Mechanisms of formation and function of eosinophil lipid bodies: inducible intracellular sites involved in arachidonic acid metabolism

Bozza, Patrı́cia T.; Yu, Wengui; Weller, Peter F.

doi:10.1590/s0074-02761997000800018

Cited by 19 publications

(20 citation statements)

References 49 publications

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“…These organelles compartmentalize different groups of proteins involved in lipid metabolism and in cell signaling, in addition to containing the complex enzyme COX and 5-LO, and even AA, cPLA 2 , MAPK, and PI3K [49, 50]. Thus, the actions of BaTX-I, BaTX-II, and BaPLA 2 on lipid body formation in J774A.1 macrophages were evaluated.…”

Section: Discussionmentioning

confidence: 99%

“…The data suggest that the activation of complement receptors during phagocytosis stimulates lipid body formation in macrophages, also induced by the action of sPLA 2 s. Thus, PLA 2 s, in addition to releasing the AA of membrane phospholipids, can hydrolyze phosphatidylcholine and cause lyso-PAF release, which is the precursor of platelet activating factor (PAF). Data from the literature indicate that this inflammatory mediator, with platelet aggregating activity, is involved in signaling pathways that favor the formation of lipid bodies and the release of mediators such as LTC 4 and PGE 2 [50]. Additional studies to determine the role of lipid bodies in the process of phagocytosis and the mechanisms of formation of these organelles are required.…”

Section: Discussionmentioning

confidence: 99%

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Activation of J77A.1 Macrophages by Three Phospholipases A₂Isolated fromBothrops atroxSnake Venom

Furtado

Oliveira

Pontes

et al. 2014

BioMed Research International

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In the present study, we investigated the in vitro effects of two basic myotoxic phospholipases A2 (PLA2), BaTX-I, a catalytically inactive Lys-49 variant, and BaTX-II, a catalytically active Asp-49, and of one acidic myotoxic PLA2, BaPLA2, a catalytically active Asp-49, isolated from Bothrops atrox snake venom, on the activation of J774A.1 macrophages. At noncytotoxic concentrations, the toxins did not affect the adhesion of the macrophages, nor their ability to detach. The data obtained showed that only BaTX-I stimulated complement receptor-mediated phagocytosis. However, BaTX-I, BaTX-II, and BaPLA2 induced the release of the superoxide anion by J774A.1 macrophages. Additionally, only BaTX-I raised the lysosomal volume of macrophages after 15 min of incubation. After 30 min, all the phospholipases increased this parameter, which was not observed within 60 min. Moreover, BaTX-I, BaTX-II, and BaPLA2 increased the number of lipid bodies on macrophages submitted to phagocytosis and not submitted to phagocytosis. However, BaTX-II and BaPLA2 induced the release of TNF-α by J774A.1 macrophages. Taken together, the data show that, despite differences in enzymatic activity, the three toxins induced inflammatory events and whether the enzyme is acidic or basic does not seem to contribute to these effects.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Activation of J77A.1 Macrophages by Three Phospholipases A₂Isolated fromBothrops atroxSnake Venom

Furtado

Oliveira

Pontes

et al. 2014

BioMed Research International

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show abstract

“…While still moist, the leukocytes on the CytoSpin slides were fixed in 3.7% formaldehyde in Ca 2+ - and Mg 2+ -free Hank’s buffered salt solution (HBSS; pH 7.4) and stained with 1.5% OsO4 [40]. The lipid bodies in 50 consecutively scanned leukocytes were enumerated by microscopy.…”

Section: Methodsmentioning

confidence: 99%

Murine lung injury caused by Leptospira interrogans glycolipoprotein, a specific Na/K-ATPase inhibitor

Gonçalves-de-Albuquerque

Burth

Silva

et al. 2014

Respir Res

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BackgroundLeptospiral glycolipoprotein (GLP) is a potent and specific Na/K-ATPase inhibitor. Severe pulmonary form of leptospirosis is characterized by edema, inflammation and intra-alveolar hemorrhage having a dismal prognosis. Resolution of edema and inflammation determines the outcome of lung injury. Na/K-ATPase activity is responsible for edema clearance. This enzyme works as a cell receptor that triggers activation of mitogen-activated protein kinase (MAPK) intracellular signaling pathway. Therefore, injection of GLP into lungs induces injury by triggering inflammation.MethodsWe injected GLP and ouabain, into mice lungs and compared their effects. Bronchoalveolar lavage fluid (BALF) was collected for cell and lipid body counting and measurement of protein and lipid mediators (PGE2 and LTB4). The levels of the IL-6, TNFα, IL-1B and MIP-1α were also quantified. Lung images illustrate the injury and whole-body plethysmography was performed to assay lung function. We used Toll-like receptor 4 (TLR4) knockout mice to evaluate leptospiral GLP-induced lung injury. Na/K-ATPase activity was determined in lung cells by nonradioactive rubidium incorporation. We analyzed MAPK p38 activation in lung and in epithelial and endothelial cells.ResultsLeptospiral GLP and ouabain induced lung edema, cell migration and activation, production of lipid mediators and cytokines and hemorrhage. They induced lung function alterations and inhibited rubidium incorporation. Using TLR4 knockout mice, we showed that the GLP action was not dependent on TLR4 activation. GLP activated of p38 and enhanced cytokine production in cell cultures which was reversed by a selective p38 inhibitor.ConclusionsGLP and ouabain induced lung injury, as evidenced by increased lung inflammation and hemorrhage. To our knowledge, this is the first report showing GLP induces lung injury. GLP and ouabain are Na/K-ATPase targets, triggering intracellular signaling pathways. We showed p38 activation by GLP-induced lung injury, which was may be linked to Na/K-ATPase inhibition. Lung inflammation induced by GLP was not dependent on TLR4 activation.

