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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 26 May 2015.

Phospholipase A2, group IB

PLA2, sPLA2
Phospholipase A2 (EC 3.1.1.4) 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 [PubMed 3028739]) .[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, fibrillin-1, V1a
Papers on PLA2
Diverse activity of human secretory phospholipases A2 on the migration of human vascular smooth muscle cells.
New
Kuksis et al., Toronto, Canada. In Inflamm Res, 22 Jun 2015
OBJECTIVE: Investigation of the diversity of human secretory phospholipases A2 (sPLA2) on the migration of human vascular smooth muscle cells (VSMC).
Phospholipase A2 inhibits cisplatin-induced acute kidney injury by modulating regulatory T cells by the CD206 mannose receptor.
New
Bae et al., Seoul, South Korea. In Kidney Int, 20 Jun 2015
UNASSIGNED: Previously, we found that Foxp3-expressing CD4(+) regulatory T (Treg) cells attenuate cisplatin-induced acute kidney injury in mice and that bee venom and its constituent phospholipase A2 (PLA2) are capable of modulating Treg cells.
Lipoprotein-associated phospholipase A2 and risk of incident cardiovascular disease in a multi-ethnic cohort: The multi ethnic study of atherosclerosis.
New
Cushman et al., Los Angeles, United States. In Atherosclerosis, 16 Jun 2015
OBJECTIVE: Prospective studies reporting a positive association of lipoprotein-associated phospholipase A2 (Lp-PLA2) mass and activity with incident cardiovascular disease (CVD) have included primarily white individuals.
AUXINS ACTION ON Glycine max SECRETORY PHOSPHOLIPASE A2 IS MEDIATED BY THE INTERFACIAL PROPERTIES IMPOSED BY THE PHYTOHORMONES.
New
Fidelio et al., Córdoba, Argentina. In Chem Phys Lipids, 15 Jun 2015
UNASSIGNED: Secretory phospholipase A2 (sPLA2) are soluble enzymes that catalyze the conversion of phospholipids to lysophospholipids and free fatty acids at membrane interfaces.
A Review of 1α,25(OH)2D3 Dependent Pdia3 Receptor Complex Components in Wnt5a Non-Canonical Pathway Signaling.
Review
New
Schwartz et al., Atlanta, United States. In J Steroid Biochem Mol Biol, 03 May 2015
1α,25(OH)2D3 binding to Pdia3 triggers the interaction between Pdia3 and phospholipase A2 (PLA2)-activating protein (PLAA), resulting in downstream activation of calcium/calmodulin-dependent protein kinase II (CaMKII), PLA2, and protein kinase C (PKC).
Reassessing lipid metabolism and its potentialities in the prediction of cardiovascular risk.
New
Ferreira et al., São Paulo, Brazil. In Arch Endocrinol Metab, 30 Apr 2015
Some of bloodstream biomarkers related to lipid metabolism are modified LDL particles, apolipoprotein AI (apo AI), apolipoprotein B, lipoprotein (a) [Lp (a)], cholesteryl ester transfer protein (CETP), subtypes of LDL and HDL particles, and lipoprotein-associated phospholipase A2 (Lp-PLA2).
Membrane-mediated actions of 1,25-dihydroxy vitamin D3: a review of the roles of phospholipase A2 activating protein and Ca(2+)/calmodulin-dependent protein kinase II.
Review
New
Boyan et al., Atlanta, United States. In J Steroid Biochem Mol Biol, Mar 2015
In its membrane-initiated pathway, after 1α,25(OH)2D3 interacts with protein disulfide isomerase, family A, member 3 (Pdia3) in caveolae, phospholipase A2 (PLA2) and protein kinase C (PKC) are activated.
Secreted phospholipase A2 and mast cells.
Review
New
Taketomi et al., Tokyo, Japan. In Allergol Int, Jan 2015
Among the PLA2 superfamily, secreted PLA2 (sPLA2) enzymes comprise the largest subfamily that includes 11 isoforms with a conserved His-Asp catalytic dyad.
HDL in infectious diseases and sepsis.
