Journal articles: 'Inflammation Phospholipase A2'

1

Pruzanski, W., and P. Vadas. "Phospholipase A2 and inflammation." Annals of the Rheumatic Diseases 48, no. 11 (November 1, 1989): 962–63. http://dx.doi.org/10.1136/ard.48.11.962-b.

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Lomonte, Bruno, Andrej Tarkowski, and Lars Å. Hanson. "Phospholipase A2 and inflammation." Molecular Medicine Today 1, no. 1 (April 1995): 9. http://dx.doi.org/10.1016/1357-4310(95)80011-5.

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Lehr, Matthias. "Phospholipase A2 inhibitors in inflammation." Expert Opinion on Therapeutic Patents 11, no. 7 (July 2001): 1123–36. http://dx.doi.org/10.1517/13543776.11.7.1123.

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Thomas, Riji, Ajaikumar Sukumaran, Thushara Thomas, Deepa K. Vijayan, Jofy K. Paul, and D. M. Vasudevan. "Lipoprotein-associated Phospholipase A2: Current Trends in Invitro Diagnostics." International Journal of Scientific & Engineering Research 12, no. 4 (April 25, 2021): 1138–42. http://dx.doi.org/10.14299/ijser.2021.04.07.

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Lipoprotein-associated phospholipase A2 is an imminent reliable precise biomarker for vascular inflammation involved in the development of unstable plaques in cardiovascular diseases. The atherosclerotic plaque formation, inflammation and rupture of arterial vessels lead to heart attacks and strokes in most of the cases. The vessel-specific inflammatory enzyme, Lipoprotein-associated phospholipase A2 shoot ups in response to the rupture of arterial vessels having atherosclerotic plaques. The accurate measurement of Lipoprotein-associated phospholipase A2 envisages the individual risk of a patient and the treatment can be customized based on the result.

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Pniewska-Dawidczyk, Ewa, Izabela Kupryś-Lipińska, Gabriela Turek, Dorota Kacprzak, Joanna Wieczfinska, Paulina Kleniewska, Piotr Kuna, and Rafal Pawliczak. "Expression of cPLA2γ mRNA and protein differs the response of PBMC from severe and non-severe asthmatics to bacterial lipopolysaccharide and house dust mite allergen." International Journal of Immunopathology and Pharmacology 35 (January 2021): 205873842199095. http://dx.doi.org/10.1177/2058738421990952.

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Chronic inflammation in asthmatics is initiated/exacerbated by many environmental factors, such as bacterial lipopolysaccharide and allergens. Phospholipase A2 and histone acetyltransferase/deacetylases are enzymes involved in inflammatory process, particularly in lipid inflammatory mediators production and control of transcription of many inflammatory genes, respectively. The aim of the study was to identify differences in the inflammatory process in patients with severe and non-severe asthma, taking as a criterion expression of two groups of enzymes: phospholipases A2 and histone acetyltransferases/deacetylases. Thirty-two patients with severe, non-severe atopic to house dust mite asthmatics and 14 healthy volunteers were recruited. Peripheral blood mononuclear cells were stimulated with Dermatophagoides pteronyssinus allergen (nDer p1) and bacterial lipopolysaccharide (LPS). The expression of phospholipases A2 and histone acetyltransferases and deacetylases were assessed using TaqMan Low Density Array Cards. The protein expression was analyzed with immunoblot. Increased expression of phospholipase A2 Group IVC ( PLA2G4C) and cytosolic phospholipase A2 gamma (cPLA2γ) protein was observed in peripheral blood mononuclear cells (PBMC) from severe asthmatics in response to LPS and nDer p1, compared to non-severe asthmatics. nDer p1-stimulated PBMC from severe asthmatics exhibit induced expression of HDAC1 and similar trend was observed in protein concentration. Decreased expression of EP300 occurred in PBMC of severe asthmatics. PBMC from non-severe asthmatics showed decreased expression of HDAC2 and PLA2G15 after LPS treatment. In conclusion, in response to LPS and dust mite allergen, PBMC from severe and non-severe asthmatics modulate expression of selected phospholipase A2, histone acetyltransferases and deacetylases, while increased expression of cPLA2γ characterizes PBMC response from severe asthmatics.

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Cher, Charmian D. N., Arunmozhiarasi Armugam, Ramkumar Lachumanan, Marelyn-Wintour Coghlan, and Kandiah Jeyaseelan. "Pulmonary Inflammation and Edema Induced by Phospholipase A2." Journal of Biological Chemistry 278, no. 33 (May 12, 2003): 31352–60. http://dx.doi.org/10.1074/jbc.m302446200.

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Hasan, S., and C. Liu. "Pyruvate targets cytosolic phospholipase A2 and resolves inflammation." Osteoarthritis and Cartilage 29 (April 2021): S357—S358. http://dx.doi.org/10.1016/j.joca.2021.02.463.

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8

Bonventre, J. V. "Phospholipase A2 and signal transduction." Journal of the American Society of Nephrology 3, no. 2 (August 1992): 128–50. http://dx.doi.org/10.1681/asn.v32128.

