Thematische Bibliographien / Phospholipase A2 (sPLA2) / Zeitschriftenartikel
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Zeitschriftenartikel zum Thema „Phospholipase A2 (sPLA2)“

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Veröffentlicht am 18. Mai 2024

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1

Themsche, Céline Van, Michèle Jacob, and Christian Salesse. "Human retinal pigment epithelium secretes a phospholipase A2 and contains two novel intracellular phospholipases A2." Biochemistry and Cell Biology 79, no. 1 (2001): 1–10. http://dx.doi.org/10.1139/o00-088.

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The sensitivity of different phospholipase A2 (PLA2)-active fractions eluted from cation-exchange chromatography to para-bromophenacylbromide (pBPB), Ca2+-EGTA, DTT, heat, and H2SO4 indicates that human cultured retinal pigment epithelial (hRPE) cells probably contain two different intracellular PLA2 enzymes. Control experiments using "back-and-forth" thin-layer chromatography confirmed that, in our assay conditions, the generation of free fatty acids originated solely from PLA2 activity. Together with immunoblot experiments where no cross-reactivity was observed between the hRPE cytosolic PLA
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Rizzo, Maria Teresa, Elisabeth Nguyen, Marlene Aldo-Benson, and Gerard Lambeau. "Secreted phospholipase A2 induces vascular endothelial cell migration." Blood 96, no. 12 (2000): 3809–15. http://dx.doi.org/10.1182/blood.v96.12.3809.

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Abstract Secreted phospholipase A2 (sPLA2) regulates a variety of cellular functions. The present investigation was undertaken to elucidate the potential role of sPLA2 in endothelial cell (EC) migration. Bovine aortic endothelial cells (BAECs) exposed to sPLA2 placed in the lower compartment of a modified Boyden chamber displayed increased migration compared to cells exposed to vehicle. The effect of sPLA2 on EC migration was time and dose dependent. Migration of BAECs was observed at 30 minutes, increased over 1 to 2 hours, and declined thereafter. At 2 hours of stimulation, sPLA2 (0.01-2 μmo
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Rizzo, Maria Teresa, Elisabeth Nguyen, Marlene Aldo-Benson, and Gerard Lambeau. "Secreted phospholipase A2 induces vascular endothelial cell migration." Blood 96, no. 12 (2000): 3809–15. http://dx.doi.org/10.1182/blood.v96.12.3809.h8003809_3809_3815.

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Secreted phospholipase A2 (sPLA2) regulates a variety of cellular functions. The present investigation was undertaken to elucidate the potential role of sPLA2 in endothelial cell (EC) migration. Bovine aortic endothelial cells (BAECs) exposed to sPLA2 placed in the lower compartment of a modified Boyden chamber displayed increased migration compared to cells exposed to vehicle. The effect of sPLA2 on EC migration was time and dose dependent. Migration of BAECs was observed at 30 minutes, increased over 1 to 2 hours, and declined thereafter. At 2 hours of stimulation, sPLA2 (0.01-2 μmol/L) indu
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Shridas, Preetha, and Nancy R. Webb. "Diverse Functions of Secretory Phospholipases A2." Advances in Vascular Medicine 2014 (July 15, 2014): 1–11. http://dx.doi.org/10.1155/2014/689815.

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Phospholipase A2 enzymes (PLA2s) catalyze the hydrolysis of glycerophospholipids at their sn-2 position releasing free fatty acids and lysophospholipids. Mammalian PLA2s are classified into several categories of which important groups include secreted PLA2s (sPLA2s) and cytosolic PLA2s (cPLA2s) that are calcium-dependent for their catalytic activity and calcium-independent cytosolic PLA2s (iPLA2s). Platelet-activating factor acetylhydrolases (PAF-AHs), lysosomal PLA2s, and adipose-specific PLA2 also belong to the class of PLA2s. Generally, cPLA2 enzymes are believed to play a major role in the
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Wei, Yulong, Lesan Yan, Lijun Luo, et al. "Phospholipase A2 inhibitor–loaded micellar nanoparticles attenuate inflammation and mitigate osteoarthritis progression." Science Advances 7, no. 15 (2021): eabe6374. http://dx.doi.org/10.1126/sciadv.abe6374.

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Treating osteoarthritis (OA) remains a major clinical challenge. Despite recent advances in drug discovery and development, no disease-modifying drug for knee OA has emerged with any notable clinical success, in part, due to the lack of valid and responsive therapeutic targets and poor drug delivery within knee joints. In this work, we show that the amount of secretory phospholipase A2 (sPLA2) enzyme increases in the articular cartilage in human and mouse OA cartilage tissues. We hypothesize that the inhibition of sPLA2 activity may be an effective treatment strategy for OA. To develop an sPLA
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Taketomi, Yoshitaka, Yoshimi Miki, and Makoto Murakami. "Old but New: Group IIA Phospholipase A2 as a Modulator of Gut Microbiota." Metabolites 12, no. 4 (2022): 352. http://dx.doi.org/10.3390/metabo12040352.

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Among the phospholipase A2 (PLA2) superfamily, the secreted PLA2 (sPLA2) family contains 11 mammalian isoforms that exhibit unique tissue or cellular distributions and enzymatic properties. Current studies using sPLA2-deficient or -overexpressed mouse strains, along with mass spectrometric lipidomics to determine sPLA2-driven lipid pathways, have revealed the diverse pathophysiological roles of sPLA2s in various biological events. In general, individual sPLA2s exert their specific functions within tissue microenvironments, where they are intrinsically expressed through hydrolysis of extracellu
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Hite, R. Duncan, Michael C. Seeds, Randy B. Jacinto, R. Balasubramanian, Moseley Waite, and David Bass. "Hydrolysis of surfactant-associated phosphatidylcholine by mammalian secretory phospholipases A2." American Journal of Physiology-Lung Cellular and Molecular Physiology 275, no. 4 (1998): L740—L747. http://dx.doi.org/10.1152/ajplung.1998.275.4.l740.

