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Pesquisa : D08.811.277.352.640.700.710 [Categoria DeCS]
Referências encontradas : 9 [refinar]
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  1 / 9 LILACS  
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Id: biblio-954860
Autor: Arán-Sekul, Tomás; Rojas, José M; Subiabre, Mario; Cruz, Victoria; Cortés, William; Osorio, Luis; González, Jorge; Araya, Jorge E; Catalán, Alejandro.
Título: Heterophilic antibodies in sera from individuals without loxoscelism cross-react with phospholipase D from the venom of Loxosceles and Sicarius spiders
Fonte: J. venom. anim. toxins incl. trop. dis;24:18, 2018. tab, ilus.
Idioma: en.
Projeto: National Fund for Scientific and Technological Development; . Fund for Promotion of Scientific and Technological Development.
Resumo: Loxoscelism is a severe human envenomation caused by Loxosceles spider venom. To the best of our knowledge, no study has evaluated the presence of antibodies against Loxosceles venom in loxoscelism patients without treatment with antivenom immunotherapy. We perform a comparative analysis for the presence of antibodies capable of recognizing Loxosceles venom in a group of patients diagnosed with loxoscelism and in a group of people without loxoscelism. Methods The detection of L. laeta venom, Sicarius venom and recombinant phospholipases D from Loxosceles (PLDs) in sera from people with loxoscelism (Group 1) and from healthy people with no history of loxoscelism (Group 2) was evaluated using immuno-dot blot, indirect ELISA, and Western blot. Results We found naturally heterophilic antibodies (IgG-type) in people without contact with Loxosceles spiders or any clinical history of loxoscelism. Either serum pools or single sera from Group 1 and Group 2 analyzed by dot blot tested positive for L. laeta venom. Indirect ELISA for venom recognition showed titles of 1:320 for Group 1 sera and 1:160 for Group 2 sera. Total IgG quantification showed no difference in sera from both groups. Pooled sera and purified IgG from sera of both groups revealed venom proteins between 25 and 32 kDa and the recombinant phospholipase D isoform 1 (rLlPLD1), specifically. Moreover, heterophile antibodies cross-react with PLDs from other Loxosceles species and the venom of Sicarius spider. Conclusions People without contact with the spider venom produced heterophilic antibodies capable of generating a cross-reaction against the venom of L. laeta and Sicarius spiders. Their presence and possible interference should be considered in the development of immunoassays for Loxosceles venom detection.(AU)
Descritores: Fosfolipase D/isolamento & purificação
Venenos de Aranha/toxicidade
Anticorpos Heterófilos/sangue
Antivenenos/uso terapêutico
-Ensaio de Imunoadsorção Enzimática/métodos
Immunoblotting/métodos
Limites: Seres Humanos
Masculino
Feminino
Adolescente
Adulto
Meia-Idade
Tipo de Publ: Estudo Comparativo
Responsável: BR33.1 - Divisão Técnica de Biblioteca e Documentação


  2 / 9 LILACS  
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Id: lil-644470
Autor: Selim, S. A; Mousa, W. M; Mohamed, K. F; Moussa, I. M.
Título: Synergistic haemolytic activity and its correlation to phospholipase D productivity by Corynebacteruim pseudotuberculosis Egyptian isolates from sheep and buffaloes
Fonte: Braz. j. microbiol;43(2):552-559, Apr.-June 2012. ilus, tab.
Idioma: en.
Resumo: Fourteen isolates of Corynebacteruim pseudotuberculosis of them 7 were isolated from sheep with Caseous Lymphadenitis "biotype 1" and 7 isolated from buffaloes with Oedematous Skin Disease "biotype 2". All isolates were identified by standard microbiological techniques and by polymerase chain reaction targeting, 16S rRNA and phospholipase D genes. Synergistic haemolytic titers of all isolates were assayed by plate technique. The presences of phospholipase D gene in supernatants of all isolates were performed by sodium dodecyl sulfate polyacrylamide gel electrophoresis immunoblot technique by using hyperimmune serum raised in rabbit immunized with recombinant phospholipase D gene antigen. The concentration of phospholipase D gene was assayed by scanning the bound phospholipase D gene with specific antibodies that appeared at 31.5 kDa. Results presented that there is no correlation between titer of Synergistic haemolytic activity and the actual phospholipase D genes concentration in culture supernatants. Also results presented that Synergistic haemolytic activity and phospholipase D genes produced by biotype 2 (buffalo isolates) was generally higher than those by biotype 1(sheep isolates).
Descritores: Infecções por Corynebacterium
Corynebacterium pseudotuberculosis/enzimologia
Corynebacterium pseudotuberculosis/isolamento & purificação
Fosfolipase D/genética
Fosfolipase D/isolamento & purificação
Regulação da Expressão Gênica
Técnicas In Vitro
Linfadenite
RNA
-Búfalos
Eletroforese
Ativação Enzimática
Métodos
Coelhos
Ovinos
Limites: Animais
Bovinos
Coelhos
Tipo de Publ: Estudo Comparativo
Responsável: BR32.1 - Serviço de Biblioteca e Informação Biomédica