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Phospholipases A2 (PLA2) comprise a family of enzymes that hydrolyze the acyl bond at the sn-2 position of phospholipids to generate free fatty acids and lysophospholipids. Different forms of PLA2 are involved in digestion, inflammation, and intercellular and intracellular signal transduction. The sn-2 position of phospholipids in mammalian cells is enriched in arachidonic acid, the precursor of eicosanoids, which have diverse physiologic and pathophysiologic effects on the kidney and other organs. Thus, the regulation of PLA2 activity has important implications for kidney function. PLA2 regulation involves: calcium, pH, protein kinases, GTP-binding proteins, inhibitory and activating proteins, metabolic product inhibition, and transcriptional control. The various roles of arachidonic acid and cyclooxygenase, lipoxygenase, and cytochrome P450 mono-oxygenase products of arachidonic acid metabolism, as intracellular messengers, in the regulation of membrane channel activities, intracellular enzyme activities, cellular calcium homeostasis, mitogenesis, differentiation, cytokine and early response gene expression are discussed.

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Pinto, Florence, Talma Brenner, Phyllis Dan, Miron Krimsky, and Saul Yedgar. "Extracellular phospholipase A2 inhibitors suppress central nervous system inflammation." Glia 44, no. 3 (October 31, 2003): 275–82. http://dx.doi.org/10.1002/glia.10296.

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Goddard, David H., John S. Bomalaski, Stanley Lipper, Robert G. L. Shorr, and Mike A. Clark. "Phospholipase A2-mediated inflammation induces regression of malignant gliomas." Cancer Letters 102, no. 1-2 (April 1996): 1–6. http://dx.doi.org/10.1016/0304-3835(96)04142-0.

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Santoso, Anwar, Teuku Heriansyah, and Mohammad S. Rohman. "Phospholipase A2 is an Inflammatory Predictor in Cardiovascular Diseases: Is there any Spacious Room to Prove the Causation?" Current Cardiology Reviews 16, no. 1 (January 28, 2020): 3–10. http://dx.doi.org/10.2174/1573403x15666190531111932.

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: Lipoprotein-associated phospholipase A2 (Lp-PLA2) is an enzyme family of phospholipase A2 produced by the inflammatory cell in atherosclerotic plaque. It is transported in the circulation, attached mainly to low-density lipoprotein-cholesterol (LDL-C). It hydrolyzes glycerophospholipids particularly fatty acids at the sn-2 position and produces numerous bioactive lipids; and leads to endothelial dysfunction, atherosclerotic plaque inflammation, and development of the necrotic core in plaques. : There are two kinds of phospholipase A2, namely: secretory phospholipase A2 (sPLA2) and Lp- PLA2. They are deemed as evolving predictors of cardiovascular disease (CVD) risk in hospitaland population-based studies, including healthy subjects, acute coronary syndromes (ACS) and patients with CVD. Unfortunately, Lp-PLA2 inhibitor (darapladib) and s-PLA2 inhibitor (varespladib methyl) failed to prove to lower the risk of composite CVD mortality, myocardial infarction and stroke in those with stable CVD and ACS. : Herein, we describe the explanation based on the existing data why there is still a discrepancy among them. So, it highlights the opinion that phospholipase A2 is merely the inflammatory biomarkers of CVD and playing an important role in atherosclerosis. Further, there is more spacious room to prove the causation.

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Sofogianni, Areti, Stelina Alkagiet, and Konstantinos Tziomalos. "Lipoprotein-associated Phospholipase A2 and Coronary Heart Disease." Current Pharmaceutical Design 24, no. 3 (April 13, 2018): 291–96. http://dx.doi.org/10.2174/1381612824666180111110550.

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In the last decades, the role of inflammation in the pathogenesis of atherosclerosis has been the topic of intense research. Several markers of inflammation have shown predictive value for first and recurrent coronary events in patients without and with established Coronary Heart Disease (CHD). Among these markers, lipoprotein- associated phospholipase A2 (Lp-PLA2) has recently received considerable attention. In the present review, the potential role of Lp-PLA2 as a marker of CHD risk and as a therapeutic target is discussed. Elevated Lp- PLA2 mass and activity appears to be associated with increased risk for CHD, both in the general population and in patients with established CHD. However, it is unclear whether the measurement of Lp-PLA2 improves risk discrimination when incorporated in models that include traditional cardiovascular risk factors. Moreover, the lack of effect on CHD events of darapladib, a potent, selective Lp-PLA2 inhibitor, in two large, randomized, placebo-controlled trials and the mostly negative findings of genetic association studies suggest that Lp-PLA2 is unlikely to represent a causal factor in atherogenesis. Therefore, it is doubtful whether Lp-PLA2 will constitute a therapeutic target for the prevention of CHD.

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Wu, Y., D. Leduc, V. Balloy, I. Garcia-Verdugo, M. Chignard, and L. Touqui. "Role of cytosolic phospholipase A2 in Pseudomonas aeruginosa-induced inflammation." Journal of Cystic Fibrosis 8 (June 2009): S52. http://dx.doi.org/10.1016/s1569-1993(09)60208-3.

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Tamaru, Shun, Hideto Mishina, Yosuke Watanabe, Kazuhiro Watanabe, Daisuke Fujioka, Soichiro Takahashi, Koji Suzuki, et al. "Deficiency of Phospholipase A2 Receptor Exacerbates Ovalbumin-Induced Lung Inflammation." Journal of Immunology 191, no. 3 (July 1, 2013): 1021–28. http://dx.doi.org/10.4049/jimmunol.1300738.