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Hydrolysis of surfactant-associated phospholipids by secretory phospholipases A2 is an important potential mechanism for surfactant dysfunction in inflammatory lung diseases. In these conditions, airway secretory phospholipase A2(sPLA2) activity is increased, but the type of sPLA2 and its impact on surfactant function are not well understood. We examined in vitro the effect of multiple secretory phospholipases A2 on surfactant, including their ability to 1) release free fatty acids, 2) release lysophospholipids, and 3) increase the minimum surface tension (γmin) on a pulsating bubble surfactom
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Krizaj, Igor. "Roles of Secreted Phospholipases A2 in the Mammalian Immune System." Protein & Peptide Letters 21, no. 12 (2014): 1201–8. http://dx.doi.org/10.2174/0929866521666140819122624.

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Secreted phospholipase A2 (sPLA2) molecules constitute a family of proteins that are involved functionally in many biological processes. In particular, they participate in diverse pathophysiological settings as enzymes that release free fatty acids and lysophospholipids from phospholipids in biological membranes, or as ligands for various cellular receptors. In this review the confirmed or expected functions of sPLA2s in the mammalian immune system are surveyed. Some of the twelve mammalian sPLA2 molecules constitute part of the so-called innate immune system by virtue of their antibacterial,
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Wong, Dennis A., Yoshihiro Kita, Naonori Uozumi та Takao Shimizu. "Discrete Role for Cytosolic Phospholipase A2α in Platelets". Journal of Experimental Medicine 196, № 3 (2002): 349–57. http://dx.doi.org/10.1084/jem.20011443.

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Among several different types of phospholipase A2 (PLA2), cytosolic PLA2 (cPLA2)α and group IIA (IIA) secretory PLA2 (sPLA2) have been studied intensively. To determine the discrete roles of cPLA2α in platelets, we generated two sets of genetically engineered mice (cPLA2α−/−/sPLA2-IIA−/− and cPLA2α−/−/sPLA2-IIA+/+) and compared their platelet function with their respective wild-type C57BL/6J mice (cPLA2α+/+/sPLA2-IIA−/−) and C3H/HeN (cPLA2α+/+/sPLA2-IIA+/+). We found that cPLA2α is needed for the production of the vast majority of thromboxane (TX)A2 with collagen stimulation of platelets. In c
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Hite, R. Duncan, Michael C. Seeds, Anca M. Safta, et al. "Lysophospholipid generation and phosphatidylglycerol depletion in phospholipase A2-mediated surfactant dysfunction." American Journal of Physiology-Lung Cellular and Molecular Physiology 288, no. 4 (2005): L618—L624. http://dx.doi.org/10.1152/ajplung.00274.2004.

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Pulmonary surfactant's complex mixture of phospholipids and proteins reduces the work of breathing by lowering alveolar surface tension during respiration. One mechanism of surfactant damage appears to be the hydrolysis of phospholipid by phospholipases activated in the inflamed lung. Humans have several candidate secretory phospholipase A2 (sPLA2) enzymes in lung cells and infiltrating leukocytes that could damage extracellular surfactant. We considered two mechanisms of surfactant disruption by five human sPLA2s, including generation of lysophospholipids and the depletion of specific phospho
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Sato, Hiroyasu, Yoshitaka Taketomi, Yuki Isogai, et al. "Group III secreted phospholipase A2 transgenic mice spontaneously develop inflammation." Biochemical Journal 421, no. 1 (2009): 17–27. http://dx.doi.org/10.1042/bj20082429.

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PLA2 (phospholipase A2) group III is an atypical sPLA2 (secretory PLA2) that is homologous with bee venom PLA2 rather than with other mammalian sPLA2s. In the present paper, we show that endogenous group III sPLA2 (PLA2G3) is expressed in mouse skin and that Tg (transgenic) mice overexpressing human PLA2G3 spontaneously develop skin inflammation. Pla2g3-Tg mice over 9 months of age frequently developed dermatitis with hyperkeratosis, acanthosis, parakeratosis, erosion, ulcer and sebaceous gland hyperplasia. The dermatitis was accompanied by infiltration of neutrophils and macrophages and by el
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K, Endang Retnowati, Wiyanda Hidayati S, and Liana . "AKTIVITAS FOSFOLIPASE-A2 SEKRETORIS PLASMA TROMBOSITOPENIA DEMAM BERDARAH DENGUE." INDONESIAN JOURNAL OF CLINICAL PATHOLOGY AND MEDICAL LABORATORY 17, no. 1 (2018): 12. http://dx.doi.org/10.24293/ijcpml.v17i1.1042.

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Infected macrophages by dengue virus will produce phospholipase-A2 (PLA2) enzyme, that can promote arachidonic acidmetabolism that produce inflammatory mediators, causing endhothelial damage and severe plasma leakage. Capillary endothelialdamage can cause platelet adhesion and aggregation, so that many platelets will be consumed. The role of sPLA2 (secretoryphospholipase-A2), which is a part of PLA2 in dengue and thrombocytopenia up to now has not been widely studied. The objective ofthe study is to analyze the association between the activity of plasma secretory phospholipase-A2 and the degre
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Ramoner, Reinhold, Thomas Putz, Hubert Gander, et al. "Dendritic-cell activation by secretory phospholipase A2." Blood 105, no. 9 (2005): 3583–87. http://dx.doi.org/10.1182/blood-2004-08-3001.

