K (show RPS6KB1 Proteins)/rS6 pathway through EGFR (show EGFR Proteins) 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 (show YWHAZ Proteins), 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).
transgenic mice overexpressing sPLA2 -IIA keratinocytes showed enhanced activation of EGFR (show EGFR Proteins) and JNK1 (show MAPK8 Proteins)/2 that led to c-Jun (show JUN Proteins) 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.
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 (show PLA2G6 Proteins)) and Group X Secreted Phospholipase A2 (show YWHAZ Proteins) (sPLA2).
Data show that the coordinated action of phospholipase A2 (show YWHAZ Proteins) IIA (sPLA2-IIA) and 12-lipoxygenase (12-LO (show ALOX15 Proteins)) 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