Relevant bibliographies by topics / PHOSPHOLIPASES A/analysis

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Academic literature on the topic 'PHOSPHOLIPASES A/analysis'

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Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "PHOSPHOLIPASES A/analysis"

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Emiliani, Yuliana, Andrés Sánchez, Marlon Munera, Jorge Sánchez, and Dilia Aparicio. "In silico analysis of cross reactivity among phospholipases from Hymenoptera species." F1000Research 10 (January 5, 2021): 2. http://dx.doi.org/10.12688/f1000research.27089.1.

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Background: Phospholipases are enzymes with the capacity to hydrolyze membrane lipids and have been characterized in several allergenic sources, such as hymenoptera species. However, cross-reactivity among phospholipases allergens are little understood. The objective of this study was to determine potential antigenic regions involved in cross-reactivity among allergens of phospholipases using an in silico approach. Methods: In total, 18 amino acids sequences belonging to phospholipase family derived from species of the order hymenoptera were retrieved from the UniProt database to perform phylogenetic analysis to determine the closest molecular relationship. Multialignment was done to identify conserved regions and matched with antigenic regions predicted by ElliPro server. 3D models were obtained from modeling by homology and were used to locate cross-reactive antigenic regions. Results: Phylogenetic analysis showed that the 18 phospholipases split into four monophyletic clades (named here as A, B, C and D). Phospholipases from A clade shared an amino acid sequences’ identity of 79%. Antigenic patches predicted by Ellipro were located in highly conserved regions, suggesting that they could be involved in cross-reactivity in this group (Ves v 1, Ves a 1 and Ves m 1). Conclusions: At this point, we advanced to the characterization of potential antigenic sites involved in cross-reactivity among phospholipases. Inhibition assays are needed to confirm our finding.
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Emiliani, Yuliana, Andrés Sánchez, Marlon Munera, Jorge Sánchez, and Dilia Aparicio. "In silico analysis of cross reactivity among phospholipases from Hymenoptera species." F1000Research 10 (March 29, 2021): 2. http://dx.doi.org/10.12688/f1000research.27089.2.

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Background: Phospholipases are enzymes with the capacity to hydrolyze membrane lipids and have been characterized in several allergenic sources, such as hymenoptera species. However, cross-reactivity among phospholipases allergens are little understood. The objective of this study was to determine potential antigenic regions involved in cross-reactivity among allergens of phospholipases using an in silico approach. Methods: In total, 18 amino acids sequences belonging to phospholipase family derived from species of the order hymenoptera were retrieved from the UniProt database to perform phylogenetic analysis to determine the closest molecular relationship. Multialignment was done to identify conserved regions and matched with antigenic regions predicted by ElliPro server. 3D models were obtained from modeling by homology and were used to locate cross-reactive antigenic regions. Results: Phylogenetic analysis showed that the 18 phospholipases split into four monophyletic clades (named here as A, B, C and D). Phospholipases from A clade shared an amino acid sequences’ identity of 79%. Antigenic patches predicted by Ellipro were located in highly conserved regions, suggesting that they could be involved in cross-reactivity in this group (Ves v 1, Ves a 1 and Ves m 1). Conclusions: At this point, we advanced to the characterization of potential antigenic sites involved in cross-reactivity among phospholipases. Inhibition assays are needed to confirm our finding.
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Kunze, Donika, Inga Melzer, Désirée Bennett, et al. "Functional analysis of the phospholipase C gene CaPLC1 and two unusual phospholipase C genes, CaPLC2 and CaPLC3, of Candida albicans." Microbiology 151, no. 10 (2005): 3381–94. http://dx.doi.org/10.1099/mic.0.28353-0.

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Phospholipases C are known to be important regulators of cellular processes but may also act as virulence factors of pathogenic microbes. At least three genes in the genome of the human-pathogenic fungus Candida albicans encode phospholipases with conserved phospholipase C (Plc) motifs. None of the deduced protein sequences contain N-terminal signal peptides, suggesting that these phospholipases are not secreted. In contrast to its orthologue in Sacharomyces cerevisiae, CaPLC1 seems to be an essential gene. However, a conditional mutant with reduced transcript levels of CaPLC1 had phenotypes similar to Plc1p-deficient mutants in S. cerevisiae, including reduced growth on media causing increased osmotic stress, on media with a non-glucose carbon source, or at elevated or lower temperatures, suggesting that CaPlc1p, like the Plc1p counterpart in S. cerevisiae, may be involved in multiple cellular processes. Furthermore, phenotypic screening of the heterozygous ΔCaplc1/CaPLC1 mutant showed additional defects in hyphal formation. The loss of CaPLC1 cannot be compensated by two additional PLC genes of C. albicans (CaPLC2 and CaPLC3) encoding two almost identical phospholipases C with no counterpart in S. cerevisiae but containing structural elements found in bacterial phospholipases C. Although the promoter sequences of CaPLC2 and CaPLC3 differed dramatically, the transcriptional pattern of both genes was similar. In contrast to CaPLC1, CaPLC2 and CaPLC3 are not essential. Although Caplc2/3 mutants had reduced abilities to produce hyphae on solid media, these mutants were as virulent as the wild-type in a model of systemic infection. These data suggest that C. albicans contains two different classes of phospholipases C which are involved in cellular processes but which have no specific functions in pathogenicity.
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Rice, K. L., P. G. Duane, G. Mielke, A. A. Sinha, and D. E. Niewoehner. "Calcium ionophores injure alveolar epithelial cells: relation to phospholipase activity." American Journal of Physiology-Lung Cellular and Molecular Physiology 259, no. 6 (1990): L439—L450. http://dx.doi.org/10.1152/ajplung.1990.259.6.l439.