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Abstract Dendritic cells (DCs), also referred to as the sentinels of the immune system, induce and coordinate important functions of immune surveillance. DCs acquire immunity-initiating capacity only after a process of maturation usually induced by ligands that bind to members of the tumor necrosis factor (TNF) or toll-like receptor families. Secretory phospholipase A2 (sPLA2), which hydrolyzes the sn-2 ester bond of glycerophospholipids, regulates a variety of cellular functions including migration of endothelial cells and neurite outgrowth. In the present study we investigated the role of sP
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Muñoz-Sanjuán, Ignacio, and Ali H. Brivanlou. "Induction of Ectopic Olfactory Structures and Bone Morphogenetic Protein Inhibition by Rossy, a Group XII Secreted Phospholipase A2." Molecular and Cellular Biology 25, no. 9 (2005): 3608–19. http://dx.doi.org/10.1128/mcb.25.9.3608-3619.2005.

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ABSTRACT The secreted phospholipases A2 (sPLA2s) comprise a family of small secreted proteins with the ability to catalyze the generation of bioactive lipids through glycophospholipid hydrolysis. Recently, a large number of receptor proteins and extracellular binding partners for the sPLA2s have been identified, suggesting that these secreted factors might exert a subset of their broad spectrum of biological activities independently of their enzymatic activity. Here, we describe an activity for the sPLA2 group XII (sPLA2-gXII) gene during Xenopus laevis early development. In the ectoderm, sPLA
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NAKASHIMA, Satoru, Yutaka IKENO, Tatsuya YOKOYAMA, et al. "Secretory phospholipases A2 induce neurite outgrowth in PC12 cells." Biochemical Journal 376, no. 3 (2003): 655–66. http://dx.doi.org/10.1042/bj20030830.

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sPLA2s (secretory phospholipases A2) belong to a broad and structurally diverse family of enzymes that hydrolyse the sn-2 ester bond of glycerophospholipids. We previously showed that a secreted fungal 15 kDa protein, named p15, as well as its orthologue from Streptomyces coelicolor (named Scp15) induce neurite outgrowth in PC12 cells at nanomolar concentrations. We report here that both p15 and Scp15 are members of a newly identified group of fungal/bacterial sPLA2s. The phospholipid-hydrolysing activity of p15 is absolutely required for neurite outgrowth induction. Mutants with a reduced PLA
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Urazov, S. P., A. N. Chernov, A. V. Cherkas, et al. "Secretory phospholipase A2: a biomarker of inflammation in autoimmune, bacterial and viral diseases." Medical Immunology (Russia) 24, no. 4 (2022): 705–28. http://dx.doi.org/10.15789/1563-0625-spa-2460.

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Secretory phospholipases A2 (sPLA2) represent a large superfamily of enzymes with a molecular weight of 14-19 kDa, including 15 groups and more than 30 isoforms belonging to four types: secretory (sPLA2), cytosolic (cPLA2), calcium-independent (iPLA2) and lipoprotein-associated phospholipase A2 (LP-PLA2, PAF-AH). Eleven species of secretory sPLA2s (IB, IIA, IIC, IID, IIE, IIF, III, V, X, XIIA, and XIIB) have been found in mammals, performing versatile functions and participating in the pathogenesis of a wide range of diseases. On the one hand, sPLA2 may promote elimination of damaged, apoptoti
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Christerson, Ulrika, Åsa V. Keita, Martin E. Winberg, Johan D. Söderholm, and Christina Gustafson-Svärd. "Possible Involvement of Intracellular Calcium-Independent Phospholipase A2 in the Release of Secretory Phospholipases from Mast Cells—Increased Expression in Ileal Mast Cells of Crohn’s Disease." Cells 8, no. 7 (2019): 672. http://dx.doi.org/10.3390/cells8070672.

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Increased activity of secretory phospholipases A2 (sPLA2) type-II was previously observed in ileum of Crohn’s disease (CD). Our aims were to explore the involvement of calcium-independent (i)PLA2β in the release of sPLA2s from the human mast cell (MC) line (HMC-1) and investigate expressions of cytosolic (c)PLA2α, iPLA2β, sPLA2-IIA and sPLA2-V in MCs of CD ileum. The release of sPLA2 was investigated in HMC-1 by immunocytochemistry and ELISA. The expression intensities of PLA2s in mucosal MCs, and the proportion of PLA2-positive MCs, were investigated in normal ileum and in ileum from patients
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POLGÁR, János, Ruth M. KRAMER, Suzane L. UM, Joseph A. JAKUBOWSKI, and Kenneth J. CLEMETSON. "Human group II 14 kDa phospholipase A2 activates human platelets." Biochemical Journal 327, no. 1 (1997): 259–65. http://dx.doi.org/10.1042/bj3270259.

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Recombinant human group II phospholipase A2 (sPLA2) added to human platelets in the low μg/ml range induced platelet activation, as demonstrated by measurement of platelet aggregation, thromboxane A2 generation and influx of intracellular free Ca2+ concentration and by detection of time-dependent tyrosine phosphorylation of platelet proteins. The presence of Ca2+ at low millimolar concentrations is a prerequisite for the activation of platelets by sPLA2. Mg2+ cannot replace Ca2+. Mg2+, given in addition to the necessary Ca2+, inhibits sPLA2-induced platelet activation. Pre-exposure to sPLA2 co
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Masuda, Seiko, Kei Yamamoto, Tetsuya Hirabayashi, et al. "Human group III secreted phospholipase A2 promotes neuronal outgrowth and survival." Biochemical Journal 409, no. 2 (2007): 429–38. http://dx.doi.org/10.1042/bj20070844.