Review
New
Norata et al., Cinisello Balsamo, Italy. In Handb Exp Pharmacol, Dec 2014
More importantly, endotoxemia modulates HDL composition and size: phospholipids are reduced as well as apolipoprotein (apo) A-I, while serum amyloid A (SAA) and secretory phospholipase A2 (sPLA2) dramatically increase, and, although the total HDL particle number does not change, a significant decrease in the number of small- and medium-size particles is observed.
Effect of darapladib on major coronary events after an acute coronary syndrome: the SOLID-TIMI 52 randomized clinical trial.
New
Impact
Steen et al., Auckland, New Zealand. In Jama, Oct 2014
IMPORTANCE: Lipoprotein-associated phospholipase A2 (Lp-PLA2) has been hypothesized to be involved in atherogenesis through pathways related to inflammation.
Varespladib and cardiovascular events in patients with an acute coronary syndrome: the VISTA-16 randomized clinical trial.
New
Impact
VISTA-16 Investigators et al., Adelaide, Australia. In Jama, Feb 2014
IMPORTANCE: Secretory phospholipase A2 (sPLA2) generates bioactive phospholipid products implicated in atherosclerosis.
Phospholipase A2 - nexus of aging, oxidative stress, neuronal excitability, and functional decline of the aging nervous system? Insights from a snail model system of neuronal aging and age-associated memory impairment.
Review
Wildering et al., Calgary, Canada. In Front Genet, 2013
This review focuses on the idea that changes in intrinsic neuronal electrical excitability associated with (per)oxidation of membrane lipids and activation of phospholipase A2 (PLA2) enzymes are an important mechanism of learning and memory failure under normal aging conditions.
Bee venom phospholipase A2 induces a primary type 2 response that is dependent on the receptor ST2 and confers protective immunity.
Impact
Medzhitov et al., New Haven, United States. In Immunity, 2013
Phospholipase A2 (PLA2) is a conserved component of venoms from multiple species and is the major allergen in bee venom.
Genetic ablation of calcium-independent phospholipase A(2)γ (iPLA(2)γ) attenuates calcium-induced opening of the mitochondrial permeability transition pore and resultant cytochrome c release.
GeneRIF
Gross et al., Saint Louis, United States. In J Biol Chem, 2012
identify iPLA(2)gamma as an important mechanistic component of the mPTP, define its downstream products as potent regulators of mPTP opening
Overexpression of Orai1 and STIM1 proteins alters regulation of store-operated Ca2+ entry by endogenous mediators.
GeneRIF
Bolotina et al., Boston, United States. In J Biol Chem, 2012
These data confirm the role of iPLA(2)beta as an essential mediator of endogenous store operated calcium entry.
Severe disturbance in the Ca2+ signaling in astrocytes from mouse models of human infantile neuroaxonal dystrophy with mutated Pla2g6.
GeneRIF
Reiser et al., Magdeburg, Germany. In Hum Mol Genet, 2012
Data show that Pla2g6 mutant mice develop pathology analogous to that observed in infantile neuroaxonal dystrophy (INAD) patients.
Association between PLA2G6 gene polymorphisms and Parkinson's disease in the Chinese Han population.
GeneRIF
Tang et al., Changsha, China. In Parkinsonism Relat Disord, 2012
The results of this study suggested that PLA2G6 is not a susceptibility gene for parkinson disease in our population.
Secreted phospholipase A(2) group IIA is a neurotoxin released by stimulated human glial cells.
GeneRIF
Klegeris et al., Kelowna, Canada. In Mol Cell Neurosci, 2012
The data obtained indicate that sPLA(2)IIA may contribute to the pathogenesis of neurodegenerative diseases involving neuroinflammation
Clinical, angiographic, and genetic factors associated with early coronary stent thrombosis.
Impact
Collet et al., Paris, France. In Jama, 2011
and ITGB3 PLA2 carriage (adjusted OR, 0.52; 95% CI, 0.28-0.95).
Biochemistry and physiology of mammalian secreted phospholipases A2.
Review
Impact
Gelb et al., Antibes, France. In Annu Rev Biochem, 2007
The mammalian genome contains 10 enzymatically active secreted PLA2s (sPLA2s) and two sPLA2-related proteins devoid of lipolytic enzymatic activity.
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