Relevant bibliographies by topics / Inflammation Phospholipase A2

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Academic literature on the topic 'Inflammation Phospholipase A2'

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Published: 4 June 2021
Last updated: 10 February 2022

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Journal articles on the topic "Inflammation Phospholipase A2"

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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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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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Dissertations / Theses on the topic "Inflammation Phospholipase A2"

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Versani, Maheshkumar Premji. "The role of phospholipase A2 in mast cell activation." Thesis, University College London (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.286756.

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Ahamada-Himidi, Azali. "Inhibiteurs de la phospholipase A₂ de groupe IIA : étude pharmacotoxicologique." Paris 7, 2003. http://www.theses.fr/2003PA077004.

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Pour obtenir de nouveaux antiinflammatoires dépourvus d'effets secondaires, nous développons des inhibiteurs spécifiques de la sPLA₂-II, enzyme impliquée dans l'inflammation en amont des COX. Nous avons montré, in vitro, que les molécules synthétisées, comme le PMS 1062 (leader), inhibent spécifiquement l'activité des sPLA₂-II, -V, et -X et qu'ils sont peu cytotoxiques. Dans diverses cellules stimulées par le LPS(ou LPS+cytokines), le PMS 1062 inhibe la production du NO, de PGE₂, de TNF-α et d'II-6 ainsi que l'activation du NF-кB, mais reste sans effet sur les activités COX₂ et COX₁. En outre, le PMS 1062 abolit la production de H₂O₂, la chute du potentiel transmembranaire et la déplétion en glutathion induites par le LPS ainsi que la formation de MDA induite par le fer/ascorbate. Ces résultats attestent que le PMS 1062 possède une activité antiinflammatoire importante liée, d'une part, à l'inhibition des activités sPLA₂-II et NOSi via NF-кB, et d'autre part, à son pouvoir antioxydant.
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Sommerfelt, Randi Magnus. "Molecular mechanisms of inflammation – a central role for cytosolic phospholipase A2." Doctoral thesis, Norges teknisk-naturvitenskapelige universitet, Institutt for biologi, 2014. http://urn.kb.se/resolve?urn=urn:nbn:no:ntnu:diva-25435.