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Human sPLA2-III [group III secreted PLA2 (phospholipase A2)] is an atypical sPLA2 isoenzyme that consists of a central group III sPLA2 domain flanked by unique N- and C-terminal domains. In the present study, we found that sPLA2-III is expressed in neuronal cells, such as peripheral neuronal fibres, spinal DRG (dorsal root ganglia) neurons and cerebellar Purkinje cells. Adenoviral expression of sPLA2-III in PC12 cells (pheochromocytoma cells) or DRG explants facilitated neurite outgrowth, whereas expression of a catalytically inactive sPLA2-III mutant or use of sPLA2-III-directed siRNA (small
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Lee, In-Chul, Dae Yong Kim, and Jong-Sup Bae. "Inhibitory Effect of Zingerone on Secretory Group IIA Phospholipase A2." Natural Product Communications 12, no. 6 (2017): 1934578X1701200. http://dx.doi.org/10.1177/1934578x1701200624.

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The expression of secretory group IIA phospholipase A2 (sPLA2-IIA) has been shown to be elevated in various inflammatory diseases, and lipopolysaccharide (LPS) up-regulates the expression of sPLA2-IIA in human umbilical vein endothelial cells (HUVECs). Zingerone (ZGR), a phenolic alkanone isolated from ginger, has been reported to have various pharmacological activities. Here, we examined the effects of ZRG on the expression and activity of sPLA2-IIA in LPS-activated HUVECs and in mouse models of endotoxemia and sepsis. Treatment of cells or mice with ZRG inhibited LPS-induced expression and a
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Henderson, William R., Emil Y. Chi, James G. Bollinger, et al. "Importance of group X–secreted phospholipase A2 in allergen-induced airway inflammation and remodeling in a mouse asthma model." Journal of Experimental Medicine 204, no. 4 (2007): 865–77. http://dx.doi.org/10.1084/jem.20070029.

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Arachidonic acid metabolites, the eicosanoids, are key mediators of allergen-induced airway inflammation and remodeling in asthma. The availability of free arachidonate in cells for subsequent eicosanoid biosynthesis is controlled by phospholipase A2s (PLA2s), most notably cytosolic PLA2-α. 10 secreted PLA2s (sPLA2s) have also been identified, but their function in eicosanoid generation is poorly understood. We investigated the role of group X sPLA2 (sPLA2-X), the sPLA2 with the highest in vitro cellular phospholipolysis activity, in acute and chronic mouse asthma models in vivo. The lungs of
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Mitsuishi, Michiko, Seiko Masuda, Ichiro Kudo, and Makoto Murakami. "Group V and X secretory phospholipase A2 prevents adenoviral infection in mammalian cells." Biochemical Journal 393, no. 1 (2005): 97–106. http://dx.doi.org/10.1042/bj20050781.

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sPLA2 (secretory phospholipase A2) enzymes have been implicated in various biological events, yet their precise physiological functions remain largely unresolved. In the present study we show that group V and X sPLA2s, which are two potent plasma membrane-acting sPLA2s, are capable of preventing host cells from being infected with an adenovirus. Bronchial epithelial cells and lung fibroblasts pre-expressing group V and X sPLA2s showed marked resistance to adenovirus-mediated gene delivery in a manner dependent on their catalytic activity. Although adenovirus particles were insensitive to recom
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Lee, In-Chul, and Jong-Sup Bae. "Inhibitory Effect of Pelargonidin on Secretory Group IIA Phospholipase A2." Natural Product Communications 13, no. 8 (2018): 1934578X1801300. http://dx.doi.org/10.1177/1934578x1801300811.

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The expression of secretory group IIA phospholipase A2 (sPLA2-IIA) has been shown to be elevated in various inflammatory diseases, and lipopolysaccharide (LPS) up-regulates the expression of sPLA2-IIA in human umbilical vein endothelial cells (HUVECs). Pelargonidin (PEL) is a well-known red pigment found in plants, and has been reported as having important biological activities that are potentially beneficial for human health. Here, PEL was examined for its effects on the expression and activity of sPLA2-IIA in HUVECs and mouse. Post treatment of cells or mouse with PEL inhibited LPS-induced e
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Styles, LA, CG Schalkwijk, AJ Aarsman, EP Vichinsky, BH Lubin, and FA Kuypers. "Phospholipase A2 levels in acute chest syndrome of sickle cell disease." Blood 87, no. 6 (1996): 2573–78. http://dx.doi.org/10.1182/blood.v87.6.2573.bloodjournal8762573.

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Acute chest syndrome (ACS) is associated with significant morbidity and is the leading cause of death in patients with sickle cell disease (SCD). Recent reports suggest that bone marrow fat embolism can be detected in many cases of severe ACS. Secretory phospholipase A2 (sPLA2) is an important inflammatory mediator and liberates free fatty acids, which are felt to be responsible for the acute lung injury of the fat embolism syndrome. We measured SPLA2 levels in 35 SCD patients during 20 admissions for ACS, 10 admissions for vaso-occlusive crisis, and during 12 clinic visits when patients were
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Kang, Bu-Gyeong, Seung-Yeon Kwon, Hyo-Ran Lee, et al. "Structural and functional characterization of a thermostable secretory phospholipase A2 from Sciscionella marina and its application in liposome biotransformation." Acta Crystallographica Section D Structural Biology 79, no. 2 (2023): 188–97. http://dx.doi.org/10.1107/s2059798323000384.

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Secretory phospholipase A2 (sPLA2), which hydrolyzes the sn-2 acyl bond of lecithin in a Ca2+-dependent manner, is an important enzyme in the oil and oleochemical industries. However, most sPLA2s are not stable under process conditions. Therefore, a thermostable sPLA2 was investigated in this study. A marine bacterial sPLA2 isolated from Sciscionella marina (Sm-sPLA2) was catalytically active even after 5 h of incubation at high temperatures of up to 50°C, which is outstanding compared with a representative bacterial sPLA2 (i.e. sPLA2 from Streptomyces violaceoruber; Sv-sPLA2). Consistent with
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Arbibe, L., D. Vial, I. Rosinski-Chupin, et al. "Endotoxin induces expression of type II phospholipase A2 in macrophages during acute lung injury in guinea pigs: involvement of TNF-alpha in lipopolysaccharide-induced type II phospholipase A2 synthesis." Journal of Immunology 159, no. 1 (1997): 391–400. http://dx.doi.org/10.4049/jimmunol.159.1.391.