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Phospholipases and certain of their hydrolytic products are toxic to alveolar epithelial cells. Since many intracellular phospholipases are Ca2+ dependent, we postulated that elevating cytosolic Ca2+ with ionophores might cause epithelial injury via phospholipase activation. Isolated perfused hamster lungs exposed to an Ca2+ ionophore A23187 develop functional evidence of severe epithelial injury. Ultrastructural studies show widespread lysis of type I epithelial cells, with only minimal abnormalities in other lung cells, including the microvascular endothelium. Analysis of whole lung lipid extracts reveals a modest elevation in free arachidonic acid but no changes in other putative products of phospholipase activity. Parallel studies were performed in cultured cells of pulmonary origin. As measured by 51Cr release, A23187 causes substantial cytotoxicity in 3-day-old cultures of rat type II alveolar epithelial cells (RAEC) but not in cultured bovine pulmonary artery endothelial cells (BPAEC). RAEC prelabeled with [14C]stearic acid [( 14C]SA) and [3H]arachidonic acid [( 3H]AA) release radiolabeled free fatty acids (FFA) in response to A23187 in a dose- and time-dependent manner that parallels the cytotoxicity index. Analyses of putative phospholipase products in cells radiolabeled with [14C]SA and [3H]AA, with [14C]choline, or with [14C]ethanolamine suggest that liberation of radiolabeled FFA may be due to several phospholipases but with principal activity being exhibited by a phospholipase C having specificity toward phosphatidylcholine and phosphatidylethanolamine. Prelabeled BPAEC release only minimal quantities of FFA in response to A23187 under the same conditions. These studies demonstrate that elevations of intracytoplasmic Ca2+ are capable of severely and selectively damaging alveolar epithelial cells and that the injury is associated with activation of intracellular phospholipases. These findings may have implications in regard to the pathogenesis of acute lung injury in humans.
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Navas, Laura Emilce, Mónica Florin-Christensen, Graciela Beatriz Benintende, Rubén Oreste Zandomeni, and Marcelo Facundo Berretta. "Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities." Journal of Molecular Microbiology and Biotechnology 28, no. 3 (2018): 99–106. http://dx.doi.org/10.1159/000491698.

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Phospholipases are classified in different enzyme families according to the ester bond they cleave within phospholipids. The use of phospholipases in industrial processes has prompted the search for new enzymes with differential properties. A gene encoding a novel phospholipase (PLP_2.9) was identified in the genome of the thermophilic strain <i>Thermus</i> sp. 2.9. The analysis of the primary sequence unveiled a patatin-like domain. The alignment of the amino acid sequence of PLP_2.9 to other bacterial patatin-related proteins showed that the four blocks characteristic of this type of phospholipases and the amino acids representing the catalytic dyad are conserved in this protein. PLP_2.9 was overexpressed in <i>Escherichia coli</i> and the purified enzyme was characterized biochemically. PLP_2.9<i></i> hydrolyzed <i>p</i>-nitrophenyl palmitate at alkaline pH over a wide range of temperatures (55–80°C), showing high thermostability. PLP_2.9 displayed phospholipase A and acyltransferase activities on egg yolk phosphatidylcholine. Due to its high thermostability, PLP_2.9 has potential applications as a catalyst in several industrial processes.
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Karasawa, Tadahiro, Xingmin Wang, Tsuneo Maegawa, et al. "Clostridium sordellii Phospholipase C: Gene Cloning and Comparison of Enzymatic and Biological Activities with Those of Clostridium perfringens and Clostridium bifermentans Phospholipase C." Infection and Immunity 71, no. 2 (2003): 641–46. http://dx.doi.org/10.1128/iai.71.2.641-646.2003.