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cPLA2α – a central regulator of inflammation Bioactive lipids are central in regulating the inflammatory process and imbalance in lipid mediator signaling contributes to progression of pathological conditions such as atherosclerosis, allergy, autoimmunity, degenerative diseases and cancer. Phospholipase A2 (PLA2) enzymes release fatty acids such as arachidonic acid (AA) and a lysophospholipid from cellular membranes. Lysophospholipids can me metabolized to biologically active lipid mediators including platelet-activating factor (PAF). PAF is a potent mediator of inflammation, but can also exert a range of other physiological and pathophysiological processes including apoptosis, proliferation and cancer development. AA is a precursor of many bioactive lipid including prostaglandins such as prostaglandin E2 (PGE2), a potent immunoregulator and inducer of inflammation, fever and pain. In particular cytosolic phosholipase A2 (cPLA2α) is associated with inflammation and inflammatory disease as a main enzyme mediating AA release and proinflammatory eicosanoid production, and is proposed as a future therapeutic target. However, lipid signaling is complex and sophisticatedly regulated, and the downstream consequences of cPLA2α inhibition are not fully understood. The overall objective of this thesis was to investigate the role of PLA2 enzymes, in particular cPLA2α, and downstream lipid messengers in cellular signaling mechanisms involved in chronic inflammatory disease. In Paper I, we investigated the role of PAF in differentiated keratinocytes, a cellular model system for psoriatic skin. We found that PAF did not primarily induce pro-inflammatory signaling, but rather proliferative responses possibly linking the inflammatory response to re-epithelialization and wound-healing. In the second part of this thesis comprising Papers II-IV, we focused on the role of cPLA2α in regulating pro-inflammatory signaling pathways central in the pathogenesis of rheumatoid arthritis (RA). In Paper II, we found cPLA2α to regulate joint-destructive and pro-inflammatory effectors induced by tumor necrosis factor (TNF), a “master” cytokine in RA. In Papers III and IV, we investigated the role of cPLA2α in modulating TLR-induced signaling. TLRs constitute a central part in the innate immune system sensing invading pathogens and tissue injury. However, TLRs can also induce “sterile” inflammation by recognizing molecules derived from the host itself, and increased TLR activation is believed to contribute to the pathogenesis of a range of inflammatory and autoimmune diseases including RA. We found that cPLA2α regulates TLR-induced activation of the transcription factor NF-κB and expression of several pro-inflammatory mediators. We furthermore identified PGE2 and possibly other related prostanoids as actors in this mechanism. Taken together, our findings expand the understanding of cPLA2α as a central regulator of molecular mechanisms in chronic inflammation, and enlighten the potential role of cPLA2α and PAF in linking the inflammatory and proliferatory processes
cPLA2α - en sentral regulator i kronisk inflammasjon Lipider spiller en viktig rolle som signalmolekyler i inflammatoriske sykdommer som aterosklerose (hjerte- og karsykdom), revmatoid artritt, psoriasis, multiple sklerose og også i kreft. I dette forskningsprosjektet har vi undersøkt rollen til et enzym, cPLA2α og ulike lipider i molekylære mekanismer i kronisk inflammasjon, med tanke på utvikling av framtidige medisiner mot kronisk inflammatoriske sykdommer. PLA2-enzymer klipper løs fettsyrer fra fosfolipider i cellemembranen, og regulerer dermed produksjonen av en rekke ulike bioaktive lipider som platelet-activating factor (PAF) og prostaglandin E2 (PGE2). Både PAF og PGE2 er kjent som potente pro-inflammatoriske signalmolekyler, med de er også involvert i en rekke andre prosesser. I Del I av prosjektet undersøkte vi rollen til PAF i hudceller, som modellsystem for psoriasis. Vi fant at PAF primært induserte proliferasjon og migrasjon, og ikke inflammasjon. Dette kan bety at PAF i hud produseres som et signal som forbinder den inflammatoriske prosessen og sårheling, og kan potensielt også være involvert i patologisk hyperproliferasjon, som hudkreft. I Del II undersøkte vi hvordan cPLA2α regulerer inflammatorisk signalisering i leddhinneceller, som et modellsystem for revmatoid artritt. Vi fant at cPLA2α regulerer genuttrykk og produksjon proteiner og lipider relatert til inflammasjon, dannelsen av nye blodårer og ledd-destruksjon. Ved å hemme cPLA2α ble disse faktorene redusert, noe som kan være gunstig med tanke på sykdomshemmende effekt. Sett i sammenheng viser våre resultater at cPLA2α og lipider dannet nedstrøms dens aktivitet regulerer viktige prosesser i kronisk inflammasjon, prosesser som også er relatert til kreft. Molekyler som hemmer cPLA2α eller PAF-signalisering kan dermed representere nye medisiner mot kronisk inflammatoriske sykdommer som revmatoid artritt og psoriasis, og potensielt også kreft.
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Jensen, Michael D. Sun Grace Y. "Secretory phospholipase A2-IIA in Alzheimer's disease and inflammatory responses in astrocytes." Diss., Columbia, Mo. : University of Missouri-Columbia, 2009. http://hdl.handle.net/10355/6738.

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The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from PDF of title page (University of Missouri--Columbia, viewed on March 25, 2010). Vita. Thesis advisor: Grace Y. Sun. "December 2009" Includes bibliographical references
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Mietla, Jennifer A. "The Group IVA Cytosolic Phospholipase A2/C1P Interaction and Its Role in Eicosanoid Synthesis and Inflammation." VCU Scholars Compass, 2014. http://scholarscompass.vcu.edu/etd/579.

