Enzymatic properties of rat group IIA and V phospholipases A2 compared

Janssen, Marcel J.W.; Vermeulen, Leendert; Helm, Hester A. van der; Aarsman, A.J.; Slotboom, Arend J.; Egmond, Maarten R.

doi:10.1016/s1388-1981(99)00122-5

Cited by 25 publications

(30 citation statements)

References 52 publications

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“…Rat recombinant group V PLA 2 has a strong affinity to phosphatidylcholine (PC) and displays activity on PC micelles and liposomes. These properties make group V PLA 2 suitable for action on biological membranes (11). The same kinds of results have been published for human group V PLA 2 (10).…”

Section: Discussionsupporting

confidence: 58%

“…The activities of rat recombinant group IIA and group V PLA 2 s have not been tested on these two phospholipids. However, they have been tested on phosphatidylglycol (PGlo), which has the same charge, size, and interfacial properties as PG (11). The maximal velocity of group IIA PLA 2 on PGlo is almost 20-fold higher than that of group V PLA 2 .…”

Section: Discussionmentioning

confidence: 99%

“…Rat group IIA and V PLA 2 s were produced by recombinant expression in E. coli and were folded in vitro as described previously (11). The isoelectric points of the group IIA and group V PLA 2 s were 9.1 and 8.3, respectively.…”

Section: Production Of Rat Group Iia and Group V Pla 2 Smentioning

confidence: 99%

“…The purpose of the present study was to evaluate the possible role of group V PLA 2 in killing various antibiotic-resistant and sensitive bacterial strains. For this purpose we used recombinant rat group IIA and V PLA 2 s that were folded in vitro to obtain full enzymatic activity (11) and measured their bactericidal properties in vitro. Our results show that rat group IIA PLA 2 is highly bactericidal against Staphylococcus aureus, methicillin-resistant S. aureus, and Listeria monocytogenes, moderately bactericidal against Enterococcus faecalis and Enterococcus faecium and shows a weak bactericidal activity against E. coli.…”

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confidence: 99%

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Bactericidal Properties of Group IIA and Group V Phospholipases A2

Grönroos

Laine

Janssen

et al. 2001

The Journal of Immunology

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Group V phospholipase A2 (PLA2) is a recently characterized 14-kDa secretory PLA2 of mammalian heart and macrophage-derived cells. Group IIA PLA2, which is structurally close to group V PLA2, has been shown to kill Gram-positive bacteria in vitro and to prevent symptoms of Gram-positive infection in vivo. We studied the antibacterial properties of fully active recombinant rat group IIA and V PLA2s. Both group IIA and V PLA2s were highly bactericidal against Gram-positive bacteria, including methicillin-resistant staphylococci and vancomycin-resistant enterococci. Only high concentrations of group IIA PLA2 showed some bactericidal effect against the Gram-negative bacterium Escherichia coli. Our results confirm that group IIA PLA2 is a potent antibacterial enzyme against Gram-positive bacteria. Moreover, we show here that group V PLA2 is a novel antibacterial mammalian protein, but is less potent than group IIA PLA2. Both enzymes may be considered as future therapeutic agents against bacterial infections.

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Section: Discussionsupporting

confidence: 58%

Section: Discussionmentioning

confidence: 99%

Section: Production Of Rat Group Iia and Group V Pla 2 Smentioning

confidence: 99%

mentioning

confidence: 99%

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Bactericidal Properties of Group IIA and Group V Phospholipases A2

Grönroos

Laine

Janssen

et al. 2001

The Journal of Immunology

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“…P hospholipase A 2 (PLA 2 ) 3 enzymes are a heterogeneous family that is generally subdivided into three subclasses: Ca 2ϩ -dependent secretory PLA 2 (1-4), Ca 2ϩ -dependent cytosolic group IVA PLA 2 (gIVA-PLA 2 ) (5-8), and Ca 2ϩ -independent PLA 2 (9,10). The 85-kDa gIVA-PLA 2 has been associated with 1) secretion of eicosanoid metabolites in inflammatory cells (11)(12)(13), 2) cell migration (14 -16), and 3) airway hyperresponsiveness in allergen-sensitized mice and guinea pigs (8,17,18).…”

