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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

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
Intranasal curcumin ameliorates airway inflammation and obstruction by regulating MAPKinase activation (p38, Erk and JNK) and prostaglandin D2 release in murine model of asthma.
New
Singh et al., Benares, India. In Int Immunopharmacol, Feb 2016
These investigations suggest that intranasal curcumin (2.5 and 5.0mg/kg) regulates airway inflammation and airway obstruction mainly by modulating cytokine levels (IL-4, 5, IFN-ƴ and TNF-α) and sPLA2 activity thereby inhibiting PGD2 release and COX-2 expression.
The role of inflammatory biomarkers in developing targeted cardiovascular therapies: lessons from the cardiovascular inflammation reduction trials.
Review
New
Ferro et al., London, United Kingdom. In Cardiovasc Res, Feb 2016
Specifically, the apparent ability of phospholipase A2 (PLA2) inhibitors and of antioxidants to ameliorate inflammation and to reduce coronary disease in Phase II trials did not translate into improved secondary cardiovascular prevention in larger population-based studies.
Lipoprotein-associated phospholipase A2 is related to risk of subclinical atherosclerosis but is not supported by Mendelian randomization analysis in a general Japanese population.
New
ACCESS and SESSA Research Groups et al., Ōtsu, Japan. In Atherosclerosis, Jan 2016
OBJECTIVE: Lipoprotein-associated phospholipase A2 (Lp-PLA2) is an enzyme predominantly bound to low-density lipoprotein (LDL).
Membrane and inhibitor interactions of intracellular phospholipases A2.
Review
New
Dennis et al., San Diego, United States. In Adv Biol Regul, Jan 2016
UNASSIGNED: Studying phospholipases A2 (PLA2s) is a challenging task since they act on membrane-like aggregated substrates and not on monomeric phospholipids.
Replacing carbohydrate with protein and fat in prediabetes or type-2 diabetes: greater effect on metabolites in PBMC than plasma.
New
Lee et al., Seoul, South Korea. In Nutr Metab (lond), Dec 2015
This study examined whether reductions in PBMCs and plasma lipoprotein-associated phospholipase A2 (Lp-PLA2) activities induced by dietary intervention affected the overall metabolic profiles of PBMC and plasma.
Deciphering the Causal Role of sPLA2s and Lp-PLA2 in Coronary Heart Disease.
Review
New
Holmes et al., Oxford, United Kingdom. In Arterioscler Thromb Vasc Biol, Nov 2015
Over the last 10 to 15 years, animal and human observational studies have identified elevated levels of both proinflammatory secretory phospholipase A2-IIA and lipoprotein-associated phospholipase A2 as potential risk factors for coronary heart disease.
Comparison of Serum LP-PLA2 Level and some Nutritional Factors between Well-Controlled and Poorly-Controlled Diabetic Patients.
New
Jalali et al., Tehrān, Iran. In Acta Med Iran, Nov 2015
Lipoprotein-associated phospholipase A2 (Lp-PLA2) is produced by inflammatory cells, bound to LDL and other lipoproteins, and hydrolyzes oxidized phospholipids in LDL.
Lipoprotein-associated phospholipase A2 prognostic role in atherosclerotic complications.
Review
New
Rossi et al., Padova, Italy. In World J Cardiol, Nov 2015
Promising results along this line were provided by studies investigating the lipoprotein-associated phospholipase A2 (Lp-PLA2), a member of phospholipase A2 proteins family that plays a key role in the metabolism of pro-inflammatory phospholipids, as oxidized low-density lipoproteins, and in the generation of pro-atherogenic metabolites, including lysophosphatidylcholine and oxidized free fatty acids.
[Lp-PLA2, a biomarker of vascular inflammation and vulnerability of atherosclerosis plaques].
Review
New
Bonnefont-Rousselot, Paris, France. In Ann Pharm Fr, Nov 2015
Among the emerging biomarkers of atherogenesis, the lipoprotein-associated phospholipase A2 (Lp-PLA2), formerly known as PAF-acetylhydrolase (McIntyre et al., 2009), hydrolyses the oxidized short chain phospholipids of low-density lipoproteins (LDL), thereby releasing pro-inflammatory mediators (lysophospholipids and oxidized fatty acids).
SYNTHESIS AND BIOLOGICAL EFFICACY OF NOVEL PIPERAZINE ANALOGUES BEARING QUINOLINE AND PYRIDINE MOIETIES.
New
Khanum et al., In Bioorg Khim, Sep 2015
The analogues were evaluated for in vitro antioxidant activity against 2,2-diphenyl-1-picryl-hydrazyl (DPPH) and ferrous ion radical scavenging activities and anti-inflammatory activity by inhibition of Vipera russelli venom (PLA2) and gastric K+/H(+)-ATPase activities.
Effect of darapladib on major coronary events after an acute coronary syndrome: the SOLID-TIMI 52 randomized clinical trial.
Impact
Steen et al., Auckland, New Zealand. In Jama, 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.
Impact
VISTA-16 Investigators et al., Adelaide, Australia. In Jama, 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.
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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