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In the presented study, we demonstrate that the interaction of group IVA cytosolic phospholipase A2 and ceramide-1-phosphate is crucial for production of eicosanoid synthesis in inflammation. Inflammation is a critical component of many disease states including anaphylaxis, cancer, cardiovascular disease, rheumatoid arthritis, diabetes and asthma. Eicosanoids are well established mediators of inflammation, and the initial rate limiting step in the production of eicosanoids is the liberation of arachidonic acid (AA) from membrane phospholipids by a phospholipase A2 (PLA2). The major phospholipase involved in this liberation of AA during the inflammatory response is group IVA cytosolic phospholipase A2 (cPLA2α). Previous studies from our laboratory demonstrated that the bioactive sphingolipid, ceramide-1-phosphate (C1P), binds cPLA2α at a three amino acid sequence, which is located in the cationic β-groove of the C2 domain of cPLA2α. In this study we examined the effects of the genetic ablation of ceramide kinase (CERK) on eicosanoid synthesis, as CERK is the only known enzyme to produce C1P in mammalian systems. We utilized primary mouse fibroblasts (MEFs) and macrophages isolated from CERK-/- and +/+ mice. The ceramide-1-phosphate and eicosanoid profiles were investigated, and both ceramide-1-phosphate and eicosanoid levels in CERK-/- MEFs were found to be dysregulated. This study also presents the development of a global eicosanoid method to analyze eicosanoids via LC-ESI-MS/MS. Using this new analysis method, we demonstrated that there are significant differences in eicosanoid levels in ex vivo CERK-/- cells when compared to wild type counterparts, but the effect of the genetic ablation of CERK on eicosanoid synthesis and the serum levels of C1P was not apparent in vivo.
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Pernas, Pierre. "Contribution à l'étude des propriétés enzymatiques et des fonctions cellulaires de la phospholipase A2." Compiègne, 1992. http://www.theses.fr/1992COMPD483.

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Le travail présenté décrit certains aspects du fonctionnement de la phospholipase A2 (PLA2), enzyme clé du métabolisme de l'acide arachidonique, et donc de la libération des médiateurs lipidiques. Nous avons d'abord montré (BBRC, 1990, 168: 644) que la PLA2 peut catalyser la synthèse de phospholipides en milieu non aqueux. Cela indique que les conditions physico-chimiques du micro-environnement de l'enzyme peuvent participer à sa régulation. La PLA2 ne peut cependant pas catalyser de réaction de transacylation dans les conditions utilisées. Nous avons ensuite cloné la partie codante du gène d'une PLA2 secrétée non digestive à partir de placenta humain (BBRC, 1991, 178: 1298). Ce gène est identique à celui isolé à partir de tissus inflammatoires. La surexpression de ce gène par transfection dans des cellules eucaryotes y entraîne une augmentation de la libération stimulée d'acide arachidonique. La PLA2 clonée peut donc interférer avec les mécanismes intracellulaires de transduction du signal. Enfin, nous proposons d'évaluer un mécanisme de régulation traductionnelle de l'adressage de la PLA2 pour rendre compte de sa présence dans la cellule.
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Gora, Sarah. "Implication de la phospholipase A2 de groupe X dans la phase inflammatoire de l’athérosclérose." Paris 6, 2009. http://www.theses.fr/2009PA066053.

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L'athérosclérose est caractérisée par l'accumulation de lipides et la formation de cellules spumeuses par absorption de lipoprotéines de faible densité (LDL) modifiées dans la paroi vasculaire. La phospholipase A2 humaine sécrétée de groupe X (PLA2-GX) a la plus grande affinité hydrolytique pour la phosphatidylcholine. Notre équipe a montré qu’elle est exprimée dans les lésions humaines d’athérosclérose et que l’hydrolyse des LDL par PLA2-GX, (LDL-X) induit la formation de particules proathérogenes. Nous avons montré que la PLA2-GX hydrolyse efficacement le Platelet-Activating-Factor (PAF), un puissant médiateur proinflammatoire. Ces résultats suggèrent que le PAF peut être un substrat pour cette enzyme dans des conditions physiologiques ou physiopathologiques. Afin de déterminer si la PLA2-GX joue un rôle étiologique dans l’athérosclérose, nous avons genotypé des polymorphismes de la PLA2-GX dans l’étude cardiovasculaire ATHEROGENE. Nos résultats montrent qu’un polymorphisme est lié avec les événements cardiovasculaires et nous montrons qu’un polymorphisme non synonyme, est responsable d’une forte diminution de l’expression et de l’activité de PLA2-GX. De plus, l’analyse transcriptomique (microarray) de cellules endothéliales en présence de LDL-X montre la régulation d’un nombre important de gènes impliqués dans l’inflammation. D’autre part, les LDL-X ont un effet important sur la réponse calcique des cellules et l’expression de gènes cibles de la voie UPR (Unfolded Protein Response). L’ensemble de ces résultats contribue à mieux définir le rôle de la PLA2-GX dans la phase inflammatoire de l’athérosclérose et identifie de nouvelles cibles moléculaires.
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Heleno, Mauricio Aurelio Gomes 1962. "Estudo das ações neurotóxica, miotóxica e pró-inflamatória da PLA2 BrTX-I, isolada do veneno de Bothrops roedingeri (Jérgon da Costa) : caracterização bioquímica e farmacológica in vivo e ex vivo." [s.n.], 2012. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314682.