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ABSTRACT The gene encoding Clostridium sordellii phospholipase C (Csp) was cloned and expressed as a histidine-tagged (His-tag) protein, and the protein was purified to compare its enzymatic and biological activities with those of Clostridium perfringens phospholipase C (Cpa) and Clostridium bifermentans phospholipase C (Cbp). Csp was found to consist of 371 amino acid residues in the mature form and to be more homologous to Cbp than to Cpa. The egg yolk phospholipid hydrolysis activity of the His-tag Csp was about one-third of that of His-tag Cpa, but the hemolytic activity was less than 1% of that of His-tag Cpa. His-tag Csp was nontoxic to mice. Immunization of mice with His-tag Cbp or His-tag Csp did not provide effective protection against the lethal activity of His-tag Cpa. These results indicate that Csp possesses similar molecular properties to Cbp and suggest that comparative analysis of toxic and nontoxic clostridial phospholipases is helpful for characterization of the toxic properties of clostridial phospholipases.
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Anderson, David M., Hiromi Sato, Aaron T. Dirck, Jimmy B. Feix, and Dara W. Frank. "Ubiquitin Activates Patatin-Like Phospholipases from Multiple Bacterial Species." Journal of Bacteriology 197, no. 3 (2014): 529–41. http://dx.doi.org/10.1128/jb.02402-14.

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Phospholipase A2enzymes are ubiquitously distributed throughout the prokaryotic and eukaryotic kingdoms and are utilized in a wide array of cellular processes and physiological and immunological responses. Several patatin-like phospholipase homologs of ExoU fromPseudomonas aeruginosawere selected on the premise that ubiquitin activation of this class of bacterial enzymes was a conserved process. We found that ubiquitin activated all phospholipases tested in bothin vitroandin vivoassays via a conserved serine-aspartate catalytic dyad. Ubiquitin chains versus monomeric ubiquitin were superior in inducing catalysis, and ubiquitin-like proteins failed to activate phospholipase activity. Toxicity studies in a prokaryotic dual-expression system grouped the enzymes into high- and low-toxicity classes. Toxicity measured in eukaryotic cells also suggested a two-tiered classification but was not predictive of the severity of cellular damage, suggesting that each enzyme may correspond to unique properties perhaps based on its specific biological function. Additional studies on lipid binding preference suggest that some enzymes in this family may be differentially sensitive to phosphatidyl-4,5-bisphosphate in terms of catalytic activation enhancement and binding affinity. Further analysis of the function and amino acid sequences of this enzyme family may lead to a useful approach to formulating a unifying model of how these phospholipases behave after delivery into the cytoplasmic compartment.
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Chandra, Vikas, Akanksha Nagpal, A. Srinivasan, and T. P. Singh. "Purification, crystallization and preliminary X-ray crystallographic analysis of a phospholipase A2 from Daboia russelli pulchella." Acta Crystallographica Section D Biological Crystallography 55, no. 4 (1999): 925–26. http://dx.doi.org/10.1107/s090744499900058x.

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Phospholipases are esterolytic enzymes which hydrolyze glycerophospholipids. The pharmacological efficiency of phospholipase A2 (PLA2) enzymes is reflected by their specificity towards a tissue or organ. The Russell's viper has been classified into two classes. Class 1 contains Viper russelli russelli, Viper russelli siamensis and Viper russelli formosensis, whereas class 2 contains Daboia russelli pulchella. The sequence identity between the PLA2s from these two classes is 47%. The novel PLA2 from Daboia russelli pulchella has been crystallized using the hanging-drop vapour-diffusion method with ammonium sulfate as precipitating agent. Crystals belong to the orthorhombic space group C2221 with unit-cell parameters a = 77.01, b = 92.29, c = 76.90 Å and two molecules in the asymmetric unit. These crystals diffract to about 2.49 Å resolution using a rotating-anode source.
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STANTON, Julie D., Mohammad B. RASHID, and Kojo MENSA-WILMOT. "Cysteine-less glycosylphosphatidylinositol-specific phospholipase C is inhibited competitively by a thiol reagent: evidence for glyco-mimicry by p-chloromercuriphenylsulphonate." Biochemical Journal 366, no. 1 (2002): 281–88. http://dx.doi.org/10.1042/bj20020367.

