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canavalia ensiformis/inflammation

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BACKGROUND Lectins are a family of proteins capable of deciphering the glycan code. Several authors have published works about crystallization and mass spectrometry analyses of ConA-like lectins. However, mass spectrometry has never been used to characterize lectin crystal content. In this study,

Purification, characterization and partial sequence of a pro-inflammatory lectin from seeds of Canavalia oxyphylla Standl. & L. O. Williams.

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Recent studies have shown that lectins are promising tools for use in various biotechnological processes, as well as studies of various pathological mechanisms, isolation, and characterization of glycoconjugates and understanding the mechanisms underlying pathological mechanisms conditions,

Structural basis of ConM binding with resveratrol, an anti-inflammatory and antioxidant polyphenol.

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Resveratrol can also inhibit the activation of proinflammatory mediators and cytokines at the early gene expression stage. It is well known that lectins are sugar-binding proteins that act as both pro- and anti-inflammatory molecules. Thus, the objective of this work was to verify the binding of a

Anti-Inflammatory Effects of Canavalia gladiata in Macrophage Cells and DSS-Induced Colitis Mouse Model.

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Canavalia gladiata, known as sword bean, has been used as a Chinese traditional medicine for anti-inflammatory effects. However, the action mechanisms of sword bean have not yet been clearly defined. In the present study, the whole parts of a ripened sword bean (RSB) and the green sword bean

Effects of Canavalia lectins on acute inflammation in sensitized and non-sensitized rats.

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The anti-inflammatory activity of Canavalia seed lectins (Canavalia gladiata [CGL], Canavalia maritima [ConM] and Canavalia brasiliensis [ConBr]) was evaluated by intravenous administration in rats. In non-sensitized rats, cellular edema elicited by carrageenan was reduced (45-51 %) by ConM and

Lectin from Canavalia villosa seeds: A glucose/mannose-specific protein and a new tool for inflammation studies.

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With important carbohydrate binding properties, lectins are proteins able to decipher the glycocode, and as such, they can be used in bioassays involving cell-cell communication, protein targeting, inflammation, and hypernociception, among others. In this study, a new glucose/mannose-specific lectin
Kujigamberol is the norlabdane compound isolated from Kuji amber and has recently been shown to prevent Ca2+-signal transduction and exert anti-allergy effects in vitro and in vivo. However, the anti-inflammatory activities of kujigamberol remain unclear. In the present study, we investigated the

Anti-inflammatory effect of glucose-mannose binding lectins isolated from Brazilian beans.

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Selectins are essential for leukocyte recruitment in inflammation. Because of a lectin domain present in the selectin structure, we investigated the anti-inflammtory activity of six mannose-glucose binding lectins from brazilian beans: Dioclea guianensis-DguiL; D. grandiflora-DgL; Cratylia

Lectin extracted from Canavalia grandiflora seeds presents potential anti-inflammatory and analgesic effects.

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Neutrophil migration is responsible for tissue damage observed in inflammatory diseases and is also implicated in inflammatory nociception. The use of lectins has been demonstrated to be effective in different activities including anti-inflammatory, antimicrobial, and in cancer therapy. In this

Exploring the carbohydrate-binding ability of Canavalia bonariensis lectin in inflammation models

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Lectins are a group of proteins of non-immune origin recognized for their ability to bind reversibly to carbohydrates. Researchers have been intrigued by oligosaccharides and glycoconjugates for their involvement as mediators of complex cellular events and then many biotechnological applications of

Structural studies of an anti-inflammatory lectin from Canavalia boliviana seeds in complex with dimannosides.

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Plant lectins, especially those purified from species of the Leguminosae family, represent the best-studied group of carbohydrate-binding proteins. Lectins purified from seeds of the Diocleinae subtribe exhibit a high degree of sequence identity notwithstanding that they show very distinct

Structural characterization of a lectin from Canavalia virosa seeds with inflammatory and cytotoxic activities.

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A lectin from Canavalia virosa, Diocleinae subtribe, was purified by affinity chromatography with Sephadex G-50 matrix and named ConV. The primary structure of ConV was obtained by mass spectrometry and crystals were obtained by the vapor diffusion method at 293K and belonged to orthorhombic space
BACKGROUND Phytotherapeutics exhibit diverse pharmacological effects that are based on the combined action of a mixture of phytoconstituents. In this study, Prunus domestica gum-loaded, stabilized gold and silver nanoparticles (Au/Ag-NPs) were evaluated for their prospective anticancer,

Inflammatory ascites formation induced by macromolecules in mice and rats.

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Different macromolecules were administered intraperitoneally to stimulate formation of protein-rich ascitic fluid in rodents. Stimulatory effect of plant lectins depended on the attachment to cell surface carbohydrates, Canavalia ensiformis (ConA) lectin was used in the majority of experiments. The
BACKGROUND Plant lectins have long been used in biomedical research as immunomodulators against tumor cells and microbial infections. OBJECTIVE To test the ability of plant lectins ConBr (Canavalia brasiliensis) and CFL (Cratylia argentea) to activate antimicrobial and immunomodulatory activities of
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