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Orientadores: Sergio Marangoni, Luis Alberto Ponce Soto
Tese (doutorado) - Universidade Estadual de Campinas, Instituto de Biologia
Made available in DSpace on 2018-08-21T10:22:36Z (GMT). No. of bitstreams: 1 Heleno_MauricioAurelioGomes_D.pdf: 8695465 bytes, checksum: 8ac64464abefb901cab1d4e5b6b96336 (MD5) Previous issue date: 2012
Resumo: Uma grande variedade de toxinas provenientes de venenos animais tem sido largamente utilizada no estudo de mecanismos de ação e processos fisiológicos, sendo consideradas valiosas ferramentas moleculares. As serpentes peçonhentas expressam no veneno diversas proteínas muito estudadas e utilizadas clinicamente, apresentando diferentes graus de variabilidade inter e intraespecífica em suas composições e nos seus efeitos biológicos. O conhecimento obtido com os estudos destas moléculas tem grande importância clínica na compreensão dos processos fisiopatológicos envolvidos nos envenenamentos ofidicos e também acadêmico-tecnológica, devido à possibilidade do desenvolvimento de novos instrumentos moleculares utilizados na pesquisa e também de novos modelos moleculares para princípios ativos de drogas. Neste trabalho pesquisamos as atividades neurotóxica, miotóxica e inflamatória de uma PLA2 básica, D49, purificada do veneno da serpente Bothrops roedingeri após duas etapas cromatográficas, exclusão molecular em Sephadex G-75 e hidrofobicidade em HPLC de fase reversa em coluna 'mi'-Bondapak C-18. A BrTX-I apresentou massa molecular relativa em tomo de ~14 kDa (SDS-PAGE) e confirmada por espectrometria de massas (ESI-MS), em 14.358,69 Da. A análise da composição de aminoácidos da BrTX-I, revelou que esta é constituída aproximadamente por 120 resíduos aminoacídicos, com alto conteúdo de aminoácidos básicos e hidrofóbicos, resultando em um valor calculado de pI de 8,63. A presença de 14 resíduos de cisteína sugere a formação de sete pontes dissulfeto. A análise estrutural da BrTX-I foi realizada por ESI-MS e as regiões analisadas mostraram semelhança com outras PLA2 miotóxicas isoladas de venenos botrópicos. A BrTX-I apresentou alta atividade PLA2 e um comportamento tipo sigmoidal em baixas concentrações do substrato. Atividade PLA2 ótima da BrTX-I foi em pH 8,0 e temperatura de 37°C. A BrTX-I mostrou-se dependente de Ca2+ (mM) e na sua substituição por zn+2, Mn+2, Mg+2 e Cd+2 a atividade foi reduzida. O estudo da homologia sequencial da BrTX-I mostrou posições extremamente conservadas na molécula. Nas posições 1 e 2 há predominância da sequência de aminoácidos (DL), na posição 4 (Q). Uma das regiões altamente conservadas na sequência de aminoácidos das PLA2 é a alça de ligação ao cálcio, segmento ...YGCYCGXGG. Resíduos formando a alça de ligação ao cálcio e a rede catalítica da BrTX-I mostraram um alto grau de conservação, refletindo na manutenção da atividade. A região relacionada à atividade neurotóxica pré-sináptica (80-11 O) apresentou principalmente resíduos hidrofóbicos. Em preparações ex vivo, o veneno e a BrTX-I causaram rápido bloqueio da neurotransmissão na preparação biventer cervicis de pintainho de modo similar a outras Bothrops, sem alterar significativamente as respostas contraturantes à adição de AChe de KCl (5 e 20 'mi'g/mL), indicando atividade neurotóxica pré-sináptica. Em camundongos, a BrTX-I induziu miotoxicidade local, determinada pelo aumento nos níveis plasmáticos de CK e mostrou efeito pró-inflamatório analisado através da formação do edema de pata e liberação das citocinas IL-1 , IL-6 e TNF-'alfa'. Como BrTX-I produz um efeito inflamatório, a hidrólise de fosfolipídios pode ser relevante na fisiopatología do envenenamento
Abstract: A great variety of animal venom toxins has been widely used in the study of action mechanisms and metabolic processes, thus considered valuable molecular tools. Poisonous snakes contains in their venom several well studied and clinically used proteins, showing these venoms different intra or interspecific variability degrees in their composition and biological effects. The knowledge obtained with these molecules study, has a great clinical relevancy understanding pathophysiological process regarding snake envenomations, and also academic technological, due to the possibility to develop new molecular tools and new molecular models to study active principies of some drugs. ln this work, we study neurotoxic, myotoxic and inflammatory activities of BrTX-I, a basic PLA2, purified from Bothrops roendigeri snake venom after two chromatographic steps, using molecular exclusion chromatography (Sephadex G-75) and reverse phase HPLC on 'mi'-Bondapak C-18 column. BrTX-I showed relative molecular mass around 14 kDa (PAGE) and specific molecular mass of 14,358.69 Da was determined by ESl-MS mass spectrometry. The amino acid composition analysis showed that BrTX-I contains 120 aminoacidic residues with high content of basic and hydrophobic amino acids, resulting in a calculated pi value of 8. 63. The presence of 14 Cysteine residues, suggests the formation of seven dissulfide bonds. Structural analysis of BrTX-I PLA2, performed by ESI-MS showed high identity values when compared to other myotoxic PLA2, isolated from Bothrops snakes venoms. BrTX-I presented high PLA2 activity and showed a sigmoidal behavior at low substrate concentrations. The BrTX-I reached its maximal PLA2 activity at pH 8.0 and 37 °C. Maximum PLA2 activity required Ca2+ (mM) and substitution of Ca2+ by zn+2, Mn+2, Mg+2 or Cd+2 showed reduced enzymatic activity. Sequence homology studies of BrTX-I showed extremely conserved positions in the molecule. ln positions 1 and 2, there is a predominance of the amino acids sequence (DL), and in position 4 (Q). One of the highly conserved regions in the amino acid sequences of PLA2 is the Ca2+ -binding loop, segment ... YGCYCGXGG. Residues forming the Ca2+-binding loop and the catalytic network of BrTX-I PLA2 showed a high conservation grade, reflecting the non-decreased catalytic activity. The region related to the presynaptic neurotoxic activity (80-110), showed mainly the presence of hydrophobic residues. ln ex vivo studies, the whole venom and BrTX-I caused a fast blockade of the neuromuscular transmission in young chick biventer cervicis preparations m a similar way to other Bothrops species, without alters significantly the contractures induced by ACh and KCL at doses of 5 and 20 'mi'g/mL, respectively, indicating presynaptic neurotoxic activity. ln mice, BrTX-I induced local myotoxicity, determined by increase in CK serum leveis, and showed proinflammatory effects analyzed through edema-forming activity and citokines IL-1 , IL-6, and TNF'alpha' release. Once BrTX-I induces a strong pro-inflammatory effect, the enzymatic phospholipid hydrolysis may be relevant for envenomation pathophysiology
Doutorado
Bioquimica
Doutor em Biologia Funcional e Molecular
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Plocki, Stéphanie. "Synthèse et étude des relations structure-activité d'inhibiteurs spécifiques de la phospholipase A2 de groupe II : modélisation moléculaire." Paris 5, 2002. http://www.theses.fr/2002PA05P607.