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Glycosylphosphatidylinositol (GPI)-specific phospholipases are highly valuable for studying the structure and function of GPIs. GPI-specific phospholipase C (GPI-PLC) from Trypanosoma brucei and phosphatidylinositol-specific phospholipase C (PI-PLC) from Bacillus cereus are the most widely studied of this class of phospholipases C. Inhibition of protein activity by thiol reagents is indicative of the participation of cysteine residues in biochemical events. The thiol reagent p-chloromercuriphenylsulphonate (pCMPS) inhibits T. brucei GPI-PLC, which has eight cysteine residues. Surprisingly, we found that the activity of B. cereus PI-PLC is also blocked by pCMPS, although the protein does not contain cysteine residues. Inhibition of B. cereus PI-PLC was reversed when pCMPS was size-separated from a preformed pCMPS·PI-PLC complex. In contrast, no activity was recovered when T. brucei GPI-PLC was subjected to a similar protocol. Equimolar β-mercaptoethanol (β-ME) reversed the inhibition of PI-PLC activity in a pCMPS·PI-PLC complex. For T. brucei GPI-PLC, however, ultrafiltration of the pCMPS·GI-PLC complex and addition of a large excess of β-ME was necessary for partial recovery of enzyme activity. Thus T. brucei GPI-PLC is susceptible to inactivation by covalent modification with pCMPS, whereas PI-PLC is not. Kinetic analysis indicated that pCMPS was a competitive inhibitor of PI-PLC when a GPI was a substrate. Curiously, with phosphatidylinositol as substrate, inhibition was no longer competitive. These data suggest that pCMPS is a glyco-mimetic that occupies the glycan binding site of PI-PLC, from where, depending on the substrate, it inhibits catalysis allosterically or competitively.
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Lee, Mi-Hwa, Ki-Hoon Oh, Chul-Hyung Kang, et al. "Novel Metagenome-Derived, Cold-Adapted Alkaline Phospholipase with Superior Lipase Activity as an Intermediate between Phospholipase and Lipase." Applied and Environmental Microbiology 78, no. 14 (2012): 4959–66. http://dx.doi.org/10.1128/aem.00260-12.

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ABSTRACTA novel lipolytic enzyme was isolated from a metagenomic library obtained from tidal flat sediments on the Korean west coast. Its putative functional domain, designated MPlaG, showed the highest similarity to phospholipase A fromGrimontia hollisaeCIP 101886, though it was screened from an emulsified tricaprylin plate. Phylogenetic analysis showed that MPlaG is far from family I.6 lipases, includingStaphylococcus hyicuslipase, a unique lipase which can hydrolyze phospholipids, and is more evolutionarily related to the bacterial phospholipase A1family. The specific activities of MPlaG against olive oil and phosphatidylcholine were determined to be 2,957 ± 144 and 1,735 ± 147 U mg−1, respectively, which means that MPlaG is a lipid-preferred phospholipase. Among different synthetic esters, triglycerides, and phosphatidylcholine, purified MPlaG exhibited the highest activity towardp-nitrophenyl palmitate (C16), tributyrin (C4), and 1,2-dihexanoyl-phosphatidylcholine (C8). Finally, MPlaG was identified as a phospholipase A1with lipase activity by cleavage of thesn-1 position of OPPC, interfacial activity, and triolein hydrolysis. These findings suggest that MPlaG is the first experimentally characterized phospholipase A1with lipase activity obtained from a metagenomic library. Our study provides an opportunity to improve our insight into the evolution of lipases and phospholipases.
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Dissertations / Theses on the topic "PHOSPHOLIPASES A/analysis"

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Bayburt, Timothy. "Kinetic analysis of the 85 kDa cytosolic phospholipase A2 on anionic phospholipid vesicles /." Thesis, Connect to this title online; UW restricted, 1996. http://hdl.handle.net/1773/9220.

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Jardim, Luciana Souza Alcântara. ""Efeitos da atividade da fosfolipase A2 nos receptores dopaminérgicos: implicações para a esquizofrenia"." Universidade de São Paulo, 2005. http://www.teses.usp.br/teses/disponiveis/5/5160/tde-03012006-093632/.

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Um aumento da atividade da PLA2 e alterações do sistema dopaminérgico tem sido descrito em esquizofrenia. No presente estudo, foram investigados os efeitos da atividade da PLA2 sobre os receptores D1 e D2 em cérebro post mortem de 10 sujeitos. Foi encontrado que a PLA2GVI é responsável por 85% do total de atividade da PLA2 no cérebro. A estimulação da PLA2GVI (por EDTA) aumentou a afinidade de D1 em estriado e em CPF e diminuiu a afinidade de D2 em estriado. A inibição da PLA2GVI (por BEL) diminuiu a afinidade de D1 em estriado, e em CPF e CT. A estimulação da PLA2GVI resultou em aumento na densidade de D1 em CPF e CT, e de D2 em estriado. Uma elevação da PLA2 em esquizofrenia poderia contribuir para a biologia da doença através de alterações na neurotransmissão dopaminérgica<br>Increased PLA2 activity and dopaminergic alterations have been described in schizophrenia. In the present study it was investigated the effects of PLA2 activity on D1 and D2 receptors in post mortem brain of 10 subjects. It was found that PLA2GVI corresponds to 85% of all PLA2 activity in the brain. The stimulation of PLA2GVI (by EDTA) increased D1 affinity in striatum and in PFC, and decreased D2 affinity in striatum. Conversely, the inhibition of PLA2GVI (using BEL) decreased D1 affinity in striatum, PFC and TC. The stimulation of PLA2GVI increased D1 density in PFC and TC, as well as the D2 density in striatum. The increased PLA2 activity in schizophrenia may contribute to the biology of the disease through alterations in dopaminergic neurotransmission
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Leslie, Dario Lyall. "Genetic analysis of alpha toxin (phospholipase C) from Clostridium perfringens." Thesis, University of Newcastle Upon Tyne, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.346420.