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“…Lipid bodies are arachidonic acid-rich cytoplasmic inclusions found in increased numbers in inflammatory cells (23,32). Fig.…”

Section: Oxldl and Oxldl Phospholipids Induce Lipid Body Formation Inmentioning

confidence: 99%

Synergism Between Platelet-Activating Factor-Like Phospholipids and Peroxisome Proliferator-Activated Receptor γ Agonists Generated During Low Density Lipoprotein Oxidation That Induces Lipid Body Formation in Leukocytes

Assis

Silva

Caiado

et al. 2003

The Journal of Immunology

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Oxidized low density lipoprotein (LDL) has an important proinflammatory role in atherogenesis. In this study, we investigated the ability of oxidized LDL (oxLDL) and its phospholipid components to induce lipid body formation in leukocytes. Incubation of mouse peritoneal macrophages with oxidized, but not with native LDL led to lipid body formation within 1 h. This was blocked by platelet-activating factor (PAF) receptor antagonists or by preincubation of oxLDL with rPAF acetylhydrolase. HPLC fractions of phospholipids purified from oxLDL induced calcium flux in neutrophils as well as lipid body formation in macrophages. Injection of the bioactive phospholipid fractions or butanoyl and butenoyl PAF, a phospholipid previously shown to be present in oxLDL, into the pleural cavity of mice induced lipid body formation in leukocytes recovered after 3 h. The 5-lipoxygenase and cyclooxygenase-2 colocalized within lipid bodies formed after stimulation with oxLDL, bioactive phospholipid fractions, or butanoyl and butenoyl PAF. Lipid body formation was inhibited by 5-lipoxygenase antagonists, but not by cyclooxygenase-2 inhibitors. Azelaoyl-phosphatidylcholine, a peroxisome proliferator-activated receptor-γ agonist in oxLDL phospholipid fractions, induced formation of lipid bodies at late time points (6 h) and synergized with suboptimal concentrations of oxLDL. We conclude that lipid body formation is an important proinflammatory effect of oxLDL and that PAF-like phospholipids and peroxisome proliferator-activated receptor-γ agonists generated during LDL oxidation are important mediators in this phenomenon.

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Mechanisms of formation and function of eosinophil lipid bodies: inducible intracellular sites involved in arachidonic acid metabolism

Cited by 19 publications

References 49 publications

Activation of J77A.1 Macrophages by Three Phospholipases A₂Isolated fromBothrops atroxSnake Venom

Activation of J77A.1 Macrophages by Three Phospholipases A₂Isolated fromBothrops atroxSnake Venom

Murine lung injury caused by Leptospira interrogans glycolipoprotein, a specific Na/K-ATPase inhibitor

Synergism Between Platelet-Activating Factor-Like Phospholipids and Peroxisome Proliferator-Activated Receptor γ Agonists Generated During Low Density Lipoprotein Oxidation That Induces Lipid Body Formation in Leukocytes

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Mechanisms of formation and function of eosinophil lipid bodies: inducible intracellular sites involved in arachidonic acid metabolism

Cited by 19 publications

References 49 publications

Activation of J77A.1 Macrophages by Three Phospholipases A2Isolated fromBothrops atroxSnake Venom

Activation of J77A.1 Macrophages by Three Phospholipases A2Isolated fromBothrops atroxSnake Venom

Murine lung injury caused by Leptospira interrogans glycolipoprotein, a specific Na/K-ATPase inhibitor

Synergism Between Platelet-Activating Factor-Like Phospholipids and Peroxisome Proliferator-Activated Receptor γ Agonists Generated During Low Density Lipoprotein Oxidation That Induces Lipid Body Formation in Leukocytes

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Activation of J77A.1 Macrophages by Three Phospholipases A₂Isolated fromBothrops atroxSnake Venom

Activation of J77A.1 Macrophages by Three Phospholipases A₂Isolated fromBothrops atroxSnake Venom