  3 / 9 LILACS  
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Id: lil-335989
Autor: Sabatini, David D; Adesnik, Milton; Ivanov, Ivanov E; Simon, Jean-Pierre.
Título: Mechanism of formation of post Golgi vesicles from TGN membranes: Arf-dependent coat assembly and PKC-regulated vesicle scission
Fonte: Biocell;20(3):287-300, Dec. 1996.
Idioma: en.
Resumo: We have developed an experimental system that utilizes purified Golgi fractions obtained from virus infected infected MDCK cells to reproduce in vitro the process of vesicle generation in the trans Golgi network, an important site for the sorting of proteins addressed to the plasma membrane, secretory vesicles, or lysosomes. Using an integrated biochemical and electron microscopic approach, we have shown that the formation of post Golgi vesicles carrying proteins destined to both plasma membrane domains of epithelial cells requires the activation of an ArF-like GTP-binding protein that serves to promote the assembly of the protein coat necessary to deform the donor membrane and generate a vesicle. The formation of the post Golgi vesicles also requires the participation of a Golgi membrane-associated Protein Kinase C, but not its phosphorylating activity. Other authors have shown that this is also the case for the PKC activation of the enzyme phospholipase D, which generates phosphatidic acid from phosphatidyl choline and may be involved in remodeling of membranes. We have been able to dissect the process of post Golgi vesicle generation into two sequential stages, one of coat assembly and bud formation, and a subsequent one of vesicle scission. The first stage can occur at 20 degrees C and requires the activation of the Arf protein necessary for coat assembly. The second stage does not require nucleotides or an energy supply, but requires cytosolic proteins, and in particular, an NEM sensitive membrane scission promoting activity that operates only at a higher temperature of incubation. Because various PKC inhibitors blocked vesicle scission without preventing bud formation, we propose that the PKC is required for the activation of a PLD in the TGN, which leads to remodeling of the donor membrane and the severing of connections between the emerging vesicles and the membranes.
Descritores: Complexo de Golgi
Membranas Intracelulares
Proteína Quinase C/fisiologia
Proteínas Virais/fisiologia
Vesículas Revestidas/fisiologia
-Transporte Biológico
Linhagem Celular
Sistema Livre de Células
Proteína Coatomer
Fosfatidilinositóis/fisiologia
Guanosina Trifosfato
Rim
Lisossomos
Fosfolipase D
Proteínas de Membrana/metabolismo
Limites: Animais
Cães
Tipo de Publ: Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Responsável: BR1.1 - BIREME


  4 / 9 LILACS  
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Id: lil-140279
Autor: Stambuk, B. U; Cardoso-de-Almeida, M. L.
Título: Further characterization of the acidic GPI-hydrolyzing phospholipase present in human sera
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(2):383-7, Feb. 1994. ilus.
Idioma: en.
Conferência: Apresentado em: GPI-Anchor Proteins: Structure and Function - 1994 Meeting, Angra dos Reis, 20-26 Feb. 1994.
Resumo: A phospholipase from human serum capable of hydrolyzing glycosylphosphatidylinositol membrane anchors was described and partially characterized by our group some years ago. This activity presented a pH optimum between 5.0 and 6.0 and was inhibited by EDTA, EGTA and 1,10-phenanthroline. Partial purification showed that the enzyme was a glycoprotein with an apparent molecular weight of 140 kDa as judged by gel filtration. Other investigators characterized at the same time a phospholipase D with similar properties but with a pH optimum near 7.5. We now confirm that the human serum enzyme is indeed a phospholipase D capable of hydrolyzing mfVSG and glycolipids A and C from T. brucei. Isoelectric focusing of whole sera suggests the presence of two isoforms, one with a pI of 4.7 which was the form previously purified by our group, and others with pI from 6.2 to 7.4
Descritores: Fosfatidilinositóis/química
Glicolipídeos/química
Hidrólise
Fosfolipase D
Plasma
-Cromatografia em Gel
Lipase
Trypanosoma brucei brucei
Glicoproteínas Variantes de Superfície de Trypanosoma
Limites: Seres Humanos
Responsável: BR26.1 - Biblioteca Central