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Sato, Hiroyasu, Yoshitaka Taketomi, Yuki Isogai, Seiko Masuda, Tetsuyuki Kobayashi, Kei Yamamoto, and Makoto Murakami. "Group III secreted phospholipase A2 transgenic mice spontaneously develop inflammation." Biochemical Journal 421, no. 1 (June 12, 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 elevated levels of pro-inflammatory cytokines, chemokines and prostaglandin E2. In addition, Pla2g3-Tg mice had increased lymph aggregates and mucus in the airway, lymphocytic sialadenitis, hepatic extramedullary haemopoiesis, splenomegaly with increased populations of granulocytes and monocytes/macrophages, and increased serum IgG1. Collectively, these observations provide the first demonstration of spontaneous development of inflammation in mice with Tg overexpression of mammalian sPLA2.

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Wu, Y., D. Leduc, I. Garcia-Verdugo, V. Balloy, M. Chignard, and L. Touqui. "Role of cytosolic phospholipase A2 in Pseudomonas aeruginosa-induced inflammation." Revue des Maladies Respiratoires 25, no. 9 (November 2008): 1190. http://dx.doi.org/10.1016/s0761-8425(08)75059-9.

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Sudhir, Krishnankutty. "Lipoprotein-associated phospholipase A2, vascular inflammation and cardiovascular risk prediction." Vascular Health and Risk Management 2, no. 2 (April 2006): 153–56. http://dx.doi.org/10.2147/vhrm.2006.2.2.153.

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Hurley, Bryan P., and Beth A. McCormick. "Multiple Roles of Phospholipase A2 during Lung Infection and Inflammation." Infection and Immunity 76, no. 6 (April 14, 2008): 2259–72. http://dx.doi.org/10.1128/iai.00059-08.

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Knuplez, Eva, Eva Maria Sturm, and Gunther Marsche. "Emerging Role of Phospholipase-Derived Cleavage Products in Regulating Eosinophil Activity: Focus on Lysophospholipids, Polyunsaturated Fatty Acids and Eicosanoids." International Journal of Molecular Sciences 22, no. 9 (April 21, 2021): 4356. http://dx.doi.org/10.3390/ijms22094356.

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Eosinophils are important effector cells involved in allergic inflammation. When stimulated, eosinophils release a variety of mediators initiating, propagating, and maintaining local inflammation. Both, the activity and concentration of secreted and cytosolic phospholipases (PLAs) are increased in allergic inflammation, promoting the cleavage of phospholipids and thus the production of reactive lipid mediators. Eosinophils express high levels of secreted phospholipase A2 compared to other leukocytes, indicating their direct involvement in the production of lipid mediators during allergic inflammation. On the other side, eosinophils have also been recognized as crucial mediators with regulatory and homeostatic roles in local immunity and repair. Thus, targeting the complex network of lipid mediators offer a unique opportunity to target the over-activation and ‘pro-inflammatory’ phenotype of eosinophils without compromising the survival and functions of tissue-resident and homeostatic eosinophils. Here we provide a comprehensive overview of the critical role of phospholipase-derived lipid mediators in modulating eosinophil activity in health and disease. We focus on lysophospholipids, polyunsaturated fatty acids, and eicosanoids with exciting new perspectives for future drug development.

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Mayne, Elizabeth S., Hellen Moabi, Diederick E. Grobbee, Roos E. Barth, Kersten Klipstein-Grobusch, Wendy S. Stevens, Alinda G. Vos, and Susan Louw. "The Utility of the Lipoprotein-Associated Phospholipase A2 (Lp-PLA2) Assay in Detecting Abnormalities in Lipid Metabolism and Cardiovascular Risk in an HIV-Infected South African Cohort." Clinical and Applied Thrombosis/Hemostasis 25 (January 1, 2019): 107602961988394. http://dx.doi.org/10.1177/1076029619883944.

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People with HIV (PWH) have an increased prevalence of cardiovascular disease (CVD) compared to uninfected patients. Lipoprotein-associated phospholipase A2 (Lp-PLA2) catalyzes the synthesis of pro-inflammatory lipids that recruit monocytes. Current guidelines for assessing cardiovascular risk in HIV-infected patients suggest that Lp-PLA2 may be a useful surrogate marker for CVD health in this patient population. Lipoprotein-associated phospholipase A2, lipids, glucose, physical parameters, and carotid intimal–medial thickness (CIMT) were measured in 98 participants (49 HIV-uninfected, 27 antiretroviral therapy [ART]-naive PWH, and 22 ART-treated PWH). HIV viral load (VL) and CD4+ T-cell count were measured in HIV-infected participants. Lipoprotein-associated phospholipase A2 was increased in participants on protease inhibitor (PI) ART (median 50.5 vs 127.0 nmol/mL, P = .05) and correlated with age, body mass index, and cholesterol. Lipoprotein-associated phospholipase A2 was not related to Framingham risk score or CIMT but correlated directly with VL ( r = .323, P = .025) and inversely with CD4+ T-cell count ( r = −.727, P < .001). Lipoprotein-associated phospholipase A2 was increased in HIV-infected participants on PIs and correlated strongly with VL and CD4+ T-cell count suggesting that HIV-associated inflammation is linked to increased Lp-PLA2, providing a mechanistic link between HIV and CVD.

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Barnwal, Bhaskar, and R. Manjunatha Kini. "Characterization of inflamin, the first member of a new family of snake venom proteins that induces inflammation." Biochemical Journal 455, no. 2 (September 27, 2013): 239–50. http://dx.doi.org/10.1042/bj20130599.

