Lectins C Type
Mostrando 1-12 de 76 artigos, teses e dissertações.
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1. Modulation of macrophage function by Nattectin: a C-type lectin from Thalassophryne nattereri fish venom. / Modulação da função de macrófagos pela nattectina: uma lectina tipo C do veneno de Thalassophryne nattereri.
A Nattectina é uma toxina isolada do veneno de Thalassophryne nattereri que possui homologia com lectinas tipo C. Este estudo consistiu em avaliar a ação da Nattectina sobre as funções de macrófagos e a influência de citocinas Th1/Th2 nessa ativação. Nossos resultados mostram que a Nattectina induziu o aumento da expressão de moléculas coestimulad
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 08/07/2011
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2. Purification and biological effects of a C-type lectin isolated from Bothrops moojeni
Snake venom proteins from the C-type lectin family have very distinct biological activities despite their highly conserved primary structure, which is homologous to the carbohydrate recognition region of true C-type lectins. We purified a lectin-like protein (BmLec) from Bothrops moojeni venom and investigated its effect on platelet aggregation, insulin secr
Journal of Venomous Animals and Toxins including Tropical Diseases. Publicado em: 2010
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3. Expression and possible functional role of galectin-3 in the / Expressão e possível papel funcional da galectina-3 no timo de camundongos diabéticos não-obesos (NOD)
Galectin-3 belongs to a family of endogenous lectins which bind to -galactosides presented on the cell surface and extracellular matrix glycoproteins. It is involved in multiple biological functions such as cell growth, adhesion, proliferation and apoptosis. Moreover, galectin-3 is found in several tissues and organs, being highly conserved among animal spec
Publicado em: 2010
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4. Evaluation on the involvement of Galatrox, a lactose binding lectin isolated from Bothrops atrox venom, on the inflammatory process / Avaliação do envolvimento da Galatrox, uma lectina ligante de lactodr isolada da peçonha de Bothrops atrox, no processo inflamatório
Lectins are proteins with no enzymatic activity and are able to bind specifically and non-covalently (reversible manner) to carbohydrates. In addition, these proteins are involved in several physiological and pathological events, as embryogenesis, immune response, cancer, and others. Galatrox, a lactose-binding protein, was purified from Bothrops atrox snake
Publicado em: 2010
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5. Avaliação do papel da galectina-3 sobre funções de neutrófilos durante a infecção por cepa virulenta RH de Toxoplasma gondii em camundongos C57BL/6
Galectins are beta-galactoside-binding animal lectins involved in several biological processes, and Gal-3 has been related to modulation of immune reactions and inflammatory responses. The present study aimed to evaluate the influence of Gal-3 in neutrophil viability, early apoptosis and cell death in parallel with its biological functions after in vivo and
Publicado em: 2009
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6. Estudo da atividade antiinflamatÃria e antinociceptiva da lectina isolada da alga marinha vermelha Hypnea cervicornis (J. Agardh). / Study of antiinflammatory and antinociceptive activities of a lectin isolated from the red marine alga Hypnea cervicornis (J. Agardh)
Lectins are (glyco)proteins that can recognize and reversibly bind to carbohydrates or other substances derived from sugars. They are found throughout animal and vegetal kingdoms. Hypnea cervicornis is a species of marine red algae found in Northeast of Brazil from which was isolated the lectin Hypnea cervicornis aglutinin (HCA), a polypeptide containing 90
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 12/07/2007
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7. A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytes
Purification of a lectin from Bothrops jararacussu venom (BjcuL) was carried out using agarose-D-galactose affinity gel. MALDI-TOF gave a major signal at m/z 32028, suggesting the presence of a dimmer composed of two identical subunits. Divalent cations were required for the lectin activity, as complete absence of such ions reduced hemagglutination. BjcuL wa
Journal of Venomous Animals and Toxins including Tropical Diseases. Publicado em: 2007
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8. CaracterizaÃÃo molecular da lectina ligadora de manose (MBL) em indivÃduos com hepatite C
Mannan-binding lectin (MBL), a member of the type-C lectins, is able to bind through multiple sites to various carbohydrate structures and activate complement. Low levels of MBL have been linked with susceptibility to several infectious diseases. Different assays used to MBL determination havenât been able to identify widely its molecular forms in the circu
Publicado em: 2007
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9. Renal effects promoted by myotoxins and lectins isolated from the snake venoms of Bothrops jararacusu and Bothrops moojeni. The role of cyclooxigenase and endothelin / Efeitos renais de miotoxinas e lectinas purificadas dos venenos das serpentes Bothrops jararacussu e Bothrops moojeni. Papel da ciclooxigenase e endotelina
Acute renal failure is one of the most common systemic complications after snakebite. However, its pathogenesis remains obscure. In this study, we evaluated the renal effects of Bothrops jararacussu myotoxins I and II (Bthtx-I Lys 49 and BthtxII, Asp 49), Bothrops moojeni myotoxin I and the lectins from Bothrops moojeni and Bothrops jararacussu. Attempting t
Publicado em: 2006
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10. ExtraÃÃo lÃquido-lÃquido da lectina da entrecasca de Crataeva tapia l. utilizando micelas invertidas
The lectins are ubiquitous protein in the nature that reversibly bind to mono, oligo, polysaccharides and glycoconjugates. They do not present catalytic activity and unlike antibodies, are not products of immune reply. The aim of the present work was to evaluate the extraction and back-extraction of a lectin purified by ionic exchange chromatography (CrataBL
Publicado em: 2006
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11. Crotacetin, a novel snake venom C-type lectin, is homolog of convulxin
Snake venom (sv) C-type lectins encompass a group of hemorrhagic toxins, which are able to interfere with hemostasis. They share significant similarity in their primary structures with C-type lectins of other animals, and also present a conserved carbohydrate recognition domain (CRD). A very well studied sv C-type lectin is the heterodimeric toxin, convulxin
Journal of Venomous Animals and Toxins including Tropical Diseases. Publicado em: 2005-12
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12. Differential effect of plant lectins on mast cells of different origins
Histamine release induced by plant lectins was studied with emphasis on the carbohydrate specificity, external calcium requirement, metal binding sites, and mast cell heterogeneity and on the importance of antibodies bound to the mast cell membrane to the lectin effect. Peritoneal mast cells were obtained by direct lavage of the rat peritoneal cavity and gui
Brazilian Journal of Medical and Biological Research. Publicado em: 2005-06