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L'inflammation joue un rôle prépondérant dans bon nombre de pathologies. Elle débute par la libération d'Acide Arachidonique grâce à une enzyme appelée la Phospholipase A2. Cet acide est alors transformé sous l'action de multiples enzymes en médiateurs inflammatoires très puissants. A ce jour, les seuls médicaments capables d'inhiber la PLA2 sont les glucocorticoi͏̈des comme la cortisone, mais leurs effets indésirables reconnus ont incité la recherche à créer d'autres médicaments : les Anti-infammatoires non stéroi͏̈diens (AINS), inhibant des enzymes en aval de la PLA2 dans la réaction d'inflammation. Non dépourvus d'effets secondaires, les AINS n'ont pas cependant la propriété de bloquer les autres voies importantes de l'inflammation, enparticulier la formation du facteur d'activation des plaquettes (PAF). Basée sur des analogies avec le substrat, notre laboratoire a découvert depuis 1999 une série de molécules capables de bloquer spécifiquement la PLA2. [. . . ]
The inflammatory reaction is a benefic process because of its self-defense property. However it can induce serious complications qualified as inflammatory pathologies. SPLA2-IIA plays a pivotal role in the propagation and amplification of inflammation. In many pathological situations, circulating sPLA2-IIA level correlates with the severity and illness outcome. Human non pancreatic secretory PLA2 (hnps-PLA2) of group II is associated with pathologies as acute pancreatitis, rhumatisms, septic shock. . . But until now, its role is not completely clarified [. . . ]
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MacKnight, Patrick. "The interaction between ceramide-1-phosphate and Group IVA cytosolic phospholipase A2 and its role in wound healing." VCU Scholars Compass, 2018. https://scholarscompass.vcu.edu/etd/5633.