  5 / 9 LILACS  
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Id: lil-140278
Autor: Deeg, M. A.
Título: GPI-specific phospholipase D as an apolipoprotein
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(2):375-81, Feb. 1994. ilus.
Idioma: en.
Conferência: Apresentado em: GPI-Anchor Proteins: Structure and Function - 1994 Meeting, Angra dos Reis, 20-26 Feb. 1994.
Resumo: Glycosylphosphatidylinositol-specific phospholipase D (GPI-PLD) has recently been shown to be associated with high-density lipoproteins (HDL) in bovine serum. To determine the distribution of GPI-PLD among lipoproteins and characterize the GPI-PLD-containing lipoproteins in human plasma, we used dextram sulfate and immunoaffinity chromatography to isolate apolipoprotein-specific lipoproteins. This procedure allowed fractionation of lipoprotein particles into those containing apolipoprotein B (Lp B), apolipoproteins AI and AII (Lp AI/AII), or apolipoprotein AI only (Lp AI). In five plasma samples with HDL cholesterol ranging from 40 to 129 mg/dl, 75 ñ 12 percent (mean ñ SD) of the GPI-PLD activity was associated with LpAI, 11 ñ 13 percent with Lp AI/AII, while only 13 ñ 9 percent was present in plasma devoid of these lipoproteins, suggesting that most of the GPI-PLD in human plasma is associated with apolipoprotein AI. No GPI-PLD activity was detected in Lp B. Further characterization of the GPI-PLD-containing lipoproteins by gel filtration chromatography, nondenaturing poly-acrylamide and agarose gel electrophoresis revealed that GPI-PLD was restricted to an apolipoprotein AI-containing particle or complex that was small (apparent mean Mw of 140 KDa) and distinct from the bulk of HDL. Thus, the majority of plasma GPI-PLD appears to be specifically associated with a small, minor fraction of apoloprotein AI
Descritores: Apolipoproteína A-I
Sulfato de Dextrana
Fosfatidilinositóis/química
Glicolipídeos/química
Lipoproteínas HDL
Fosfolipase D/metabolismo
Plasma/enzimologia
-Cromatografia de Afinidade
Cromatografia em Gel
Eletroforese em Gel de Ágar/métodos
Fosfatidilinositóis/metabolismo
Glicolipídeos/metabolismo
Ultracentrifugação/métodos
Limites: Seres Humanos
Bovinos
Responsável: BR26.1 - Biblioteca Central


  6 / 9 LILACS  
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Id: lil-140277
Autor: Brodbeck, U; Bütikofer, P.
Título: GPI anchor-hydrolyzing phospholipases
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(2):369-74, Feb. 1994. tab.
Idioma: en.
Conferência: Apresentado em: GPI-Anchor Proteins: Structure and Function - 1994 Meeting, Angra dos Reis, 20-26 Feb. 1994.
Resumo: Glycosilphosphatidylinositol(GPI) anchor-hydrolyzing phospholipases include C- and D- type phospholipases and have been described in a number of organisms including bacteria, protozoan parasites, plants, and mammals. Although these phospholipases efficiently cleave GPI structures in vitro, the physiological role of GPI hydrolysis by anchor-specific phospholipases is still unclear. In order to permit comparison of the known GPI anchor-hydrolyzing phospholipases, we studied the kinetic parameters of these enzymes and provide an overview of the currently available information
Descritores: Fosfatidilinositóis/química
Glicolipídeos/química
Hidrólise
Técnicas In Vitro
Fosfolipase D
Fosfolipases Tipo C
-Acetilcolinesterase
Eritrócitos
Mamíferos
Trypanosoma brucei brucei
Glicoproteínas Variantes de Superfície de Trypanosoma
Limites: Bovinos
Camundongos
Ratos
Responsável: BR26.1 - Biblioteca Central


