학술논문
The galactose-binding lectin isolated from Bauhinia bauhinioides Mart seeds inhibits neutrophil rolling and adhesion via primary cytokines.
Document Type
Article
Author
Girão, Deysen Kerlla Fernandes Bezerra; Cavada, Benildo Sousa; Freitas Pires, Alana; Martins, Timna Varela; Franco, Álvaro Xavier; Morais, Cecília Mendes; Nascimento, Kyria Santiago do; Delatorre, Plinio; Silva, Helton Colares; Nagano, Celso Shiniti; Assreuy, Ana Maria Sampaio; Soares, Pedro Marcos Gomes
Source
Subject
Language
ISSN
0952-3499
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-β (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-β levels via the lectin domain. Copyright © 2015 John Wiley & Sons, Ltd. [ABSTRACT FROM AUTHOR]