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confidence: 99%

Transcellular Secretion of Group V Phospholipase A2 from Epithelium Induces β2-Integrin-Mediated Adhesion and Synthesis of Leukotriene C4 in Eosinophils

Muñoz

Meliton

Lambertino

et al. 2006

The Journal of Immunology

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We examined the mechanism by which secretory group V phospholipase A2 (gVPLA2) secreted from stimulated epithelial cells activates eosinophil adhesion to ICAM-1 surrogate protein and secretion of leukotriene (LT)C4. Exogenous human group V PLA2 (hVPLA2) caused an increase in surface CD11b expression and focal clustering of this integrin, which corresponded to increased β2 integrin-mediated adhesion. Human IIaPLA2, a close homolog of hVPLA2, or W31A, an inactive mutant of hVPLA2, did not affect these responses. Exogenous lysophosphatidylcholine but not arachidonic acid mimicked the β2 integrin-mediated adhesion caused by hVPLA2 activation. Inhibition of hVPLA2 with MCL-3G1, a mAb against gVPLA2, or with LY311727, a global secretory phospholipase A2 (PLA2) inhibitor, attenuated the activity of hVPLA2; trifluoromethylketone, an inhibitor of cytosolic group IVA PLA2 (gIVA-PLA2), had no inhibitory effect on hVPLA2-mediated adhesion. Activation of β2 integrin-dependent adhesion by hVPLA2 did not cause ERK1/2 activation and was independent of gIVA-PLA2 phosphorylation. In other studies, eosinophils cocultured with epithelial cells were stimulated with FMLP/cytochalasin B (FMLP/B) and/or endothelin-1 (ET-1) before LTC4 assay. FMLP/B alone caused release of LTC4 from eosinophils, which was augmented by coculture with epithelial cells activated with ET-1. Addition of MCL-3G1 to cocultured cells caused ∼50% inhibition of LTC4 secretion elicited by ET-1, which was blocked further by trifluoromethylketone. Our data indicate that hVPLA2 causes focal clustering of CD11b and β2 integrin adhesion by a novel mechanism that is independent of arachidonic acid synthesis and gIVA-PLA2 activation. We also demonstrate that gVPLA2, endogenously secreted from activated epithelial cells, promotes secretion of LTC4 in cocultured eosinophils.

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A Novel Nonhemorragic Protease from the African Puff Adder (Bitis Arietans) Venom

Nok

2001

J Biochem & Molecular Tox

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A nonhemorrhagic proteinase B-20 from the venom of Bitis arietans has been purified to apparent electrophoretic homogeneity by chromatography on Sephadex G-100, Q-Sepharose, and CM-cellulose. It has a molecular weight of 20 k Da as determined by size exclusion chromatography on Sephadex G-100 and migrated as a single 20-k Da band on SDS polyacrylamide. It has an optimum pH of 6-8 and is inactive at pH 4.0. EDTA and 1,10-phenanthroline strongly inhibited the enzyme suggesting it is a metalloenzyme. Also it is inhibited by antipain but is unaffected by trasylol, antitrypsin, and pepsptatin. Colombin, an identified active component of Aristolochia albida used in the treatment of snake poisoning, did not inhibit the protease activity. It lost over 90% of its activity in the presence of 0.5 microM Hg(2+) but the inhibition was completely blocked in the presence of 10 microM mercaptoethanol implicating sulfhydryl groups in the catalytic entity of the protein. The activity was also inhibited competitively by glutathione and cysteine with inhibition binding constants K(i) of 240 and 40 microM, respectively. The enzyme is unaffected by several divalent cations but activated by 1 mM Fe(3+). It had a prolyl endopeptidase and thermolysin-like activity. The enzyme displayed a fast acting alpha-fibrinolytic and delayed gamma-fibrinolytic activity when tested on human fibrinogen. The relevance of these findings is discussed.

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Enzymatic properties of rat group IIA and V phospholipases A2 compared

Cited by 25 publications

References 52 publications

Bactericidal Properties of Group IIA and Group V Phospholipases A2

Bactericidal Properties of Group IIA and Group V Phospholipases A2

Transcellular Secretion of Group V Phospholipase A2 from Epithelium Induces β2-Integrin-Mediated Adhesion and Synthesis of Leukotriene C4 in Eosinophils

A Novel Nonhemorragic Protease from the African Puff Adder (Bitis Arietans) Venom

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