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Abstract Elevated levels of secretory type II phospholipase A2 (sPLA2-II) have been associated with a poor clinical outcome in the acute respiratory distress syndrome. This study identifies the cell source(s) and the mechanisms of sPLA2-II synthesis in the guinea pig model of acute respiratory distress syndrome induced by intratracheal injection of LPS. Administration of LPS led to an increase in lung membrane-associated calcium-dependent sPLA2 activity, which was abrogated by LY311727, a selective inhibitor of sPLA2-II. No sPLA2 activity was detected in the vascular compartment of the lung. L
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Zhao, Hongxia, and Paavo K. J. Kinnunen. "Modulation of the Activity of Secretory Phospholipase A2 by Antimicrobial Peptides." Antimicrobial Agents and Chemotherapy 47, no. 3 (2003): 965–71. http://dx.doi.org/10.1128/aac.47.3.965-971.2003.

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ABSTRACT The antimicrobial peptides magainin 2, indolicidin, and temporins B and L were found to modulate the hydrolytic activity of secretory phospholipase A2 (sPLA2) from bee venom and in human lacrimal fluid. More specifically, hydrolysis of phosphatidylcholine (PC) liposomes by bee venom sPLA2 at 10 μM Ca2+ was attenuated by these peptides while augmented product formation was observed in the presence of 5 mM Ca2+. The activity of sPLA2 towards anionic liposomes was significantly enhanced by the antimicrobial peptides at low [Ca2+] and was further enhanced in the presence of 5 mM Ca2+. Sim
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Rodrigues, Caroline Fabri Bittencourt, Marcelo José Pena Ferreira, Mariana Novo Belchor, et al. "Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2." Marine Drugs 17, no. 7 (2019): 403. http://dx.doi.org/10.3390/md17070403.

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Ellagitannins constitute the largest group of hydrolyzable tannins of plants, and, from this group, casuarictin (Casu) was identified in some plant species. However, to our knowledge, no investigation of secretory phospholipase A2 (sPLA2) inhibition by Casu has been performed yet. Casuarictin was isolated by chromatography n-butanol (n-BuOH) partition of Laguncularia racemosa leaves. The pharmacological and biological effects of Casu were evaluated on isolated sPLA2 from the rattlesnake (Crotalus durissus terrificus) and using a plant bacterial strain. The compound was able to form a protein c
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Styles, Lori A., Anton J. Aarsman, Elliott P. Vichinsky, and Frans A. Kuypers. "Secretory phospholipase A2 predicts impending acute chest syndrome in sickle cell disease." Blood 96, no. 9 (2000): 3276–78. http://dx.doi.org/10.1182/blood.v96.9.3276.

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Abstract Acute chest syndrome (ACS) is the leading cause of death in sickle cell disease. Severe ACS often develops in the course of a vaso-occlusive crisis (VOC), but currently there are no predictors for its development. Secretory phospholipase A2(sPLA2), a potent inflammatory mediator, is elevated in ACS, and previous work suggests that sPLA2 predicts impending ACS. We prospectively evaluated sPLA2concentration during 21 admissions for VOC; 6 of these patients went on to develop ACS. Elevation of sPLA2 was detected all 6 patients 24 to 48 hours before ACS was clinically diagnosed. Adding th
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Styles, Lori A., Anton J. Aarsman, Elliott P. Vichinsky, and Frans A. Kuypers. "Secretory phospholipase A2 predicts impending acute chest syndrome in sickle cell disease." Blood 96, no. 9 (2000): 3276–78. http://dx.doi.org/10.1182/blood.v96.9.3276.h8003276_3276_3278.

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Acute chest syndrome (ACS) is the leading cause of death in sickle cell disease. Severe ACS often develops in the course of a vaso-occlusive crisis (VOC), but currently there are no predictors for its development. Secretory phospholipase A2(sPLA2), a potent inflammatory mediator, is elevated in ACS, and previous work suggests that sPLA2 predicts impending ACS. We prospectively evaluated sPLA2concentration during 21 admissions for VOC; 6 of these patients went on to develop ACS. Elevation of sPLA2 was detected all 6 patients 24 to 48 hours before ACS was clinically diagnosed. Adding the require
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Choi, Hyukjae, Sae-Kwang Ku, and Jong-Sup Bae. "Inhibitory Effect of Three Diketopiperazines from Marine-derived Bacteria on Secretory Group IIA Phospholipase A2." Natural Product Communications 11, no. 9 (2016): 1934578X1601100. http://dx.doi.org/10.1177/1934578x1601100919.

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Diketopiperazines, natural products found in bacteria, fungi, marine sponges, gorgonian and red algae, are cyclic dipeptides possessing relatively simple and rigid structures with chiral nature and various side chains. The compounds in this structure class have been known to possess diverse bioactivities including antibiotic activity, anti-cancer activity, neuroprotective activity, and anti-inflammatory activity. The expression of secretory group IIA phospholipase A2 (sPLA2-IIA) is enhanced by development of inflammatory disorders. Aim of this study is to determine the effects of diketopiperaz
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KOUMANOV, Kamen, Claude WOLF, and Gilbert BÉREZIAT. "Modulation of human type II secretory phospholipase A2 by sphingomyelin and annexin VI." Biochemical Journal 326, no. 1 (1997): 227–33. http://dx.doi.org/10.1042/bj3260227.