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Boukli-Hacène, Latifa. "Inhibiteurs de la phospholipase A2 recombinante humaine : synthèse, analyses spectroscopiques : relations structure-activité." Paris 7, 2001. http://www.theses.fr/2001PA077266.

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Suite à une lésion, l'organisme s'adapte puis se défend, il s'agit de la réaction inflammatoire. Ce processus est donc bénéfique mais peut générer des complications sévères et incontrôlables; c'est le cas des pathologies inflammatoires. Nous citerons l'asthme, l'allergie et le choc septique. Bien que l'on ne connaisse pas entièrement son rôle dans le processus inflammatoire, la snpPLA₂ apparaît comme une cible certaine puisqu'elle est présente à des taux très élevés dans les liquides biologiques issus de foyers inflammatoires. De ce fait son inhibition représente une alternative thérapeutique très intéressante aux antiinflammatoires classiques. C'est dans cet esprit que notre laboratoire conçoit et développe de nouvelles séries de molécules et les travaux antérieurs nous ont amenés au choix des structures décrites. Le cycle oxadiazolone, important pour l'activité anti-PLA₂ et surtout pour la spécificité d'action sur la PLA₂ de groupe II impliquée dans le processus inflammatoire, est ici porté par un squelette pipérazinique. Le dosage fluorimétrique de l'activité enzymatique in vitro a révélé que nos composés inhibent de façon spécifique la PLA₂ de groupe II avec des CI₅₀ allant jusqu'à 0,1 ? M. Des modifications autour de la pipérazine ont permis d'améliorer cette activité sans toucher à la spécificité. Une étude spectrophotométrique a permis de vérifier le caractère réel de l'inhibition. Pour le moment, l'étude pharmacologique montre que deux de nos composés sont actifs in vivo par les deux voies d'administration (p. O et i. P) sur l'oedème à la carragénine chez le rat et les résultats encourageants prouvent l'efficacité de la stratégie de "drug design" suivie.
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Olson, Erin Dalene. "A comparative analysis of hydrolysis kinetics by sPLA₂ isoforms during adoptosis in S49 cells /." Diss., CLICK HERE for online access, 2008. http://contentdm.lib.byu.edu/ETD/image/etd2539.pdf.

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Gonzalez, Adriana [Verfasser]. "Biochemical characterization and functional analysis of phospholipase D3 (PLD3) / Adriana Gonzalez." Kiel : Universitätsbibliothek Kiel, 2019. http://d-nb.info/1184274894/34.

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Valentin, Emmanuel. "Diversité structurale des phospholipases A2 sécrétées : clonage et étude fonctionnelle de nouvelles enzymes." Nice, 2000. http://www.theses.fr/2000NICE5473.

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Les phospholipases A2 hydrolysent la liaison ester en position 2 des phospholipides, libérant un acide gras et un lysophospholipide. Ces enzymes jouent un rôle dans la libération d'acide arachidonique et de ses métabolites. Elles interviennent dans des fonctions telles que la digestion, l'inflammation, la défense antibactérienne, le cancer ou l'athérosclérose. Au moins quinze gènes de phospholipases A2 intracellulaires et sécrétées (sPLA2) sont connus. Trois nouvelles sPLA2 de groupe II ont été clonées au cours de cette thèse. Une sPLA2 humaine de groupe III a aussi été clonée. Une sPLA2 de groupe I et cinq sPLA2 de groupe III homologues à la sPLA2 humaine de groupe III ont été clonées chez D. Melanogaster. Enfin, une sPLA2 humaine appartenant à un groupe structural nouveau (groupe XII) a été clonée. Les sPLA2 de mammifères ont une distribution tissulaire distincte. La sPLA2 de groupe IB est impliquée dans la digestion du bol alimentaire mais aussi dans d'autres fonctions. L'expression de la sPLA2 de groupe IIA augmente dans l'inflammation. La sPLA2 de groupe V semble jouer un rôle similaire à celui de la sPLA2 de groupe IIA. Les fonctions physiologiques des autres sPLA2 restent inconnues. L'utilisation de sPLA2 de venin a permis la caractérisation de deux types majeurs de récepteurs (M et N). Les sPLA2 se lient également à d'autres protéines, comme les protéoglycanes ou le facteur Xa de la coagulation, suggérant que les sPLA2 possèdent non seulement des fonctions d'enzyme mais aussi des fonctions de ligand. (. . . )
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Hyvönen, M. (Marja). "Molecular dynamics simulations on phospholipid membranes." Doctoral thesis, University of Oulu, 2001. http://urn.fi/urn:isbn:9514259432.

