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Sivu 1 alkaen 142 tuloksia
Vatairea macrocarpa lectin induces paw edema with leukocyte infiltration.
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A lectin from Vatairea macrocarpa (Vmac) seeds was investigated in a model of paw edema in rats and the possible involvement of leukocytes. Vmac (200 and 400 microg/paw, s.c.) induced a significant time- and dose-dependent paw edema, with leukocyte infiltration, which was drastically reduced in
Neutrophil-infiltrated paw edema induced by mannose-binding Dioclea violacea lectin.
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BACKGROUND
The potential edematogenic effect and the pharmacological characterization of a glucose-mannose-binding lectin from Dioclea violacea (DvL) were investigated.
METHODS
Paw edema was induced with DvL in control animals, and in animals pretreated with glucocorticoid or with blockers of
Rat paw edema and leukocyte immigration induced by plant lectins.
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Lectins from Dioclea grandiflora (DG) and Canavalia brasiliensis (CB) were compared with Concanavalin A (ConA) for their ability to induce paw edema and peritoneal cell immigration in rats. ConA caused a slight edema with a peak at 1 h after injection, while DG or CB induced a pronounced and
Protein crystal content analysis by mass spectrometry and preliminary X-ray diffraction of a lectin from Canavalia grandiflora seeds with modulatory role in 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 analysis, molecular docking and molecular dynamics of an edematogenic lectin from Centrolobium microchaete seeds.
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Lectins represent a class of proteins or glycoproteins capable of reversibly binding to carbohydrates. Seed lectins from the Dalbergieae tribe (Leguminosae) have structural variability, carbohydrate specificity, and biological effects, such as inflammation, vasorelaxation and cancer antigen binding.
Prevention of cyclophosphamide-induced hemorrhagic cystitis by glucose-mannose binding plant lectins.
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OBJECTIVE
Neutrophils are implicated in the physiopathologic alterations of hemorrhagic cystitis (HC). Thus, we decided to test the antiinflammatory activity of glucose-mannose binding lectins extracted from D. violacea and D. guianensis seeds, which showed an inhibitory effect upon neutrophil
Utilization of lectin-histochemistry in forensic neuropathology: lectin staining provides useful information for postmortem diagnosis in forensic neuropathology.
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We have investigated the deposition of glycoconjugates in human brain tissue with or without brain disorders. In this review we describe the application of lectin-histochemistry techniques to forensic neuropathology. Lectin staining is able to reveal several kinds of carbohydrate-related depositions
Purification and molecular characterization of a novel mannose-specific lectin from Dioclea reflexa hook seeds with inflammatory activity.
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A novel lectin present in Dioclea reflexa seeds (DrfL) was discovered and described in this study. DrfL was purified in a single step by affinity chromatography in a Sephadex G-50 column. The lectin strongly agglutinated rabbit erythrocytes and was inhibited by α-methyl-D-mannoside, D-mannose, and
A novel N-acetyl-glucosamine lectin of Lonchocarpus araripensis attenuates acute cellular inflammation in mice.
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OBJECTIVE
This study had investigated the anti-inflammatory activity of a seed lectin (LAL) isolated from Lonchocarpus araripensis.
METHODS
LAL was purified by affinity chromatography (chitin column) and ion exchange chromatography (DEAE-Sephacel). In vitro LAL was tested for hemagglutinating
Purification and biological activities of Abelmoschus esculentus seed lectin.
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The Abelmoschus esculentus (Malvaceae) plant originated in Africa and has spread across a number of tropic countries, including northeastern Brazil. The plant has been used to treat various disorders, such as cancer, microbial infections, hypoglycemia, constipation, urine retention and inflammation.
Inhibitory effect of Lonchocarpus araripensis lectin in rat acute models of inflammation.
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Dalbergieae tribe lectins, possessing binding affinity for galactose and mannose, present inflammatory and nociceptive effects, while those for N-acetylglucosamine are anti-inflammatory. Since the anti-inflammatory effect of the seed lectin of L. araripensis (LAL) had been already demonstrated in
Healing activity induced by Cramoll 1,4 lectin in healthy and immunocompromised mice.
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Cramoll 1,4 is a lectin extracted from seeds of Cratylia mollis Mart. Many assays have shown the cytokine release activity and pro-inflammatory profile of this lectin. Here, we used Cramoll 1,4 in the treatment of cutaneous wounds in normal and immunocompromised mice for available your cicatricial
Molecular modeling, docking and dynamics simulations of the Dioclea lasiophylla Mart. Ex Benth seed lectin: An edematogenic and hypernociceptive protein.
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Lectins are proteins, or glycoproteins, capable of reversibly binding to specific mono- or oligosaccharides via a noncatalytic domain. The Diocleinae subtribe presents lectins with high structural similarity, but different effects based on biological activity assays. This variability results from
An anti-inflammatory lectin from Luetzelburgia auriculata seeds inhibits adhesion and rolling of leukocytes and modulates histamine and PGE2 action in acute inflammation models.
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OBJECTIVE
To study and characterize the in vivo effect of the lectin from Luetzelburgia auriculata seed on acute inflammation models.
METHODS
The lectin was purified from the crude saline extract by affinity chromatography on a guar-gum matrix. Native, heat-treated, and digested lectin was evaluated
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