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Conjectural results have been reported on the capacity of inflammatory secreted phospholipase A2 (sPLA2) to hydrolyse mammalian membrane phospholipids. Development of an assay based on the release of non-esterified fatty acids by the enzyme acting on the organized phospholipid mixture constituting the membrane matrix has led to the identification of two prominent effectors, sphingomyelin (SPH) and annexin. Recombinant human type II sPLA2 hydrolyses red-cell membrane phospholipids with a marked preference for the inner leaflet. This preference is apparently related to the high content of SPH in
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Petrovič, Uroš, Jernej Šribar, Maja Matis, et al. "Ammodytoxin, a secretory phospholipase A2, inhibits G2 cell-cycle arrest in the yeast Saccharomyces cerevisiae." Biochemical Journal 391, no. 2 (2005): 383–88. http://dx.doi.org/10.1042/bj20050417.

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Ammodytoxin (Atx), an sPLA2 (secretory phospholipase A2), binds to γ and ε isoforms of porcine 14-3-3 proteins in vitro. 14-3-3 proteins are evolutionarily conserved eukaryotic regulatory proteins involved in a variety of biological processes, including cell-cycle regulation. We have now shown that Atx binds to yeast 14-3-3 proteins with an affinity similar to that for the mammalian isoforms. Thus yeast Saccharomyces cerevisiae can be used as a model eukaryotic cell, which lacks endogenous phospholipases A2, to assess the in vivo relevance of this interaction. Atx was expressed in yeast cells
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MASUDA, Seiko, Makoto MURAKAMI, Michiko MITSUISHI, et al. "Expression of secretory phospholipase A2 enzymes in lungs of humans with pneumonia and their potential prostaglandin-synthetic function in human lung-derived cells." Biochemical Journal 387, no. 1 (2005): 27–38. http://dx.doi.org/10.1042/bj20041307.

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Although a number of sPLA2 (secretory phospholipase A2) enzymes have been identified in mammals, the localization and functions of individual enzymes in human pathologic tissues still remain obscure. In the present study, we have examined the expression and function of sPLA2s in human lung-derived cells and in human lungs with pneumonia. Group IID, V and X sPLA2s were expressed in cultured human bronchial epithelial cells (BEAS-2B) and normal human pulmonary fibroblasts with distinct requirement for cytokines (interleukin-1β, tumour necrosis factor α and interferon-γ). Lentivirus- or adenoviru
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O'Donoghue, Michelle L., Ziad Mallat, David A. Morrow, et al. "Prognostic Utility of Secretory Phospholipase A2 in Patients with Stable Coronary Artery Disease." Clinical Chemistry 57, no. 9 (2011): 1311–17. http://dx.doi.org/10.1373/clinchem.2011.166520.

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BACKGROUND Secretory phospholipase A2 (sPLA2) may contribute to atherogenesis. To date, few prospective studies have examined the utility of sPLA2 for risk stratification in coronary artery disease (CAD). METHODS We measured plasma sPLA2 activity at baseline in 3708 subjects in the PEACE randomized trial of trandolapril vs placebo in stable CAD. Median follow-up was 4.8 years. We used Cox regression to adjust for demographics, clinical risk factors, apolipoprotein B, apolipoprotein A1, and medications. RESULTS After multivariable adjustment, sPLA2 was associated with an increased risk of cardi
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Ball, James B., Samina Y. Khan, Nathan JD McLaughlin, Rachelle Nuss, Laura Cole, and Christopher C. Silliman. "Hydroxyurea Treatment of Children with Sickle Cell Disease Inhibits RBC Membrane Degradation by Secretory Phospholipase a2." Blood 112, no. 11 (2008): 1427. http://dx.doi.org/10.1182/blood.v112.11.1427.1427.

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Abstract Background: Secretory phospholipase A2 is an enzyme that is elevated in SCD patients with acute chest syndrome (ACS) and vaso-occlusive pain crisis (VOC) and inhibition of its enzymatic activity is in trials for ACS prevention (Styles LA. Blood.1996; 87:2573). This enzyme cleaves arachidonic acid from the phospholipids of red blood cell (RBC) membranes; and arachidonic acid can be converted to other pro-inflammatory lipid compounds (Murakami M. J Biochem.2002; 131:285). sPLA2 cleaves phosphatidylserine (PS) expressing lipid membranes. PS is usually in the inner leaflet (unexposed) in
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Hite, R. Duncan, Bonnie L. Grier, B. Moseley Waite, et al. "Surfactant protein B inhibits secretory phospholipase A2 hydrolysis of surfactant phospholipids." American Journal of Physiology-Lung Cellular and Molecular Physiology 302, no. 2 (2012): L257—L265. http://dx.doi.org/10.1152/ajplung.00054.2011.

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Hydrolysis of surfactant phospholipids (PL) by secretory phospholipases A2 (sPLA2) contributes to surfactant damage in inflammatory airway diseases such as acute lung injury/acute respiratory distress syndrome. We and others have reported that each sPLA2 exhibits specificity in hydrolyzing different PLs in pulmonary surfactant and that the presence of hydrophilic surfactant protein A (SP-A) alters sPLA2-mediated hydrolysis. This report tests the hypothesis that hydrophobic SP-B also inhibits sPLA2-mediated surfactant hydrolysis. Three surfactant preparations were used containing varied amounts
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Pruzanski, W., F. C. de Beer, M. C. de Beer, E. Stefanski, and P. Vadas. "Serum amyloid A protein enhances the activity of secretory non-pancreatic phospholipase A2." Biochemical Journal 309, no. 2 (1995): 461–64. http://dx.doi.org/10.1042/bj3090461.