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Abstract Phospholipids are the main components of cell membranes, lipoproteins and other membrane structures in living organisms. Properties of lipid molecules are important to the overall behaviour and interactions of membranes. Furthermore, characteristics of the biological membranes act as important regulators of membrane functions. Molecular dynamics (MD) simulations were applied in this thesis to study properties of biological membranes. A certain degree of acyl chain polyunsaturation is essential for the proper functioning of membranes, but earlier MD simulations had not addressed the effects of polyunsaturation. Therefore a solvated all-atom bilayer model consisting of diunsaturated 1-palmitoyl-2-linoleoyl-3-phosphatidylcholine (PLPC) molecules was simulated. The analysis of the simulation data was focused on the effects of double bonds on a membrane structure. Self-organising neural networks were applied to the analysis of the conformational data from the 1-ns simulation of PLPC membrane. Mapping of 1.44 million molecular conformations to a two-dimensional array of neurons revealed, without human intervention or requirement of a priori knowledge, the main conformational features. This method provides a powerful tool for gaining insight into the main molecular conformations of any simulated molecular assembly. Furthermore, an application of MD simulations in the comparative analysis of the effects of lipid hydrolysis products on the membrane structure was introduced. The hydrolysis products of the phospholipase A2 (PLA2) enzyme are known to have a role in a variety of physiological processes and the membrane itself acts as an important regulator of this enzyme. The simulations revealed differences in the bilayer properties between the original and hydrolysed phospholipid membranes. This study provides further evidence that MD simulations on biomembranes are able to provide information on the properties of biologically and biochemically important lipid systems at the molecular level.
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Millard, Alexander. "Analysis of PI-PLC Binding to PC and PMe Vesicle Surfaces Using EPR and NMR." Thesis, Boston College, 2005. http://hdl.handle.net/2345/361.

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Thesis advisor: Mary F. Roberts<br>Phosphatidylinositol-specific phospholipase C (PI-PLC) is an enzyme important in membrane-associated signal transduction in eukaryotes, and pathogenic factors in bacteria. It catalyzes the conversion of PI to DAG and cIP, which is further converted to I-1-P. The phospholipid PC has been shown to activate cIP hydrolysis. EPR and NMR were used to examine PI-PLC binding to PC and PMe vesicles through the use of spin labels attached to cysteine mutants. It was concluded that the spin label interacted more significantly with the phosphorus of PC than that of PMe. The results also suggested the -OCH3 group was preferred over the -N(CH3)3 group, and that the protein penetrated into the bulk methylene region of the phospholipid bilayer<br>Thesis (BS) — Boston College, 2005<br>Submitted to: Boston College. College of Arts and Sciences<br>Discipline: Chemistry<br>Discipline: College Honors Program
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Touaibia, Mohamed. "Inhibiteurs de la phospholipase A2 de groupe II : synthèse, analyses spectroscopiques : relations structure-activité." Paris 7, 2002. http://www.theses.fr/2002PA077247.

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Books on the topic "PHOSPHOLIPASES A/analysis"

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N, Fain John, ed. Lipid metabolism in signalling systems. Academic Press, Inc., 1993.

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Methods in Neurosciences: Lipid Metabolism in Signaling Systems (Methods in Neurosciences). Academic Press, 1993.

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N, Fain John, ed. Lipid metabolism in signaling systems. Academic Press, 1993.

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Book chapters on the topic "PHOSPHOLIPASES A/analysis"

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Grossman, Shlomo, Guillermo Oestreicher, and Thomas P. Singer. "Determination of the Activity of Phospholipases A, C, and D." In Methods of Biochemical Analysis. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470110423.ch4.

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Pazzini, Fabiano, Fernanda Oliveira, Jorge A. Guimarães, and Hermes Luís Neubauer de Amorim. "Prediction of Myotoxic and Neurotoxic Activities in Phospholipases A2 from Primary Sequence Analysis." In Advances in Bioinformatics and Computational Biology. Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/11532323_21.

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Carlier, M. B., R. Brasseur, J. M. Ruysschaert, and P. M. Tulkens. "In Vitro Study and Conformational Analysis of 1-N-Aminohydroxybutyryl Derivatives of Aminoglycosides in Correlation with Their Inhibitory Potency Towards Lysosomal Phospholipases." In Archives of Toxicology. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73113-6_30.

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Novotná, Z., O. Valentová, J. Daussant, and J. Káš. "Purification and Immunological Analysis of Phospholipase D from Brassica Napus (Rape Seed)." In Physiology, Biochemistry and Molecular Biology of Plant Lipids. Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-017-2662-7_128.

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Zhao, Jian, and Xuemin Wang. "Biochemical Analysis of the Interaction Between Phospholipase Dα1 and GTP-Binding Protein α-Subunit from Arabidopsis thaliana." In Methods in Molecular Biology. Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-532-3_3.