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Kanagaraj, Jyothi. "Phospholipase A2 (PLA2) Sequences in Rattus norvegicus Genome." International Journal for Research in Applied Science and Engineering Technology 9, no. VI (June 20, 2021): 1388–90. http://dx.doi.org/10.22214/ijraset.2021.34874.

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Phospholipase A2 is enzyme that hydrolyses phospholipids at sn-2 position. This class of enzymes are significant due to their ability to cleave membrane phospholipids and hence causing inflammation. The PLA2 enzymes present in Rattus norvegicus is extensively studied to predict its properties. The Protparam analysis was performed to predict the physical properties like number of amino acids, Theoretical pH, stability index value, aliphatic index value and GRAVY value. The SOPMA analysis predicted its structural properties like the number of alpha-helices and beta-strands. Hence the focus of the present study was to perform a preliminary in silico analysis to identify the PLA2 protein sequences in the genome of Rattus norvegicus.

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Pruzanski, W., and P. Vadas. "Phospholipase A2 — a mediator between proximal and distal effectors of inflammation." Immunology Today 12, no. 5 (January 1991): 143–46. http://dx.doi.org/10.1016/s0167-5699(05)80042-8.

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Miele, Lucio. "New weapons against inflammation: dual inhibitors of phospholipase A2 and transglutaminase." Journal of Clinical Investigation 111, no. 1 (January 1, 2003): 19–21. http://dx.doi.org/10.1172/jci17506.

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Ferguson, Jane F., Christine C. Hinkle, Nehal N. Mehta, Roshanak Bagheri, Stephanie L. DerOhannessian, Rhia Shah, Megan I. Mucksavage, et al. "Translational Studies of Lipoprotein-Associated Phospholipase A2 in Inflammation and Atherosclerosis." Journal of the American College of Cardiology 59, no. 8 (February 2012): 764–72. http://dx.doi.org/10.1016/j.jacc.2011.11.019.

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D, Dayanand C., Vanishree Bambrana, and Sheela Sr. "PHOSPHOLIPASE A 2 , PLASMA ELASTASE ACTIVITY IN PRE- AND POST-PARTUM OF PRE-ECLAMPTIC WOMEN." Asian Journal of Pharmaceutical and Clinical Research 10, no. 1 (January 1, 2016): 317. http://dx.doi.org/10.22159/ajpcr.2017.v10i1.15358.

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ABSTRACTObjective: The objectives of the present study were to evaluate the activity of phospholipase A2, plasma elastase enzymes and to assess relation withan inflammatory marker high sensitive C-reactive protein (hs-CRP) in nonpregnant before and after delivery of normotensive pregnant and preeclampticwomen.Methods: The study population consists of three groups: Nonpregnant (Group 1, n=57), normotensive pregnant (Group 2, n=57), and pre-eclampticwomen (Group 3, n=57). Groups 2 and 3 were followed after delivery within 48 hrs. Phospholipase A, plasma elastase, and hs-CRP levels weredetermined spectrophotometrically.Results: The plasma elastase, phospholipase A22 activity, and hs-CRP were elevated in pre-eclampsia significantly (p<0.05), nonsignificant rise innormotensive pregnant before delivery condition compared to nonpregnant women. However, plasma elastase in normal pregnancy and pre-eclampsiawere decreased by 1.2- and 2.07-fold, respectively, after delivery. Whereas phospholipase A and hs-CRP found to be nonsignificantly decreased in thepostdelivery status of the both the groups. Receiver operating characteristics curve analysis showed that elastase enzyme has diagnostic importanceto assess inflammation on the basis of area under curve (0.758).2Conclusion: Our research findings generated knowledge about raised level of plasma elastase enzyme by neutrophil degranulation representsinflammation in pre-eclampsia. Elevated elastase, phospholipase AKeywords: Elastase, High sensitive C - reactive protein, Phospholipase A2 with hs-CRP in pre-eclampsia serves as indicators of inflammation., Pre-eclampsia.

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Thiele, Jan R., Jonathon Habersberger, David Braig, Yvonne Schmidt, Kurt Goerendt, Valentin Maurer, Holger Bannasch, et al. "Dissociation of Pentameric to Monomeric C-Reactive Protein Localizes and Aggravates Inflammation." Circulation 130, no. 1 (July 2014): 35–50. http://dx.doi.org/10.1161/circulationaha.113.007124.

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Background— The relevance of the dissociation of circulating pentameric C-reactive protein (pCRP) to its monomeric subunits (mCRP) is poorly understood. We investigated the role of conformational C-reactive protein changes in vivo. Methods and Results— We identified mCRP in inflamed human striated muscle, human atherosclerotic plaque, and infarcted myocardium (rat and human) and its colocalization with inflammatory cells, which suggests a general causal role of mCRP in inflammation. This was confirmed in rat intravital microscopy of lipopolysaccharide-induced cremasteric muscle inflammation. Intravenous pCRP administration significantly enhanced leukocyte rolling, adhesion, and transmigration via localized dissociation to mCRP in inflamed but not noninflamed cremaster muscle. This was confirmed in a rat model of myocardial infarction. Mechanistically, this process was dependent on exposure of lysophosphatidylcholine on activated cell membranes, which is generated after phospholipase A2 activation. These membrane changes could be visualized intravitally on endothelial cells, as could the colocalized mCRP generation. Blocking of phospholipase A2 abrogated C-reactive protein dissociation and thereby blunted the proinflammatory effects of C-reactive protein. Identifying the dissociation process as a therapeutic target, we stabilized pCRP using 1,6-bis(phosphocholine)-hexane, which prevented dissociation in vitro and in vivo and consequently inhibited the generation and proinflammatory activity of mCRP; notably, it also inhibited mCRP deposition and inflammation in rat myocardial infarction. Conclusions— These results provide in vivo evidence for a novel mechanism that localizes and aggravates inflammation via phospholipase A2–dependent dissociation of circulating pCRP to mCRP. mCRP is proposed as a pathogenic factor in atherosclerosis and myocardial infarction. Most importantly, the inhibition of pCRP dissociation represents a promising, novel anti-inflammatory therapeutic strategy.