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The sphingolipid, ceramide-1-phosphate (C1P), directly binds and activates Group IVA cytosolic phospholipase A2 (cPLA2a) to generate eicosanoids. Due to the role of eicosanoids in wound healing, we choose to use our novel genetic mouse model expressing cPLA2a with an ablated C1P interaction site (KI) to examine the cPLA2a/C1P interaction in wound healing. Wound closure rate was not affected, but wound maturation was dramatically enhanced by loss of the C1P/cPLA2α interaction based on the following findings. Wounds in KI mice displayed: i) increased infiltration of dermal fibroblasts into the wound environment; ii) increased wound tensile strength; and iii) higher Type I/Type III collagen ratios. These findings were recapitulated in vitro as primary dermal fibroblasts (pDFs) from KI mice showed significantly increased collagen deposition and migration velocity compared to WT and KO pDFs. Additionally, the KI showed an altered eicosanoid profile of reduced pro-inflammatory prostaglandins (e.g., PGE2) and increased levels of specific HETE species (e.g., 5-HETE). Elevated 5-HETE levels promoted increased dermal fibroblast migration and collagen deposition. This “gain of function” role for the mutant cPLA2a was also linked to differential cellular localization of cPLA2α and 5-HETE biosynthetic factors. These studies demonstrate regulation of key in vivo biological mechanisms by a defined protein:lipid interaction and provide new insights into cPLA2a function.
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Books on the topic "Inflammation Phospholipase A2"

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Symposium on Phospholipase A₂: Pathophysiological Role of Soluble and Membrane-Bound Enzymes (1989 New York, N.Y.). Phospholipase A₂: Role and function in inflammation. New York: Plenum Press, 1990.

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B, Glaser Keith, and Vadas P. 1953-, eds. Phospholipase A2 in clinical inflammation: Moleculaar approaches to pathophysiology. Boca Raton: CRC Press, 1995.

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(Editor), Patrick Y.-K. Wong, and Edward A. Dennis (Editor), eds. Phospholipase A2: Role and Function in Inflammation (Advances in Experimental Medicine and Biology). Springer, 1990.

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Glaser, Keith B., and Peter Vadas. Phospholipase A2 in Clinical InflammationMolecular Approaches to Pathophysiology (Handbooks in Pharmacology and Toxicology). CRC, 1995.

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1955-, Büchler Markus, Nevalainen Timo J, and Uhl W, eds. Phospholipase A2: Basic and clinical aspects in inflammatory diseases. Basel: Karger, 1997.

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Book chapters on the topic "Inflammation Phospholipase A2"

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Weiss, Jerrold, and Grace Wright. "Mobilization and Function of Extracellular Phospholipase A2 in Inflammation." In Phospholipase A2, 103–13. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5805-3_6.

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Gans, Kathleen R., Susan R. Lundy, Randine L. Dowling, William M. Mackin, Theresa M. Stevens, and Janet S. Kerr. "Extracellular Phospholipase A2 Activity in Two in Vivo Models of Inflammation." In Phospholipase A2, 155–67. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5805-3_10.

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Vadas, Peter, and Waldemar Pruzanski. "Phospholipase A2 Activation is the Pivotal Step in the Effector Pathway of Inflammation." In Phospholipase A2, 83–101. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5805-3_5.