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Collins, A. Bernard, and R. Neal Smith. "Western Blot Analysis for the Detection of Anti-Glomerular Basement Membrane Antibodies and Anti-Phospholipase A2 Receptor Antibodies." In Manual of Molecular and Clinical Laboratory Immunology. ASM Press, 2016. http://dx.doi.org/10.1128/9781555818722.ch42.

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Heinrikson, Robert L. "[18] Dissection and sequence analysis of phospholipases A2." In Methods in Enzymology. Elsevier, 1991. http://dx.doi.org/10.1016/0076-6879(91)97146-p.

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G., Rodrigo, Rodrigo Simoes-Silva, Anderson M., et al. "Purification of Phospholipases A2 from American Snake Venoms." In Chromatography - The Most Versatile Method of Chemical Analysis. InTech, 2012. http://dx.doi.org/10.5772/53052.

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Brown, H. Alex, Lee G. Henage, Anita M. Preininger, Yun Xiang, and John H. Exton. "Biochemical Analysis of Phospholipase D." In Methods in Enzymology. Elsevier, 2007. http://dx.doi.org/10.1016/s0076-6879(07)34004-4.

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Blank, Merle L., and Fred Snyder. "[14] Chromatographic analysis of phospholipase reaction products." In Methods in Enzymology. Elsevier, 1991. http://dx.doi.org/10.1016/0076-6879(91)97142-l.

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Conference papers on the topic "PHOSPHOLIPASES A/analysis"

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Tonello, Fiorella, and Caterina Peggion. "<em>In silico</em> analysis of short linear motifs present in snake venom phospholipases A2." In 1st International Electronic Conference on Toxins. MDPI, 2021. http://dx.doi.org/10.3390/iect2021-09137.

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Hattori, A., R. Nagayama, I. Fuse, T. Takeshige, S. Takizawa, and A. Shibata. "FURTHER CHARACTERIZATION OF PLATELET RELEASE MECHANISM DEFECT WITH DEFECTIVE A23187 AGGREGATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644878.

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In order to clarify the basic abnormality of patients with release mechanism abnormality with defective response to A23187 (A23) (Hattori et al. Acta Haematol. Jap. 44:969, 1981), the proband (female) showing a life long mild hemorrhagic tendency was further examined. Her platelet (pit) count, morphology, storage pool was normal. Bleeding time (Duke) was more than 15 min.PRP-aggregation (Ag) was normal when induced by PMA, whereas decreased (only primary Ag) by ADP, adrenalin, arachidonate (AA) (−2mM), Tx analog STA2 (−4μM), PAF (−10μM). Ag was defective in response to A23 (−40μM), Ag using washed pits was decreased slightly in response to thrombin or considerably to ionomycin. Adrenalin potentiation was observed in Ag and ATP release (R) by either AA or A23. Ca replacement (over 2mM) with heparinization normalized both Ag and R to those agonists, but Ca agonists did not improve the abnormality. Ca, Na and Cl contents were within normal range. Ca mobilization by Quin-2AM method occurred normally in response to thrombin (0.1, 0.5U/ml), and that by Aequo-rin method was also normal, but retarded with normal peak values in response to A23 and decreased to STA2. Shape change response to various agonists including A23 was normal. AA metabolite analysis by HPLC was normal, but Tx production was low by low dose of A23 but normal by high dose A23 and thrombin (serum). 20 and 40 K protein phosphorylation occured normally when challenged by high and low concentrations of A23 or thrombin, Clot retraction was normal.These results suggest that the abnormality do not exsist in agonist-receptor reactions, enzymes related to production of Tx, Ca slow channel (if it exists), c-Kinase system, Ca content and amount of mobilizable Ca, actomyosin system, protein phosphorylation and reactions after Ca mobilization, but may exsist in activation of phospholipases and an early stage of Ca mobilization based on unknown defect(s).
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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&gt; 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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De Chaffoy de Courcells, D., and F. De Clerck. "THE EFFECT OF A COMBINED TXA2SYNTHETASE AND TXA2/PROSTAGLANDIN ENDOPEROXIDE RECEPTOR BLOCKER(R 68 070)ON THE ACTIVATION OF EXCITATORY RECEPTOR-COUPLEDPHOSPHOLIPASE C IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643758.

