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Dog (Canine) Polyclonal YWHAZ Primary Antibody für ELISA, WB - ABIN548004
Kolko, Christoffersen, Varoqui, Bazan: Expression and induction of secretory phospholipase A2 group IB in brain. in Cellular and molecular neurobiology 2006
identified the radish gene by positional cloning and comparative sequencing, finding a mutant stop codon in gene CG15720 from the Drosophila Genome Project
sPLA2-IB was correlated with the level of proteinuria in membranous nephropathy patients suggesting to be a potential biomarker for monitoring disease severity and therapeutic effects of both primary membranous nephropathy and secondary membranous nephropathy.
The sPLA2 IB-PLA2R interaction stimulated podocyte apoptosis through activating ERK1/2 and cPLA2alpha and through increasing the podocyte AA content
TNF-alpha-induced cPLA2 expression and PGE2 release were mediated through a Jak2/PDGFR/PI3K/Akt/p42/p44 MAPK/Elk-1 pathway in human lung epithelial cells.
Exogenously added sPLA(2)-IB decreases phagocytosis of photoreceptor outer segments regardless of enzymatic activity.
stimulation of three isoforms of PLA2 by thapsigargin liberates free AA that, in turn, induces capacitative calcium influx in human T-cells
results indicate a selective sorting of a cell-derived cPLA2 during human cytomegalovirus maturation, which is further required for infectivity
Group IB phospholipase A2 (PLA2G1B) stimulates leukotriene B4 (LTB4) production in the absence of cytochalasin B in human neutrophils.
Here, we report sPLA2-IB in rat and human brain as well as in neurons in primary culture. The distribution of sPLA2-IB seems to be mainly neuronal, with the highest abundance occurring in the cerebral cortex and hippocampus.
a critical regulatory role of arachidonate reacylation that limits leukotriene biosynthesis in concert with 5-lipoxygenase and cytosolic phospholipase A(2)alpha activation
Results describe the structural basis for bile salt inhibition of pancreatic phospholipase A2.
MMP-2/9 production is regulated by sPLA2-IB acting as a receptor ligand to activate cPLA2
pro-hG1B forms a trimer and PROP occupies the catalytic cavity and can be self-cleaved at 37 degrees C; A new membrane-bound surface and activation mechanism are proposed based on the trimeric model of pro-hG1B
Equilibrium unfolding of porcine pancreatic phospholipase A2 was monitored using multiple approaches. An unusually broad unfolding transition at remarkably high denaturant concentration was observed.
Porcine group IB secretory phospholipase A2 (PLA2G1B) stimulates the expression and secretion of CXC chemokine ligand 8 (CXCL8) in human neutrophils without affecting other proinflammatory cytokines.
Porcine pancreatic PLA(2) shows a long lag phase of several hours during which the enzyme binds to the bilayer surface, but only 5+/-3% of the lipids react before the onset of rapid hydrolysis.
Results show that the decylsulfate epitope for the successive E i (#) complexes increasingly resembles the micellar complex formed by the binding of PLA2 to preformed micelles.
An increased sPLA(2) activity and a reduced inhibition may play an important role in the pathogenesis of ischemia-reperfusion injury of non-heart-beating donor liver grafts.
Interfacial activation of pig pancreatic IB phospholipase A(2) (PLA2) is modeled in terms of the three discrete premicellar complexes (E(i)(#), i = 1, 2, or 3) consecutively formed by the cooperative binding of a monodisperse amphiphile to the i-face
Phospholipase A2 isoforms are differentially regulated; they selectively participate in retinal signaling in an experimental model of age-related macular degeneration.
results suggest the hydrophobic surfactant protein, SP-B, protects alveolar surfactant phospholiopids from hydrolysis mediated by multiple sPLA(2) in both vesicles (alveolar subphase) and monomolecular films (air-liquid interface)
crystal structure of the triple mutant pancreatic phospholipase A2 with calcium.
NMR characterization of a unique low-barrier hydrogen bond between an active site residue from the enzyme and a bound inhibitor: the complex between secreted phospholipase A(2) (sPLA(2), from bovine pancreas) and a transition-state analog inhibitor HK32
The final protein model consists of 123 amino-acid residues, two calcium ions, one chloride ion, 243 water molecules and six 2-methyl-2,4-pentanediol molecules.
The crystal structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2 complexed with an organic molecule, p-methoxybenzoic acid (anisic acid), is reported.
The quadruple mutant of phospholipase A2 has monoclinic or trigonal crystal structures and results suggested evidence for the involvement of the second calcium and surface loop in interfacial binding.
Pla2g1b inactivation suppressed diet-induced body weight gain and reduced diabetes and atherosclerosis in LDL receptor-deficient mice.
Exogenously added sPLA(2)-IB decreases phagocytosis of outer retinal segments regardless of enzymatic activity.
inhibition of Pla2g1b protects against diet-induced hyperlipidemia
Lysophospholipids produced by Pla2g1b hydrolysis suppress hepatic fat utilization and down-regulate energy expenditure, preventing metabolically beneficial adaptation to a high-fat diet exposure in promoting diet-induced obesity and type 2 diabetes.
sPLA2IB has a role in promoting MMP-2 mediated cell migration via the phosphatidylinositol 3-kinase and Akt pathway
Elevating plasma lysophospholipid levels in Pla2g1b deficient mice via intraperitoneal injection resulted in glucose intolerance.
pro-inflammatory effects of Ps. aeruginosa involve release of an sPLA2 of epithelial origin that, in part, via distinct signalling molecules, transactivates the ABCA1 gene, leading to export of phospholipid.
The results indicate that PLA2 activity in equine endometrium changes with the stage of the oestrous cycle and thus may be influenced by systemic hormone concentrations.
During pregnancy, PLA2 expression may be sufficient to initiate the cascade for prostaglandin f2alpha secretion and does not play a direct role in maternal recognition of pregnancy.
Phospholipase A2 (EC 22.214.171.124) catalyzes the release of fatty acids from glycero-3-phosphocholines. The best known varieties are the digestive enzymes secreted as zymogens by the pancreas of mammals. Sequences of pancreatic PLA2 enzymes from a variety of mammals have been reported. One striking feature of these enzymes is their close homology to venom phospholipases of snakes. Other forms of PLA2 have been isolated from brain, liver, lung, spleen, intestine, macrophages, leukocytes, erythrocytes, inflammatory exudates, chondrocytes, and platelets (Seilhamer et al., 1986
, phospholipase A2
, allergen Api m 1
, allergen Api m I
, phosphatidylcholine 2-acylhydrolase
, phosphatidylcholine 2-acylhydrolase 1B
, group IB phospholipase A2
, group IB secretory phospholipase A(2)
, phospholipase A2, major isoenzyme
, Group IB phospholipase A2
, Phosphatidylcholine 2-acylhydrolase 1B
, phospholipase A2, group IB, pancreas
, phospholipase A2 group IB
, phospholipase A2, group 1B
, cytosolic phospholipase A2
, phospholipase A2 group IVA
, phospholipase A2, group IB (pancreas)