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Pruzanski, W., and P. Vadas. "Secretory Nonpancreatic Phospholipase A2 (sPLA2) as a Mediator of Inflammation." In Phospholipase A2, 38–42. Basel: KARGER, 1997. http://dx.doi.org/10.1159/000075485.

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Tibes, U., W. V. Scheuer, H. J. Thierse, E. Burgermeister, S. Schramm, W. G. Friebe, and E. Dietz. "Role of Cytosolic PLA2, Secretory PLA2 and Nitric Oxide Synthase in Inflammation." In Phospholipase A2, 153–67. Basel: KARGER, 1997. http://dx.doi.org/10.1159/000075459.

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Barbour, Suzanne E., Salma Al-Darmaki, and Alex D. Manguikian. "Phospholipase A2 and remodeling in inflammatory cells." In Arachidonate Remodeling and Inflammation, 13–36. Basel: Birkhäuser Basel, 2004. http://dx.doi.org/10.1007/978-3-0348-7848-7_2.

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Dennis, Edward A., Florence E. Davidson, and Raymond A. Deems. "Enzymatic Mechanisms and Inhibition of Phospholipase A2." In Cellular and Molecular Aspects of Inflammation, 413–26. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5487-1_21.

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Marion, Chad R., and Alfred N. Fonteh. "Enzymatic and receptor mediated effects of secretory phospholipase A2 on the pathophysiology of inflammatory diseases." In Arachidonate Remodeling and Inflammation, 37–60. Basel: Birkhäuser Basel, 2004. http://dx.doi.org/10.1007/978-3-0348-7848-7_3.

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Balsinde, Jesús, Rebeca Pérez, Yolanda Sáez, and María A. Balboa. "Control of arachidonic acid levels in resting and activated U937 phagocytic cells by Ca2+-independent phospholipase A2." In Arachidonate Remodeling and Inflammation, 61–72. Basel: Birkhäuser Basel, 2004. http://dx.doi.org/10.1007/978-3-0348-7848-7_4.

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Dieter, P. "Regulation of Eicosanoid Formation in Liver Macrophages: Role of Phospholipase A2." In Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation and Radiation Injury, 191–93. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-3520-1_39.

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Conference papers on the topic "Inflammation Phospholipase A2"

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Sekararum, Woro Ayu, Nurfitri Bustamam, Hikmah Muktamiroh, and Harli Amir Mahmudji. "The Correlation between Secretory Phospholipase A2 Type IIA Levels and Mean Platelet Volume among Type 2 Diabetes Mellitus Patients." In The 7th International Conference on Public Health 2020. Masters Program in Public Health, Universitas Sebelas Maret, 2020. http://dx.doi.org/10.26911/the7thicph.01.09.

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Background: Platelet activity plays a role in the occurrence of diabetic angiopathy with an increase in mean platelet volume (MPV) as a marker of platelet activity. Platelet activity is influenced by phospholipase A2 type IIA (sPLA2 type IIA), which is a lipid-mediating enzyme that connects the pathogenesis of Diabetes Mellitus (DM) with complications of diabetic angiopathy. This study aimed to examine the relationship between levels of type IIA sPLA2 and MPV among type II DM patients. Subjects and Method: This was a cross-sectional study. A total of 63 patients with type II DM was selected for this study. The inclusion criteria for the study subjects were type 2 diabetes mellitus patients who did not experience an infectious disease, acute inflammation, trauma, surgery or malignancy, anemia, taking antiplatelet drugs, having abnormal platelet counts, and smoking. The dependent variable was levels of type IIA sPLA2. The independent variable was MPV. The data were obtained from the medical records of Prof. Dr. Soerojo Mental Hospital, Magelang. The data were analyzed using Spearman correlation test. Results: The study showed the median level of sPLA2 type IIA was 3841.50 ng / dL and the average MPV value was 7.36 fl. The results of the Spearman correlation analysis showed that there was no relationship between sPLA2 type IIA and MPV (p = 0.551), but there was a tendency for an increase in type IIA sPLA2 followed by an increase in MPV value (r = 0.077). There was a difference in the average MPV value in the subject group with DM ≤ 10 years and> 10 years (p = 0.009), and it was statistically significant. Conclusion: There is a tendency for an increase in type IIA sPLA2 followed by an increase in the MPV value among type II DM patients. Keywords: type II diabetes melitus, type IIA sPLA2 enzyme, mean platelet volume Correspondence: Woro Ayu Sekararum. Faculty of Medicine, Universitas Pembangunan Nasional ‘Veteran’ Jakarta. Jl, Rumah Sakit Fatmawati, Pondok Labu, South Jakarta, Indonesia. E-mail: woroayu.sekararum@gmail.com. Mobile: 0811975511 DOI: https://doi.org/10.26911/the7thicph.01.09
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Mointire, V. L., A. J. Frangos, G. B. Rhee, G. S. Eskin, and R. E. Hall. "RHEOLOGY AND CELL ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643988.

