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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 02 Oct 2014.

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, IIa, fibrillin-1
Papers on PLA2
Short-term cigarette smoke exposure leads to metabolic alterations in lung alveolar cells.
New
Cadenas et al., Los Angeles, United States. In Am J Respir Cell Mol Biol, Aug 2014
The increase in palmitate use for energy production likely affects the surfactant biosynthesis pathway, as evidenced by the decrease in phosphatidylcholine levels and the increase in phospholipase A2 activity after CS exposure.
PLA2R1: expression and function in cancer.
Review
New
Vindrieux et al., Lyon, France. In Biochim Biophys Acta, Aug 2014
The phospholipase A2 receptor 1 (PLA2R1 or PLA2R) was isolated twenty years ago for its ability to bind several secretory phospholipase A2 proteins (sPLA2).
In silico molecular interaction analysis of LTNF peptide-LT10 with snake venom enzymes.
New
Deobagkar et al., Pune, India. In Protein Pept Lett, Jul 2014
We applied molecular modeling, docking and molecular dynamic (MD) simulation techniques to compute the interaction of LT10 peptide with few snake venom enzymes, namely PLA2 from Naja naja and Atrolysin -C from Crotalus atrox.
Renaturation and one step purification of the chicken GIIA secreted phospholipase A2 from inclusion bodies.
New
Bezzine et al., Sfax, Tunisia. In Int J Biol Macromol, Jun 2014
Recombinant expression of chicken intestinal sPLA2-IIA (ChPLA2-IIA) in Escherichia coli shows that the enzyme is Ca(2+) dependent, maximally active at pH 8-9, and hydrolyses phosphatidylglycerol versus phosphatidylcholine with a 10-fold preference.
Bariatric surgery in morbidly obese patients improves the atherogenic qualitative properties of the plasma lipoproteins.
New
Peinado-Onsurbe et al., Barcelona, Spain. In Atherosclerosis, May 2014
Plasma and lipoproteins were assayed for chemical composition and lipoprotein-associated phospholipase A2 (Lp-PLA2) activity.
New insights on membrane mediated effects of 1α,25-dihydroxy vitamin D3 signaling in the musculoskeletal system.
Review
New
Schwartz et al., Atlanta, United States. In Steroids, Mar 2014
Long term efforts to investigate the roles of these two receptors demonstrated thatPdia3 is located in caveolae, where it interacts with phospholipase A2 (PLA2) activating protein (PLAA) and caveolin-1 (Cav-1) to initiate rapid signaling via Ca(++)/calmodulin-dependent protein kinase II (CaMKII), PLA2, phospholipase C (PLC), protein kinase C (PKC), and ultimately the ERK1/2 family of mitogen activated protein kinases (MAPK).
sPLA2 and the epidermal barrier.
Review
New
Mauro et al., Seattle, United States. In Biochim Biophys Acta, Mar 2014
The secretory phospholipase 2 (sPLA2) enzymes control important processes in skin and other organs, including inflammation and differentiation.
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.
Bee venom phospholipase A2 induces a primary type 2 response that is dependent on the receptor ST2 and confers protective immunity.
New
Impact
Medzhitov et al., New Haven, United States. In Immunity, Dec 2013
Phospholipase A2 (PLA2) is a conserved component of venoms from multiple species and is the major allergen in bee venom.
Hemolytic activity and platelet aggregation inhibitory effect of vipoxin's basic sPLA2 subunit.
New
Petrova et al., Sofia, Bulgaria. In Interdiscip Toxicol, Sep 2013
In the present study we evaluated the effect of secreted phospholipase A2 (sPLA2) (the toxic subunit of the heterodimeric neurotoxin vipoxin, isolated from the Bulgarian long-nosed viper Vipera ammodytes meridionalis) on hemolysis, erythrocyte morphology and platelet aggregation.
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
Secreted Phospholipases A2 - not just Enzymes.
Review
Križaj et al., In Acta Chim Slov, 2011
However, since pharmacologically active sPLA2 molecules without enzymatic activity have been discovered, first in snake venom and then also in human, it has become increasingly evident that, on many occasions, the action of these proteins has to be considered as arising from the interplay of their receptor-binding and enzymatic functions.
Structural and Functional Characterization of Anticoagulant, FXa-binding Viperidae Snake Venom Phospholipases A2.
Review
Saul et al., In Acta Chim Slov, 2011
Certain snake venom phospholipases A2 (PLA2) have been identified as specific, non-competitive blood coagulation inhibitors that bind with high affinity to human activated blood coagulation factor X (hFXa).
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.
Equivalent effects of snake PLA2 neurotoxins and lysophospholipid-fatty acid mixtures.
Impact
Montecucco et al., Padova, Italy. In Science, 2006
Snake presynaptic phospholipase A2 neurotoxins (SPANs) paralyze the neuromuscular junction (NMJ).
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