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The acute-phase proteins serum amyloid A protein (SAA) and secretory phospholipase A2 (sPLA2) are simultaneously expressed during inflammatory conditions. SAA associates with high-density lipoprotein (HDL) altering its physicochemical composition. We found that purified acute-phase SAA, but not the constitutive form, markedly enhances the lipolytic activity of sPLA2 in a dose-related manner with phosphatidylcholine/lysophosphatidylcholine or phosphatidylethanolamine/lysophosphatidylethanolamine liposomal substrates. Normal HDL was found to reduce activity of sPLA2 in a dose-dependent manner, b
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Nakashima, Akina, Susumu Tomono, Tatsuya Yamazaki, et al. "Phospholipase A2 from bee venom increases poly(I:C)-induced activation in human keratinocytes." International Immunology 32, no. 6 (2020): 371–83. http://dx.doi.org/10.1093/intimm/dxaa005.

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Abstract Bee venom (BV) induces skin inflammation, characterized by erythema, blisters, edemas, pain and itching. Although BV has been found to have an inhibitory effect on toll-like receptors (TLRs), we here show that BV enhances keratinocyte responses to polyinosinic-polycytidylic acid [poly(I:C)], a ligand for TLR3. Our results revealed that the enhanced TLR activity was primarily induced by secretory phospholipase A2 (sPLA2), a component of BV (BV-sPLA2). PLA2 mediates the hydrolysis of membrane phospholipids into lysophospholipids and free fatty acids. We demonstrated that BV-sPLA2 increa
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Autilio, Chiara, Shivani Shankar-Aguilera, Angelo Minucci, Lhoussaine Touqui, and Daniele De Luca. "Effect of cooling on lung secretory phospholipase A2 activity in vitro, ex vivo, and in vivo." American Journal of Physiology-Lung Cellular and Molecular Physiology 316, no. 3 (2019): L498—L505. http://dx.doi.org/10.1152/ajplung.00201.2018.

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Hypothermia can modify surfactant composition and function. Secretory phospholipase A2 (sPLA2) hydrolyses surfactant phospholipids and is important in the pathobiology of several critical respiratory disorders. We hypothesize that sPLA2 activity might be influenced by the temperature partially explaining surfactant changes. This study aims to evaluate comprehensively the effect of hypothermia on sPLA2 activity. We measured sPLA2 activity at different temperatures, alone or combined with bile acids, in vitro (incubating human recombinant sPLA2-IIA and porcine sPLA2-IB), ex vivo (by cooling bron
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Watanabe, Kazuhiro, Yoshitaka Taketomi, Yoshimi Miki, Kiyotaka Kugiyama, and Makoto Murakami. "Group V secreted phospholipase A2 plays a protective role against aortic dissection." Journal of Biological Chemistry 295, no. 30 (2020): 10092–111. http://dx.doi.org/10.1074/jbc.ra120.013753.

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Aortic dissection is a life-threatening aortopathy involving separation of the aortic wall, whose underlying mechanisms are still incompletely understood. Epidemiological evidence suggests that unsaturated fatty acids improve cardiovascular health. Here, using quantitative RT-PCR, histological analyses, magnetic cell sorting and flow cytometry assays, and MS-based lipidomics, we show that the activity of a lipid-metabolizing enzyme, secreted phospholipase A2 group V (sPLA2-V), protects against aortic dissection by endogenously mobilizing vasoprotective lipids. Global and endothelial cell–speci
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Giresha, Aladahalli S., Deepadarshan Urs, Sophiya Pundalik, et al. "Sinapicacid Inhibits Group IIA Secretory Phospholipase A2 and Its Inflammatory Response in Mice." Antioxidants 11, no. 7 (2022): 1251. http://dx.doi.org/10.3390/antiox11071251.

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Human Group IIA secreted phospholipase A2 (sPLA2-IIA) enzyme plays a crucial role in several chronic inflammatory diseases such asasthma, atherosclerosis, gout, bronchitis, etc. Several studies showed that the antioxidants exert an anti-inflammatory function by inhibiting the sPLA2-IIA enzyme. Hence, the present study evaluated an antioxidant molecule, sinapic acid, for sPLA2-IIA inhibition as an anti-inflammatory function. Initially, the antioxidant efficacy of sinapic acid was evaluated, and it showed greater antioxidant potency. Further, sinapic acid inhibited 94.4 ± 4.83% of sPLA2-IIA acti
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SUN, Yong-Xin, Kazuhito TSUBOI, Yasuo OKAMOTO, et al. "Biosynthesis of anandamide and N-palmitoylethanolamine by sequential actions of phospholipase A2 and lysophospholipase D." Biochemical Journal 380, no. 3 (2004): 749–56. http://dx.doi.org/10.1042/bj20040031.

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Anandamide (an endocannabinoid) and other bioactive long-chain NAEs (N-acylethanolamines) are formed by direct release from N-acyl-PE (N-acyl-phosphatidylethanolamine) by a PLD (phospholipase D). However, the possible presence of a two-step pathway from N-acyl-PE has also been suggested previously, which comprises (1) the hydrolysis of N-acyl-PE to N-acyl-lysoPE by PLA1/PLA2 enzyme(s) and (2) the release of NAEs from N-acyllysoPE by lysoPLD (lysophospholipase D) enzyme(s). In the present study we report for the first time the characterization of enzymes responsible for this pathway. The PLA1/P
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Leiguez, Elbio, Priscila Motta, Rodrigo Maia Marques, Bruno Lomonte, Suely Vilela Sampaio, and Catarina Teixeira. "A Representative GIIA Phospholipase A2 Activates Preadipocytes to Produce Inflammatory Mediators Implicated in Obesity Development." Biomolecules 10, no. 12 (2020): 1593. http://dx.doi.org/10.3390/biom10121593.

