phospholipase/inflammation

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Cytotoxic and inflammatory potential of a phospholipase A2 from Bothrops jararaca snake venom.

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Background

Snake venom phospholipases A₂ (PLA₂s) have been reported to induce myotoxic, neurotoxic, hemolytic, edematogenic, cytotoxic and proinflammatory effects. This work aimed at the isolation and functional characterization of a PLA₂ isolated

Inhibition of the activity of pro-inflammatory secretory phospholipase A(2) by acute phase proteins.

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Pro-Inflammatory non-pancreatic phospholipase A(2) (sPLA(2)) is markedly over-expressed in acute systemic and chronic local inflammatory processes. Since in acute phase reaction sPLA(2) is often over-expressed simultaneously with acute phase proteins (APP), it is important to determine whether APP

Morelloflavone, a novel biflavonoid inhibitor of human secretory phospholipase A2 with anti-inflammatory activity.

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The flavanonylflavone morelloflavone inhibited secretory phospholipase A2 (PLA2) in vitro, with a high potency on the human recombinant synovial and bee venom enzymes (IC50 = 0.9 and 0.6 microM, respectively). The inhibition was apparently irreversible. In contrast, the compound was inactive on

Identification and isolation of a phospholipase A2 activating protein in human rheumatoid arthritis synovial fluid: induction of eicosanoid synthesis and an inflammatory response in joints injected in vivo.

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Eicosanoids are important mediators of the destructive arthropathy observed in rheumatoid arthritis. The rate-limiting step in the eicosanoid synthesis pathway is the availability of free arachidonic acid. The phospholipase enzymes release arachidonic acid from membrane phospholipids and thus play

Studies of synthetic chalcone derivatives as potential inhibitors of secretory phospholipase A2, cyclooxygenases, lipoxygenase and pro-inflammatory cytokines.

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Arachidonic acid metabolism leads to the generation of key lipid mediators which play a fundamental role during inflammation. The inhibition of enzymes involved in arachidonic acid metabolism has been considered as a synergistic anti-inflammatory effect with enhanced spectrum of activity. A series

Phospholipase A in acute lung injury after trauma and sepsis: its relation to the inflammatory mediators PMN-elastase, C3a, and neopterin.

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Inflammatory mediators involved in the pathogenesis of the adult respiratory distress syndrome (ARDS) are products of the humeral cascade systems like the complement cascade and substances released from neutrophil granulocytes and macrophages like proteases, O2-radicals and arachidonate products.

Role of lipoprotein-associated phospholipase A2 in leukocyte activation and inflammatory responses.

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BACKGROUND Lipoprotein-associated phospholipase A2 (Lp-PLA2) is an emerging cardiovascular risk marker. To explore the biologic role of Lp-PLA2 in atherosclerosis, we examined its expression and contribution to leukocyte activation under proatherogenic conditions. RESULTS Following the induction of

Translational studies of lipoprotein-associated phospholipase A₂ in inflammation and atherosclerosis.

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OBJECTIVE This study sought to examine the role of lipoprotein-associated phospholipase A₂ (Lp-PLA₂/PLA2G7) in human inflammation and coronary atherosclerosis. BACKGROUND Lp-PLA₂ has emerged as a potential therapeutic target in coronary heart disease. Data supporting Lp-PLA₂ are indirect and

Lipoprotein-associated phospholipase A(2), inflammatory biomarkers, and risk of cardiovascular disease in the Prospective Study of Pravastatin in the Elderly at Risk (PROSPER).

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OBJECTIVE Lipoprotein-associated phospholipase A(2) (Lp-PLA(2)) is an inflammatory biomarker that circulates mainly bound to LDL. We evaluated the association of Lp-PLA(2) with vascular events in the elderly where the importance of LDL is diminished as a risk factor for coronary

Novel acidic phospholipase A2 from Porthidium hyoprora causes inflammation with mast cell rich infiltrate.

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Phospholipases A2 (PLA2) are a group of enzymes that hydrolyze phospholipids at the sn-2 position, being present in all nature. In venomous animals, these proteins assume a special role, being able to exert diverse pharmacological effects. In this work, authors identified a new isoform of PLA2 in

Active compound from the leaves of Vitex negundo L. shows anti-inflammatory activity with evidence of inhibition for secretory Phospholipase A(2) through molecular docking.

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Novel compounds with significant medicinal properties have gained much interest in therapeutic approaches for treating various inflammatory disorders like arthritis, odema and snake bites and the post-envenom (impregnating with venom) consequences. Inflammation is caused by the increased

Proteinaceous inhibitors of phospholipase A2 purified from inflammatory sites in rats.

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We have purified two phospholipase A2 inhibitory proteins (37 and 33 kDa) from peritoneal fluid of dexamethasone-treated rats. The extracellular phospholipase A2 found in inflammatory sites differed from the exocrine phospholipase A2 in susceptibility to these endogenous inhibitors; both proteins

Antiflammins. Anti-inflammatory activity and effect on human phospholipase A2.

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Two anti-inflammatory peptides (antiflammins) corresponding to a high amino acid similarity region between lipocortin I and uteroglobin were tested for their ability to inhibit purified human synovial fluid phospholipase A2 (HSF-PLA2). No inhibitory activity was observed, even at such high

Effects of flavonoids on Naja naja and human recombinant synovial phospholipases A2 and inflammatory responses in mice.

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Six flavonoid derivatives were tested for their influence on Naja naja and human recombinant synovial phospholipase A2. They showed a selectivity for the last enzyme with IC50 = 14.3, 17.6, 12.2 and 28.2 microM for quercetagetin, kaempferol-3-O-galactoside, scutellarein and

Phospholipase A2-induced pleural inflammation in rats.

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Injection of Naja mocambique mocambique phospholipase A2 [PLA2] into the rat pleural cavity induced dose- and time-dependent fluid accumulation and cellular infiltration. The time course of the cell influx was initially neutrophilic [2-6 h] and later mononuclear [6-24 h]. During reverse passive

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