  7 / 9 LILACS  
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Id: lil-140272
Autor: Rademacher, T. W; Caro, H; Kunjara, S; Wang, D. Y; Greenbaum, A. L; McLean, P.
Título: Inositolphosphoglycan second messengers
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(2):327-41, Feb. 1994. ilus.
Idioma: en.
Conferência: Apresentado em: GPI-Anchor Proteins: Structure and Function - 1994 Meeting, Angra dos Reis, 20-26 Feb. 1994.
Resumo: The mechanisms by which cellular receptors can elicit different biological responses in a maturation state-dependent manner is one of the central problems in cell differentiation which remains to be resolved. The signals generated are likely to be due to additional (as yet unknown) transmembrane signalling pathways. In addition, the recent observation that a single growth factor receptor can activate a whole family of different putative second messengers and that the combinatorial interactions and stoichiometric ratios between the different messengers determine the resulting biological activities has opened up a whole new area of cell biology. It has been proposed that membrane GPI-anchors may function in signal transduction. We have recently confirmed the presence of a family of inositolphosphoglycan second messengers. Partial structural data suggest that these second messengers are not derived from known GPI membrane anchors and may thus constitute a novel class of non-protein-conjugated GPI
Descritores: Glicolipídeos
Inositol/química
Insulina
Fosfatidilinositóis
-Hidrólise
Fosfolipase D
Proteínas Tirosina Quinases
Fosfolipases Tipo C
Responsável: BR26.1 - Biblioteca Central


  8 / 9 LILACS  
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Id: lil-140266
Autor: Censullo, P; Davitz, M. A.
Título: The fate of GPI-anchored molecules
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(2):289-95, Feb. 1994. ilus.
Idioma: en.
Conferência: Apresentado em: GPI-Anchor Proteins: Structural and Function - 1994 Meeting, Angra dos Reis, 20-26 Feb. 1994.
Resumo: Glycosylphosphatidylinositol (GPI)-anchored proteins comprise a diverse class of membrane molecules. They protect cells from complement-mediated lysis, control cell to cell adhesion, activate T cells, and play a role in the etiology of slow viral diseases. Despite their functional diversity, GPI-anchored proteins are all attached to the plasma membrane by a common glycolipid anchor. We will examine one aspect of GPI-anchor metabolism, namely, the processing of the molecule after it arrives at the plasma membrane. After biosynthesis and transport to the plasma membrane, the GPI-anchored protein can be endocytosed and degraded or cleaved and released. The enzymatic machinery controlling the catabolism of GPI-anchored molecules at the plasma membrane is likely to play a central role in regulating the cell surface expression of these molecules
Descritores: Fosfatidilinositóis/metabolismo
Glicolipídeos/metabolismo
Heparitina Sulfato
Fosfolipase D
Príons
Proteoglicanas
-Membrana Celular
Proteínas de Membrana
Responsável: BR26.1 - Biblioteca Central


  9 / 9 LILACS  
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Sousa, Marcelo Valle de
Morhy, Lauro
Id: lil-85476
Autor: Sousa, Marcelo Valle de; Morhy, Lauro.
Título: Enterolobin, a hemolytic protein from Enterolobium contortisiliquum seeds (Leguminosae - Mimosoideae): purification and characterization
Fonte: An. acad. bras. ciênc;61(4):405-12, dez. 1989. ilus, tab.
Idioma: en.
Resumo: Hemolytic and phospholipase D activities were found in the saline extract of Enterolobium contortisiliquum seeds. The hemolytic activity is due to a protein which was named enterolobin. This protein was highly purified by extraction with 0.15 M NaCl, precipitation with ammonium sulphate from 0 to 33% of highly purified by extraction with 0.15 M NaCl, precipitation with ammonium sulphate from 0 to 33% of saturation, batch separation by adsorption on DEASE - cellulose and gel filtration chromatography on Sephadex G-100 or G-150. In the batch separation the fraction showing hemolytic activity was not adsorbed by the resin while the fraction with phospholipase activity was. In this manner it was shown that those two activities were due to different proteins. Mouse erythrocytes were less susceptible to hemolysis by enterolobin than human and rabbit erythrocytes. The hemolytic activity was rapidly lost at or above 55§C and in extreme acid (1.6) and basic (10.8) pHs. The following characteristics of purified enterolobin were determined: molecular weights of 55.000 D (by SDS-PAGE), 59.800 D (by gel filtration) and 51.300 D (by HPLC); pI=7,0; Gln as the N-terminal amino acid residue; high levels of Asp(Asx), Glu(Glx), Ser and Thr residues and low levels of Cys and Met residues. Similarities were noticed between enterolobin and crotin, a hemolytic protein of Croton tiglium seeds
Descritores: Fabaceae/análise
Proteínas de Plantas/isolamento & purificação
-Hemólise
Fosfolipase D/isolamento & purificação
Sementes/análise
Limites: Camundongos
Coelhos
Animais
Seres Humanos
Responsável: BR1.1 - BIREME



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