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Prostaglandin endoperoxides (PGEND) and thromboxane A2 (TxA2)contribute to the activation of platelets, involving inositol-containing phospholipids as a signal transducing system. A primary step in this signal transduction consists of the activation of phospholipase C, which then yields diacylglycerol and inositol phosphates;diacylglycerol is subsequently phosphorylated to phosphatidic acid (PA). In platelets prelabelled with [32P] orthophosphate,receptor activation is quantitatively reflected by an increased formation of [32P]-PA.Using this assay, the relativeimportance of endogenously generated PGEND and TxA2 for the subsequent PA-formation was analysed by means of pharmacological manipulations. R 68 070, an oxime-alkanecarboxylic acid derivative combining specific TxA2 synthetase inhibition with TxA2/PGEND receptor blockade in one molecule (1 x 10-6M) inhibited the formation of PA in collagen-stimulated platelets; by contrast, synthetase inhibitors without receptor effect (da-zoxiben, OKY-1581,1x 10-6M) increased the PA-response tocollagen.Using U 46619 as a stimulus, R 68 070 as well as BM 13177, a receptor blocker withouteffect on synthetase (1 x 10-6 M)both reduced the PA-response to the same extent while OKY-1581 (1 x 10-6 M) was ineffective. The phospholipid response induced by serotonin, vasopressin or PAF were not affected by R 68 070, demonstrating its specificity for the prostanoid system.From these data we suggest that selectiveinhibition of TxA2 synthetase does not prevent activation of excitatory platelet receptors for arachidonate metabolites. Effectiveness was only obtained by combined TxA2 synthetase/PGEND receptor blockade.
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Akkerman, JW N. "INTRACELLULAR PH CHANGES AND PLATELET ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644774.

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It is long known that platelet aggregation and secretion are accompanied by acidification of the extracellular medium. Much of the proton extrusion results from hydrolysis of ATP generated in the glycolytic pathway and liberation of secretion granules, which are slightly acidic. Recent eyidence points at a third source for extracellular protons.Following early observations (1) that epinephrine-induced platelet functions depended on extracellular Na+ (Na+ o ), it became evident that platelets possess a Na+ /H+ antiport, which regulates the cytosolic pH (pH.) via stochiometric exchange of intracellular protons with extracellular Na+ (2). Platelet functions triggered by epinephrine, AdP or low doses of thrombin are impaired by (i) the absence of Na+ o, and (ii) the presence of EIPA, an amiloride analogue which blocks the antiport. Ionophores which enhance proton efflux enhance the platelet responses. Thus, the antiport affects platelet functions via changes in pHi, but this has been difficult to establish experimentally. Early studies by Simons based on 6-carboxyfluorescein indeed reported a rise in pHi. during platelet activation, but more precise analysis awaited the development of more sensitive pHi-indicators. Recently (3),1studies employing BCECF, have confirmed that resting platelets maintain a pH. of about 7.1 via an EIPA-sensitive mechanism.Platelet activation induces a rise of 0.1-0.2 pH units, which lasts for several minutes unless the antiport is inhibited. When Na+/H+ exchange is gradually inhibited by lowering Na+ o , EIPA-sensitive proton efflux, mobilization of Ca2+ ions and aggregation are inhibited in parallel following stimulation with a low dose of thrombin. Artificial alkalinization reverses these effects. Alkalinization alone is not a trigger for platelet functions. Furthermore, high doses of thrombin (&gt; 0.2 U/ml) initiate Ca2+ -mobilization and aggregation independent of changes in pHi Possibly, Na+ /H+ exchange enhances Ca mobilization by inositol-P3, generated by weak stimulation of the thrombin receptor, wfiich accords with the pH profile of IP3-induced Ca2+ liberation from isolated dense tubular membranes. However, concurrent measurement of Quin-2 and BCECF-fluoresence indicate that Ca2+ mobilization slightly precedes the rise in pHi which would make Ca+ mobilization a trigger for Na+ /H+ exchange is stead of one of its effects. Recent data favour a role for protein kinase C in activation of the antiport. A rise in pHi. is seen during incubation with OAG, an activator of protein kinase C. Thrombin (low dose)-induced Na /H exchange is inhibited by TFP, an inhibitor of this enzyme. These findings are bes^explained by assuming that low doses of thrombin initiate phospholipase C-mediated formation of inositol-P3, which triggers Ca2+ mobilization. Concurrently, diacylglycerol is formed, which activates protein kinase C. The result is a rise in pHi, which enhances the mobilization of Ca2+ by inositol-P3.This scheme differs from the sequence seen during activation by ADP or epinephrine (1), where Na+ /H2+ exchange is an early step after receptor occupancy and precedes phospholipid A2-mediated PG-endoperoxides/TxA2 formation. These metabolites activate phospholipase C resulting in diacylglycerol and inositol-P3-formation at a rather late stage in signal processing. Recent evidence (4) indicates that in epinephrine-stimulated platelets Na+ /H+ exchange requires fibrinogen binding, which opens the intriguing possibility that occupancy of GPIIb-IIIa starts a process that affects signal processing pathways in platelets.Sweatt, J.D., Limbird, L.E, et al. J.B.C. 1983, 1985, 1986Siffert, W., Akkerman, J.W.N., et al. FEBS Lett 1984, 1987; Nature 1987.Zavoico, G.B., Feinstein, M.B st al. J.B.C. 1986Banga, H.D., Rittenhouse, S.E. PNAS 1986
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