Human Neutrophils Store Type II 14-kDa Phospholipase A2 in Granules and Secrete Active Enzyme in Response to Soluble Stimuli

Rosenthal, Miriam D.; Gordon, Maureen; Buescher, E. Stephen; Slusser, James H.; Harris, Lesley K.; Franson, Richard C.

doi:10.1006/bbrc.1995.1388

Cited by 84 publications

(36 citation statements)

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“…The sPLA2-IIA staining was also detected in infiltrating neutrophils. Similar observation has been previously reported, but this remained controversial 40,41 . sPLA2-IIA is stored in granules of neutrophils but this may also reflect the phagocytosis of extracellular sPLA2-IIA associated with bacteria.…”

Section: Discussionsupporting

confidence: 72%

Pseudomonas aeruginosa eradicates Staphylococcus aureus by manipulating the host immunity

et al. 2014

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Young cystic fibrosis (CF) patients' airways are mainly colonized by Staphylococcus aureus, while Pseudomonas aeruginosa predominates in adults. However, the mechanisms behind this infection switch are unclear. Here, we show that levels of type-IIA-secreted phospholipase A2 (sPLA2-IIA, a host enzyme with bactericidal activity) increase in expectorations of CF patients in an age-dependent manner. These levels are sufficient to kill S. aureus, with marginal effects on P. aeruginosa strains. P. aeruginosa laboratory strains and isolates from CF patients induce sPLA2-IIA expression in bronchial epithelial cells from CF patients (these cells are a major source of the enzyme). In an animal model of lung infection, P. aeruginosa induces sPLA2-IIA production that favours S. aureus killing. We suggest that sPLA2-IIA induction by P. aeruginosa contributes to S. aureus eradication in CF airways. Our results indicate that a bacterium can eradicate another bacterium by manipulating the host immunity.

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Section: Discussionsupporting

confidence: 72%

Pseudomonas aeruginosa eradicates Staphylococcus aureus by manipulating the host immunity

et al. 2014

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“…Thus in macrophages, most of the arachidonate released into the medium is derived from a secreted type II PLA 2 (sPLA 2 ) acting on the outer surface of the cell, while a group IV PLA 2 (cPLA 2 ) acting intracellularly is coupled to eicosanoid biosynthesis and is only responsible for a portion of the arachidonate released into the medium. In PMN, the situation may be similar, although direct evidence for secretion of sPLA 2 activity has been elusive (40). Alternatively, activated neutrophils may also generate arachidonate by the concerted action of phospholipase C or D (41) and a lipase located at the inner leaflet of the plasma membrane.…”

Section: Discussionmentioning

confidence: 99%

Protein-facilitated Export of Arachidonic Acid from Pig Neutrophils

Krischer¹,

Eisenmann²,

Böck³

et al. 1997

Journal of Biological Chemistry

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Activated neutrophils release a variety of eicosanoids into the extracellular medium including arachidonic acid, 5-hydroxyicosatetraenoic acid, and leukotriene A 4 and B 4 . In this study, the mechanism of arachidonic acid export has been examined using inside-out plasma membrane vesicles from pig polymorphonuclear leukocytes. Tritiated arachidonic acid associated rapidly with the membrane vesicles and crossed the membrane into the intravesicular space in a time-dependent and saturable manner. Half the maximal influx rate was measured at an arachidonate concentration of 5.7 M, and a maximal influx velocity of 3.0 nmol/mg ؋ min was determined at pH 6.8. Influx into vesicles was sensitive to a number of common anion transport inhibitors including pentachlorophenol, phloretin, diiodosalicylic acid, and quercetin as well as to the proteases trypsin and Pronase, suggesting a protein-dependent process. Furthermore, influx was temperature-sensitive with an energy of activation of 11.6 kcal/mol. Varying extravesicular concentration of ATP, Na ؉ , or K ؉ had no impact on arachidonate influx, whereas changes in pH had a profound effect; optimum transport activity was observed at an extravesicular pH of 6, whereas raising the pH to 9.5 essentially abolished uptake. These results indicate and initially characterize a novel protein-facilitated arachidonate export mechanism in pig neutrophils.

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“…Neutrophils Release GV sPLA 2 following Exposure to fMLP or OZ-sPLA 2 enzymes may be released by cells into their extracellular environment (37). Thus, when neutrophils were exposed to the bacterial tripeptide fMLP, sPLA 2 activity (as measured with radiolabeled bacterial membranes) in the extracellular fluid increased by 3-4-fold (Fig.…”

Section: Fig 4 Neutrophils Contain Gv and Gx Splamentioning

confidence: 95%

“…PLA 2 enzymatic activity has been detected in intracellular granules in human neutrophils (37)(38)(39). Subcellular fractionation experiments have shown that neutrophils have a heterogenous population of granules that have distinct intra-granular and membrane-bound proteins (40).…”

mentioning

confidence: 99%

Groups IV, V, and X Phospholipases A2s in Human Neutrophils

Dégousée¹,

Ghomashchi²,

Stefanski³

et al. 2002

Journal of Biological Chemistry

165

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The bacterial tripeptide formyl-Met-Leu-Phe (fMLP) induces the secretion of enzyme(s) with phospholipase A 2 (PLA 2 ) activity from human neutrophils. We show that circulating human neutrophils express groups V and X sPLA 2 (GV and GX sPLA 2 ) mRNA and contain GV and GX sPLA 2 proteins, whereas GIB, GIIA, GIID, GIIE, GIIF, GIII, and GXII sPLA 2 s are undetectable. GV sPLA 2 is a component of both azurophilic and specific granules, whereas GX sPLA 2 is confined to azurophilic granules. Exposure to fMLP or opsonized zymosan results in the release of GV but not GX sPLA 2 and most, if not all, of the PLA 2 activity in the extracellular fluid of fMLPstimulated neutrophils is due to GV sPLA 2 . GV sPLA 2 does not contribute to fMLP-stimulated leukotriene B 4 production but may support the anti-bacterial properties of the neutrophil, because 10 -100 ng per ml concentrations of this enzyme lead to Gram-negative bacterial membrane phospholipid hydrolysis in the presence of human serum. By use of a recently described and specific inhibitor of cytosolic PLA 2 -␣ (group IV PLA 2 ␣), we show that this enzyme produces virtually all of the arachidonic acid used for the biosynthesis of leukotriene B 4 in fMLP-and opsonized zymosan-stimulated neutrophils, the major eicosanoid produced by these pro-inflammatory cells.

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Human Neutrophils Store Type II 14-kDa Phospholipase A2 in Granules and Secrete Active Enzyme in Response to Soluble Stimuli

Cited by 84 publications

References 0 publications

Pseudomonas aeruginosa eradicates Staphylococcus aureus by manipulating the host immunity

Pseudomonas aeruginosa eradicates Staphylococcus aureus by manipulating the host immunity

Protein-facilitated Export of Arachidonic Acid from Pig Neutrophils

Groups IV, V, and X Phospholipases A2s in Human Neutrophils

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