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Rosenson, Robert S., and Diana M. Stafforini. "Modulation of oxidative stress, inflammation, and atherosclerosis by lipoprotein-associated phospholipase A2." Journal of Lipid Research 53, no. 9 (June 4, 2012): 1767–82. http://dx.doi.org/10.1194/jlr.r024190.

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Krimsky, M., S. Yedgar, L. Aptekar, O. Schwob, G. Goshen, A. Gruzman, S. Sasson, and M. Ligumsky. "Amelioration of TNBS-induced colon inflammation in rats by phospholipase A2 inhibitor." American Journal of Physiology-Gastrointestinal and Liver Physiology 285, no. 3 (September 2003): G586—G592. http://dx.doi.org/10.1152/ajpgi.00463.2002.

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The pathophysiology of inflammatory bowel disease (IBD) involves the production of diverse lipid mediators, namely eicosanoids, lysophospholipids, and platelet-activating factor, in which phospholipase A2 (PLA2) is the key enzyme. Accordingly, it has been postulated that control of lipid mediator production by inhibition of PLA2 would be useful for the treatment of IBD. This hypothesis was tested in the present study by examining the therapeutic effect of a novel extracellular PLA2 inhibitor (ExPLI), composed of carboxymethylcellulose-linked phosphatidylethanolamine (CMPE), on trinitrobenzenesulfonic acid-induced colitis. Intraperitoneal administration of CMPE suppressed the colitis as measured by mortality rate, intestinal permeability, plasma PLA2 activity, intestinal myeloperoxidase activity, and histological morphometry. Current therapeutic approaches for inflammatory conditions focus on the selective control of a lipid mediator(s) (e.g., prostaglandins or leukotrienes). The present study supports the concept that inclusive control of lipid mediator production by PLA2 inhibition is a plausible approach to the treatment of colitis and introduces the ExPLIs as a prototype of a novel NSAID for the treatment of intestinal inflammation.

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Munzel, T., and T. Gori. "Lipoprotein-associated phospholipase A2, a marker of vascular inflammation and systemic vulnerability." European Heart Journal 30, no. 23 (August 30, 2009): 2829–31. http://dx.doi.org/10.1093/eurheartj/ehp311.

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Dore, Etienne, and Eric Boilard. "Roles of secreted phospholipase A2 group IIA in inflammation and host defense." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1864, no. 6 (June 2019): 789–802. http://dx.doi.org/10.1016/j.bbalip.2018.08.017.

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Hamaguchi, Katsuhiko, Hiroshi Kuwata, Kumiko Yoshihara, Seiko Masuda, Satoko Shimbara, Sachiko Oh-ishi, Makoto Murakami, and Ichiro Kudo. "Induction of distinct sets of secretory phospholipase A2 in rodents during inflammation." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1635, no. 1 (November 2003): 37–47. http://dx.doi.org/10.1016/j.bbalip.2003.10.004.

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Wei, Yulong, Lesan Yan, Lijun Luo, Tao Gui, Bian Jang, Ahmad Amirshaghaghi, Tianyan You, Andrew Tsourkas, Ling Qin, and Zhiliang Cheng. "Phospholipase A2 inhibitor–loaded micellar nanoparticles attenuate inflammation and mitigate osteoarthritis progression." Science Advances 7, no. 15 (April 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 sPLA2-responsive and nanoparticle (NP)–based interventional platform for OA management, we incorporated an sPLA2 inhibitor (sPLA2i) into the phospholipid membrane of micelles. The engineered sPLA2i-loaded micellar NPs (sPLA2i-NPs) were able to penetrate deep into the cartilage matrix, prolong retention in the joint space, and mitigate OA progression. These findings suggest that sPLA2i-NPs can be promising therapeutic agents for OA treatment.

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Balboa, María A., Rebeca Pérez, and Jesús Balsinde. "Amplification Mechanisms of Inflammation: Paracrine Stimulation of Arachidonic Acid Mobilization by Secreted Phospholipase A2 Is Regulated by Cytosolic Phospholipase A2-Derived Hydroperoxyeicosatetraenoic Acid." Journal of Immunology 171, no. 2 (July 15, 2003): 989–94. http://dx.doi.org/10.4049/jimmunol.171.2.989.

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Miki, Yoshimi, Kei Yamamoto, Yoshitaka Taketomi, Hiroyasu Sato, Kanako Shimo, Tetsuyuki Kobayashi, Yukio Ishikawa, et al. "Lymphoid tissue phospholipase A2 group IID resolves contact hypersensitivity by driving antiinflammatory lipid mediators." Journal of Experimental Medicine 210, no. 6 (May 20, 2013): 1217–34. http://dx.doi.org/10.1084/jem.20121887.

