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J Mol Recognit ; 28(5): 285-92, 2015 May.
Article in English | MEDLINE | ID: mdl-25706245

ABSTRACT

In this study, the amino acid sequence and anti-inflammatory effect of Bauhinia bauhinioides (BBL) lectin were evaluated. Tandem mass spectrometry revealed that BBL possesses 86 amino acid residues. BBL (1 mg/kg) intravenously injected in rats 30 min prior to inflammatory stimuli inhibited the cellular edema induced by carrageenan in only the second phase (21% - 3 h, 19% - 4 h) and did not alter the osmotic edema induced by dextran. BBL also inhibited carrageenan peritoneal neutrophil migration (51%), leukocyte rolling (58%) and adhesion (68%) and the neutrophil migration induced by TNF-α (64%). These effects were reversed by the association of BBL with galactose, demonstrating that the carbohydrate-binding domain is essential for lectin activity. In addition, BBL reduced myeloperoxidase activity (84%) and TNF-α (68%) and IL1-ß (47%) levels. In conclusion, the present investigation demonstrated that BBL contains highly homologous isolectins, resulting in a total of 86 amino acid residues, and exhibits anti-inflammatory activity by inhibiting neutrophil migration by reducing TNF-α and IL1-ß levels via the lectin domain.


Subject(s)
Anti-Inflammatory Agents/pharmacology , Bauhinia/chemistry , Galectins/pharmacology , Neutrophils/physiology , Plant Extracts/pharmacology , Plant Lectins/pharmacology , Amino Acid Sequence , Animals , Anti-Inflammatory Agents/chemistry , Cell Adhesion , Cytokines/physiology , Drug Evaluation, Preclinical , Galectins/chemistry , Leukocyte Rolling , Molecular Sequence Data , Neutrophils/drug effects , Peritonitis/immunology , Plant Extracts/chemistry , Plant Lectins/chemistry , Rats, Wistar , Seeds/chemistry
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