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Adipose tissue secretes proinflammatory mediators which promote systemic and adipose tissue inflammation seen in obesity. Group IIA (GIIA)-secreted phospholipase A2 (sPLA2) enzymes are found to be elevated in plasma and adipose tissue from obese patients and are active during inflammation, generating proinflammatory mediators, including prostaglandin E2 (PGE2). PGE2 exerts anti-lipolytic actions and increases triacylglycerol levels in adipose tissue. However, the inflammatory actions of GIIA sPLA2s in adipose tissue cells and mechanisms leading to increased PGE2 levels in these cells are uncle
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Rys-Sikora, Krystyna E., Raymond L. Konger, John W. Schoggins, Rama Malaviya, and Alice P. Pentland. "Coordinate expression of secretory phospholipase A2 and cyclooxygenase-2 in activated human keratinocytes." American Journal of Physiology-Cell Physiology 278, no. 4 (2000): C822—C833. http://dx.doi.org/10.1152/ajpcell.2000.278.4.c822.

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PGE2 levels are altered in human epidermis after in vivo wounding; however, mechanisms modulating PGE2 production in activated keratinocytes are unclear. In previous studies, we showed that PGE2 is a growth-promoting autacoid in human primary keratinocyte cultures, and its production is modulated by plating density, suggesting that regulated PGE2 synthesis is an important component of wound healing. Here, we examine the role of phospholipase A2(PLA2) and cyclooxygenase (COX) enzymes in modulation of PGE2 production. We report that the increased PGE2 production that occurs in keratinocytes grow
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Lewin, Matthew, José Gutiérrez, Stephen Samuel, et al. "Delayed Oral LY333013 Rescues Mice from Highly Neurotoxic, Lethal Doses of Papuan Taipan (Oxyuranus scutellatus) Venom." Toxins 10, no. 10 (2018): 380. http://dx.doi.org/10.3390/toxins10100380.

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There is an unmet need for economical snakebite therapies with long shelf lives that are effective even with delays in treatment. The orally bioavailable, heat-stable, secretory phospholipase A2 (sPLA2) inhibitor, LY333013, demonstrates antidotal characteristics for severe snakebite envenoming in both field and hospital use. A murine model of lethal envenoming by a Papuan taipan (Oxyuranus scutellatus) demonstrates that LY333013, even with delayed oral administration, improves the chances of survival. Furthermore, LY333013 improves the performance of antivenom even after it no longer reverses
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Nijmeijer, R., M. Willemsen, C. J. L. M. Meijer, et al. "Type II secretory phospholipase A2 binds to ischemic flip-flopped cardiomyocytes and subsequently induces cell death." American Journal of Physiology-Heart and Circulatory Physiology 285, no. 5 (2003): H2218—H2224. http://dx.doi.org/10.1152/ajpheart.00887.2002.

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Type II secretory phospholipase A2 (sPLA2) is a cardiovascular risk factor. We recently found depositions of sPLA2 in the necrotic center of infarcted human myocardium and normally appearing cardiomyocytes adjacent to the border zone. The consequences of binding of sPLA2 to ischemic cardiomyocytes are not known. To explore a potential effect of sPLA2 on ischemic cardiomyocytes at a cellular level we used an in vitro model. The cardiomyocyte cell line H9c2 or adult cardiomyocytes were isolated from rabbits that were incubated with sPLA2 in the presence of metabolic inhibitors to mimic ischemia-
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DONG, Chang-Zhi, Anthony ROMIEU, Carine M. MOUNIER, Françoise HEYMANS, Bernard P. ROQUES, and Jean-Jacques GODFROID. "Total direct chemical synthesis and biological activities of human group IIA secretory phospholipase A2." Biochemical Journal 365, no. 2 (2002): 505–11. http://dx.doi.org/10.1042/bj20011648.

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Human group IIA secretory phospholipase A2 (hGIIA sPLA2) is reported to be involved in inflammation, since its expression level is enhanced under various inflammatory conditions. In this work, we report the total chemical synthesis of this enzyme (124 amino acids) by solid-phase method. The identity of the protein, in denatured or folded (7 disulphide bonds) forms, was confirmed by electrospray MS. Synthetic sPLA2 possesses the same circular dichroism spectrum, enzymic activity in hydrolysing different phospholipid substrates, and inhibitory effect in thrombin formation from prothrombinase com
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Ewing, Heather, Virneliz Fernández-Vega, Timothy P. Spicer, et al. "Fluorometric High-Throughput Screening Assay for Secreted Phospholipases A2 Using Phospholipid Vesicles." Journal of Biomolecular Screening 21, no. 7 (2016): 713–21. http://dx.doi.org/10.1177/1087057116646742.

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There is interest in developing inhibitors of human group III secreted phospholipase A2 (hGIII-sPLA2) because this enzyme plays a role in mast cell maturation. There are no potent inhibitors for hGIII-sPLA2 reported to date, so we adapted a fluorescence-based enzyme activity monitoring method to a high-throughput screening format. We opted to use an assay based on phospholipid substrate present in phospholipid vesicles since this matrix more closely resembles the natural substrate of hGIII-sPLA2, as opposed to phospholipid/detergent mixed micelles. The substrate is a phospholipid analogue cont
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Kirschnek, Susanne, and Erich Gulbins. "Phospholipase A2 Functions in Pseudomonas aeruginosa- Induced Apoptosis." Infection and Immunity 74, no. 2 (2006): 850–60. http://dx.doi.org/10.1128/iai.74.2.850-860.2006.

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ABSTRACT Pseudomonas aeruginosa, a gram-negative, facultative pathogen, causes severe and often even lethal infections in immunocompromised patients, as well as cystic fibrosis patients. We show here that a variety of P. aeruginosa strains activate phospholipase A2 (PLA2), cultured epithelial cells, and fibroblasts, resulting in increased intracellular and extracellular arachidonic acid release. The use of different PLA2 inhibitors revealed that P. aeruginosa-induced arachidonic acid release is mediated by activation of cytosolic PLA2 (cPLA2), whereas iPLA2 or sPLA2 do not seem to be involved
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