C Type Lectin
Mostrando 1-12 de 169 artigos, teses e dissertações.
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1. Subproteome of Lachesis muta rhombeata venom and preliminary studies on LmrSP-4, a novel snake venom serine proteinase
Abstract Background: Lachesis muta rhombeata is one of the venomous snakes of medical importance in Brazil whose envenoming is characterized by local and systemic effects which may produce even shock and death. Its venom is mainly comprised of serine and metalloproteinases, phospholipases A2 and bradykinin-potentiating peptides. Based on a previously report
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 15/04/2019
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2. Endogenous phospholipase A2 inhibitors in snakes: a brief overview
Abstract The blood plasma of numerous snake species naturally comprises endogenous phospholipase A2 inhibitors, which primarily neutralize toxic phospholipases A2 that may eventually reach their circulation. This inhibitor type is generally known as snake blood phospholipase A2 inhibitors (sbPLIs). Most, if not all sbPLIs are oligomeric glycosylated proteins
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 19/01/2017
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3. Expression of non-TLR pattern recognition receptors in the spleen of BALB/c mice infected with Plasmodium yoelii and Plasmodium chabaudi chabaudi AS
The spleen plays a crucial role in the development of immunity to malaria, but the role of pattern recognition receptors (PRRs) in splenic effector cells during malaria infection is poorly understood. In the present study, we analysed the expression of selected PRRs in splenic effector cells from BALB/c mice infected with the lethal and non-lethal Plasmodium
Mem. Inst. Oswaldo Cruz. Publicado em: 2012-05
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4. Purificação e caracterização química e funcional de uma lectina tipo-C ligante de D-galactose da peçonha de Bothropoides pauloensis (Bothrops pauloensis) / Purification and biochemical characterization of an agglutinating C-type lectin (BpLec) from Bothropoides pauloensis (Bothrops pauloensis) snake venom
CAPÍTULO II: Lectinas tipo C são proteínas caracterizadas por se ligarem a carboidratos de forma não-covalente. Estão descritas em diversos organismos, incluindo peçonhas ofídicas. Esse trabalho teve como objetivo isolar e a caracterizar bioquimicamente uma lectina tipo C da peçonha de Bothropoides pauloensis. A proteína denominada BpLec é específ
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 27/07/2011
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5. 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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6. Estudo das atividades das cabenegrinas A-I e A-II frente aos efeitos hematolÃgicos e histolÃgicos induzidos pelo veneno total e fraÃÃes da serpente Bothrops neuwiedi em camundongos Swiss. / Study of the activities of cabenegrinas A-I and A-II compared to the histological and hematological effects induced by the venom and fractions of the snake Bothrops neuwiedi in Swiss mice.
The venom of the Bothrops neuwiedi provokes an action mainly of the hemorrhagic, proteolytic and coagulant type. When inoculated, the venom cause primarily a local action, and secondarily a systemic action. The systemic effects of poisoning include changes in various systems such as hematological, cardiovascular, liver, urinary, respiratory, immune, digestiv
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 30/06/2011
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7. 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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8. Evaluation of the involvement of Toll like and C-type lectin receptors in the immunessuppression induced by high molecular weight components from Ascaris suum extract. / Avaliação da participação dos receptores do tipo Toll e lectinas tipo C na supressão da resposta imune induzida por componentes de alta massa molecular do extrato de Ascaris suum.
Helminths and antigens derived from them are potent immunemodulators. High molecular weight components of Ascaris suum extract (PI) suppress the anti-ovalbumin response. The PI components inhibit in antigen-presenting cells (APCs), as dendritic cells (DCs), the expression of MHC-II and coestimulatory molecules and, thus the CD4 + T cells activation. APCs via
Publicado em: 2010
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9. 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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10. 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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11. Atividades antinociceptiva e antiinflamatÃria da lectina da alga marinha verde Caulerpa cupressoides (Vahl) C. Agardh var. lycopodium em animais / Antinociceptive and anti-inflammatory activities of the lectin from the green marine alga Caulerpa cupressoides (Vahl) C. Agardh var lycopodium (CcL) in animals.
The search of new alternative compounds in the control of the pain and inflammation, with minima collateral effects, it has been aroused from marine algae. The aim of this work was to investigate the potential antinociceptive and anti-inflammatory of the lectin from the green marine alga Caulerpa cupressoides (Vahl) C. Agardh var lycopodium (CcL) in animals.
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 19/11/2008
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12. Expressão de recptores do tipo Toll e dectina em monocitos e neutrofilos estimulados pelo Paracoccidioides brasiliensis / Expression of Toll-like receptos and dectin-1 in monocytes and neutrophils stimulated by Paracoccidioides brasiliensis
Paracoccidioidomycosis (PCM) is an endemic mycosis in Latin America caused by the dimorphic fungus Paracoccidioides brasiliensis. The pattern of the immune responses to P. brasiliensis determines the disease progression and clinical outcome. Innate immune response is mediated by phagocytic cells, such as macrophage and neutrophils, which ingest and kill inva
Publicado em: 2008