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Resolution of inflammation is an active process that is mediated in part by antiinflammatory lipid mediators. Although phospholipase A2 (PLA2) enzymes have been implicated in the promotion of inflammation through mobilizing lipid mediators, the molecular entity of PLA2 subtypes acting upstream of antiinflammatory lipid mediators remains unknown. Herein, we show that secreted PLA2 group IID (PLA2G2D) is preferentially expressed in CD11c+ dendritic cells (DCs) and macrophages and displays a pro-resolving function. In hapten-induced contact dermatitis, resolution, not propagation, of inflammation was compromised in skin and LNs of PLA2G2D-deficient mice (Pla2g2d−/−), in which the immune balance was shifted toward a proinflammatory state over an antiinflammatory state. Bone marrow-derived DCs from Pla2g2d−/− mice were hyperactivated and elicited skin inflammation after intravenous transfer into mice. Lipidomics analysis revealed that PLA2G2D in the LNs contributed to mobilization of a pool of polyunsaturated fatty acids that could serve as precursors for antiinflammatory/pro-resolving lipid mediators such as resolvin D1 and 15-deoxy-Δ12,14-prostaglandin J2, which reduced Th1 cytokine production and surface MHC class II expression in LN cells or DCs. Altogether, our results highlight PLA2G2D as a “resolving sPLA2” that ameliorates inflammation through mobilizing pro-resolving lipid mediators and points to a potential use of this enzyme for treatment of inflammatory disorders.

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Boeno, Charles Nunes, Mauro Valentino Paloschi, Jéssica Amaral Lopes, Weverson Luciano Pires, Sulamita da Silva Setúbal, Jaína Rodrigues Evangelista, Andreimar Martins Soares, and Juliana Pavan Zuliani. "Inflammasome Activation Induced by a Snake Venom Lys49-Phospholipase A2 Homologue." Toxins 12, no. 1 (December 31, 2019): 22. http://dx.doi.org/10.3390/toxins12010022.

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Background: Snake venom phospholipases A2 (PLA2s) have hemolytic, anticoagulant, myotoxic, oedematogenic, bactericidal, and inflammatory actions. BthTX-I, a Lys49-PLA2 isolated from Bothrops jararacussu venom, is an example of Lys49-PLA2 that presents such actions. NLRP3 is a cytosolic receptor from the NLR family responsible for inflammasome activation via caspase-1 activation and IL-1β liberation. The study of NLRs that recognize tissue damage and activate the inflammasome is relevant in envenomation. Methods: Male mice (18–20 g) received an intramuscular injection of BthTX-I or sterile saline. The serum was collected for creatine-kinase (CK), lactate dehydrogenase (LDH), and interleukin-1β (IL-1β) assays, and muscle was removed for inflammasome activation immunoblotting and qRT-PCR expression for nucleotide and oligomerization domain, leucine-rich repeat-containing protein family, pyrin-containing domain 3 receptor (NLRP3) inflammasome components. Results: BthTX-I-induced inflammation and myonecrosis, shown by intravital microscope, and LDH and CK release, respectively. Mouse treatment with A438079, a P2X7 receptor antagonist, did not modify these effects. BthTX-I induced inflammasome activation in muscle, but P2X7R participation in this effect was not observed. Conclusion: Together, the results showed for the first time that BthTX-I in gastrocnemius muscle induces inflammation and consequently, inflammasome activation via NLRP3 with caspase-1 activation and IL-1β liberation.

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Homaidan, Fadia R., Liming Zhao, Iman Chakroun, Carla A. Martin, and Robert Burakoff. "The Mechanisms of Action of Interleukin-1 on Rabbit Intestinal Epithelial Cells." Mediators of Inflammation 8, no. 4-5 (1999): 189–97. http://dx.doi.org/10.1080/09629359990342.

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Interleukin-1 (IL-1) is an inflammatory mediator that increases Cl-secretion in intestinal epithelial cells. To identify the signal transduction pathway(s) involved in IL-1's action, cells were treated with IL-1 and the levels of cyclooxygenase (COX) enzymes, prostaglandin E2(PGE2) and phospholipase A2-activating protein (PLAP), and the activity of phospholipase A2(PLA2) were measured. IL-1 caused concentrationand time-dependent increases in the levels of PLA2activity, and/or in the levels of PLAP, COX-2 and PGE2. The IL-induced increase in PGE2levels was biphasic, with the first peak due to the increase in PLAP levels, and the second peak due to the increase in COX-2 levels. This increase in PGE2levels may provide a mechanism for acute and chronic inflammation in the intestine.

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Tian, G., and G. Xig. "P73 RELATIONSHIP BETWEEN LIPOPROTEIN-ASSOCIATED PHOSPHOLIPASE A2 AND INFLAMMATION IN CORONARY HEART DISEASES." Atherosclerosis Supplements 11, no. 2 (June 2010): 31–32. http://dx.doi.org/10.1016/s1567-5688(10)70140-9.

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Sawada, Kanako, Miki Hiraoka, Akira Abe, Robert Kelly, James A. Shayman, and Hiroshi Ohguro. "Prolonged Ocular Inflammation in Endotoxin-Induced Uveitis in Lysosomal Phospholipase A2-Deficient Mice." Current Eye Research 42, no. 4 (September 9, 2016): 611–16. http://dx.doi.org/10.1080/02713683.2016.1214967.

