Navegando por Palavras-chave "neutrophil haptotaxis"

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    Lectin KM+-induced neutrophil haptotaxis involves binding to laminin
    (Elsevier B.V., 2005-01-18) Ganiko, L.; Martins, A. R.; Freymuller, E.; Mortara, R. A.; Roque-Barreira, M. C.; Universidade de São Paulo (USP); Universidade Federal de São Paulo (UNIFESP)
    The lectin KM+ from Artocarpus integrifolia, also known as artocarpin, induces neutrophil migration by haptotaxis. the interactions of KM+ with both the extracellular matrix (ECM) and neutrophils depend on the lectin ability to recognize mannose-containing glycans. Here, we report the binding of KM+ to laminin and demonstrate that this interaction potentiates the KM+-induced neutrophil migration. Labeling of lung tissue by KM+ located its ligands on the endothelial cells, in the basement membrane, in the alveolus, and in the interstitial connective tissue. Such labeling was inhibited by 400 mM D-mannose, 10 mM Manalpha1-3[Manalpha1-6]Man or 10 muM peroxidase (a glycoprotein-containing mannosyl heptasaccharide). Laminin is a tissue ligand for KM+, since both KM+ and anti-laminin antibodies not only reacted with the same high molecular mass components of a lung extract, but also determined colocalized labeling in basement membranes of the lung tissue. the relevance of the KM+-laminin interaction to the KM+ property of inducing neutrophil migration was evaluated. the inability of low concentrations of soluble KM+ to induce human neutrophil migration was reversed by coating the microchamber filter with laminin. So, the interaction of KM+ with laminin promotes the formation of a substrate-bound KM+ gradient that is able to induce neutrophil haptotaxis. (C) 2004 Elsevier B.V. All rights reserved.