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The subject of this work is to examine the hypothesis that some sublytic levels of mechanical perturbation of cells can stimulate cell metabolism. As a marker metabolite, we have chosen arachidonic acid. Principal metabolites for platelets include the cyclooxygenase product thromboxane A2(TXA2) and the lipoxygenase product 12-hydroperoxy-eicosatetraenoic acid (12-HPETE). Polymorphonuclear leukocytes (PMNLs) initally produce principally 5-HPETE, somtimes leading to the formation leukotrienes, though many other metabolites of arachidonic acid have been isolated from activated neutrophils. Human umbilical vein endothelial cells utilize arachidonic acid to produce mainly prostaglandin I2(PGI2). All of these metabolites are biologically active and modulate cell function - sometimes in quite contrasting ways. We will show that levels of sublytic mechanical stress exposure can stimulate arachidonic acid metabolism in all three of the cell types mentioned above. The biological implications of this stress/metabolism coupling may be quite far reaching.Human platelets, leukocytes and endothelial cells all appear to be sensitive to mechanical stress induced activation of arachidonic acid metabolism. Sheared PRP exhibited greatly increased synthesis of 12-HETE and surprisingly little thromboxane B2 production. This indicates that shear stress stimulation of platelets may produce quite different arachidonic acid metabolism than that seen with many direct chemical stimuli, such as thrombin or collagen.Our data demonstrate that a substance derived from shear induced platelet activation may activate the C-5 lipoxygenase of human PMNL under stress, leading to the production of LTB4. We hypothesize that this substance maybe 12-HPETE. LTB4 is known to be a very potent chemotactic factor and to induce PMNL aggregation and degranulation. Our studies provide further evidence that lipoxygenase products of one cell type can modulate production of lipoxygenase products in a second cell type, and that shear stress can initiate cell activation. This kind of coupling could have far reaching implications in terms of our understanding of cell/cell interaction in flowing systems, such as acute inflammation, artificial organ implantation and tumor metastasis.The data on PGI2 production by endothelial cells demonstrate that physiological levels of shear stress can dramatically increase arachidonic acid metabolism. Step increases in shear stress lead to a burst in production of PGI2 which decayed to a steady state value in several minutes. This longer term stimulation of prostacyclin production rate increased linearly with shear stress over the range of 0-24 dynes/cm2. In addition, pulsatile flow of physiological frequency and amplitude caused approximately 2.4 times the PGI2 production rate as steady flow with the same mean stress. Although only PGI2 was measured, it is likely that other arachidonic acid metabolites of endothelial cells are also affected by shear stress.The ability of cells to respond to external stimuli involves the transduction of a signal across the plasma membrane. One such external stimulus appears to be fluid shear stress. Steady shear flow induces cell rotation in suspended cells, leading to a periodic membrane loading, with the peak stress proportional to the bulk shear stress. On anchorage-dependent cells, such as endothelial cells, steady shear stress may act by amplifying the natural thermal or Brownian fluttering or rippling of the membrane. There are several possible mechanisms by which shear stress induced membrane perturbation could mimic a hormone/receptor interaction, leading to increased intracellular metabolism. Shear stress may induce increased phospholipase C activity, caused by translocation of the enzyme, increased substrate (arachidonic acid) pool availability to phospholipase C (particularly from that stored in phosphoinositols) due to shear-induced membrane movements or changes in membrane fluidity, direct activation of calcium - activated phospholipase A2 by increased membrane calcium ion permeability, or most probably by a combination of these mechanisms.
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