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Scott, Kieran F., Katherine J. Bryant, and Matthew J. Bidgood. "Functional coupling and differential regulation of the Phospholipase A2 -cyclooxygenase pathways in inflammation." Journal of Leukocyte Biology 66, no. 4 (October 1999): 535–41. http://dx.doi.org/10.1002/jlb.66.4.535.

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Malaviya, Ravi, Justin Ansell, LeRoy Hall, Mila Fahmy, Rochelle L. Argentieri, Gilbert C. Olini, David W. Pereira, Runa Sur, and Druie Cavender. "Targeting cytosolic phospholipase A2 by arachidonyl trifluoromethyl ketone prevents chronic inflammation in mice." European Journal of Pharmacology 539, no. 3 (June 2006): 195–204. http://dx.doi.org/10.1016/j.ejphar.2006.03.018.

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Duchez, Anne-Claire, Luc H. Boudreau, Gajendra S. Naika, Matthieu Rousseau, Nathalie Cloutier, Tania Levesque, Michael H. Gelb, and Eric Boilard. "Respective contribution of cytosolic phospholipase A2α and secreted phospholipase A2 IIA to inflammation and eicosanoid production in arthritis." Prostaglandins & Other Lipid Mediators 143 (August 2019): 106340. http://dx.doi.org/10.1016/j.prostaglandins.2019.106340.

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Singh, Pushpendra, Mohammad Yasir, Ruchi Khare, and Rahul Shrivastava. "Green synthesis of silver nanoparticles using Indian male fern (Dryopteris Cochleata), operational parameters, characterization and bioactivity on Naja naja venom neutralization." Toxicology Research 9, no. 5 (September 2020): 706–13. http://dx.doi.org/10.1093/toxres/tfaa070.

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Abstract Snakebite is considered as one of the acute severe medical problems across the world. Snake venoms composed of various group of toxins, enzymes and non-toxic enzymes. Phospholipases A2 present in Naja naja snake venom plays a significant role in lipid signalling and contributes to different inflammation in the human body. Dryopteris cochleata rhizomes have antioxidant, antimicrobial property and used to treat lesions, gonorrhoea, sores, muscular pain, rheumatic and also useful in dog and snake bites. In this study, Indian male fern D. cochleata rhizomes have been used for green synthesis of silver nanoparticles with the aim to increase the bioactivity of plant extract and to evaluate N. naja snake venom inhibition activity of prepared nanoparticles. Green synthesized nanoparticles were characterized with the help of ultraviolet–visible spectroscopy, Fourier-transform infrared spectroscopy, X-ray powder diffraction and atomic force microscopy. Naja naja venom inhibition activity of nanoparticles was performed using in vitro phospholipases A2 assay and tissue damage activity. The results showed that surface plasmon resonance maxima peaks of nanoparticles were observed at 424 nm. Average particle size was around 35 nm, with a spherical shape. Neutralization results exhibited that synthesized silver nanoparticles from D. cochleata decreased percentage of tissue damage, resulting in significant inhibition of phospholipase A2 and N. naja snake venom. Results concluded that green synthesized silver nanoparticles from D. cochleata rhizome neutralize N. naja snake venom activity.

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RIBARDO, D., S. CROWE, J. PETERSON, and A. CHOPRA. "Phospholipase C, phospholipase D and phospholipase A2 (PLA2)-activating protein (PLAA) as new targets to control inflammation in inflammatory bowel disease (IBD)." Gastroenterology 120, no. 5 (April 2001): A185—A186. http://dx.doi.org/10.1016/s0016-5085(01)80919-7.

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Ribardo, Deborah A., Sheila E. Crowe, Johnny W. Peterson, and Ashok K. Chopra. "Phospholipase C, phospholipase D and phospholipase A2 (PLA2)-activating protein (PLAA) as new targets to control inflammation in inflammatory bowel disease (IBD)." Gastroenterology 120, no. 5 (April 2001): A185—A186. http://dx.doi.org/10.1016/s0016-5085(08)80919-5.

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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 metabolism of arachidonic acid, the iPLA2 family to membrane homeostasis and energy metabolism, and the sPLA2 family to various biological processes. The focus of this review is on recent research developments in the sPLA2 field. sPLA2s are secreted enzymes with low molecular weight (with the exception of GIII sPLA2), Ca2+-requiring enzymes with a His-Asp catalytic dyad. Ten enzymatically active sPLA2s and one devoid of enzymatic activity have been identified in mammals. Some of these sPLA2s are potent in arachidonic acid release from cellular phospholipids for the biosynthesis of eicosanoids, especially during inflammation. Individual sPLA2 enzymes exhibit unique tissue and cellular localizations and specific enzymatic properties, suggesting their distinct biological roles. Recent studies indicate that sPLA2s are involved in diverse pathophysiological functions and for most part act nonredundantly.

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Kim, D. K., and J. V. Bonventre. "Purification of a 100 kDa phospholipase A2 from spleen, lung and kidney: antiserum raised to pig spleen phospholipase A2 recognizes a similar form in bovine lung, kidney and platelets, and immunoprecipitates phospholipase A2 activity." Biochemical Journal 294, no. 1 (August 15, 1993): 261–70. http://dx.doi.org/10.1042/bj2940261.

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Phospholipase A2 (PLA2) plays a key role in the production of intracellular and extracellular chemical mediators such as arachidonic acid, eicosanoids and platelet-activating factor, which modulate membrane channel activity, signal transduction, are vasoactive and chemotactic, and are implicated in many pathophysiological mechanisms of inflammation and tissue injury. We previously identified, purified and characterized an arachidonic acid-selective cytosolic 100-110 kDa PLA2 from bovine platelets and rat kidney that is activated during cell stimulation. The purification schemes previously published resulted in low yields of enzyme, insufficient for extensive biochemical characterization. We report the purification of a large-molecular-mass (100 kDa) PLA2 from pig spleen, bovine kidney and bovine lung, using a novel large-scale purification scheme. The enzyme was purified to near homogeneity from an acidified extract obtained from 4.8 kg of pig spleen by sequential use of DEAE-cellulose anionic exchange, Butyl-Toyopearl hydrophobic chromatography and DEAE-5PW h.p.l.c., and further purified by non-denaturing PAGE. This purification scheme will permit the preparation of quantities of purified native enzyme sufficient to study its properties and regulation. To generate antiserum against the PLA2 enzyme, the 100 kDa protein was excised and electroeluted from SDS/PAGE gels of the active fractions after DEAE-5PW h.p.l.c., and this was used as antigen. This polyclonal antibody against pig spleen 100 kDa PLA2 protein reacted with 100 kDa bands in preparations partially purified from bovine platelets, kidney and lung as well as pig spleen, and immunoprecipitated PLA2 activity from these sources. The antibody also immunoprecipitated a 100 kDa protein from cytosolic fractions of cultured renal mesangial cells, human erythroleukaemia cells and human monocytic U937 cells. Considerable PLA2 activity was present in the immunoprecipitates. To our knowledge this antibody is unique in its ability to permit measurement of PLA2 activity in the immunoprecipitate itself, and will be a useful tool for the study of the regulation and the activation mechanisms of the native PLA2 enzyme.

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Nevalainen, Timo J., V. Jukka O. Laine, and David S. Grass. "Expression of Human Group II Phospholipase A2 in Transgenic Mice." Journal of Histochemistry & Cytochemistry 45, no. 8 (August 1997): 1109–19. http://dx.doi.org/10.1177/002215549704500808.

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Group II phospholipase A2 (PLA2) has been proposed to play an important role in inflammation and defense against bacterial infection. We investigated tissues of transgenic mice expressing the human group II PLA2 gene by immunohistochemistry using rabbit anti-human group II PLA2 antibodies, and by in situ hybridization by probing with human group II PLA2 mRNA anti-sense (test) and sense (control) riboprobes. By immunohis-tochemistry, human group II PLA2 was found in various mouse tissues and cell types including hepatocytes, proximal tubule cells of the kidney, epithelial cells of the renal pelvis, urinary bladder and ureter, granulosa cells of Graafian follicles, aortic intima and media, cartilage, epiphyseal bone, bronchial epithelial cells, and connective tissue cells in the dermis. By in situ hybridization, group II PLA2 mRNA was localized in hepatocytes, epidermal cells, dermal cells, connective tissue fibroblasts, epithelial and smooth muscle cells of the urinary bladder, and cells of Bowman's capsule. These results show that human group II PLA2 is expressed in large amounts in hepatocytes and many extrahepatic tissues of the transgenic mice. These animals provide a useful new tool for studies on the metabolism, in vivo effects, and physiological and pathological roles of phospholipase A2. (J Histochem Cytochem 45:1109–1119, 1997)

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Krizaj, Igor. "Roles of Secreted Phospholipases A2 in the Mammalian Immune System." Protein & Peptide Letters 21, no. 12 (November 5, 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, antiviral and antifungal activities. They are also involved in acute inflammation, a protective reaction of the body to infection or injury. The acute inflammation sometimes escapes regulation, becomes chronic and can evolve into a severe pathology. One or more types of sPLA2 are involved in asthma, rheumatoid arthritis, sepsis, atherosclerosis, myocardial infarction, Crohn’s disease, ulcerative colitis and cancer. sPLA2s are thus important therapeutic targets as well as biotherapeutic molecules. Improving the selectivity of inhibitors of sPLA2s to be able to target a particular sPLA2 could therefore be one of the most important tasks for future research.

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SATTAR, Naveed. "Inflammation and endothelial dysfunction: intimate companions in the pathogenesis of vascular disease?" Clinical Science 106, no. 5 (May 1, 2004): 443–45. http://dx.doi.org/10.1042/cs20040019.

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There is increasing evidence to implicate inflammation as an important precursor of endothelial dysfunction. This mechanistic link is apparent across the entire spectrum of inflammatory status, i.e. endothelial function is apparent following acute infection, and in subjects with chronic high-grade inflammation and, perhaps most importantly, persistent low-grade inflammation. The recognition of this relationship has present therapeutic ramifications, but also requires that future longitudinal studies determining the predictive ability of endothelial function measures for vascular events should incorporate markers of inflammation as potential confounders. In this issue of Clinical Science, Fichtlscherer and co-workers describe a link between endothelial function and sPLA2 (secretory non-pancreatic type II phospholipase A2) serum activity.

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Journal articles on the topic 'Inflammation Phospholipase A2'

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