Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9886169 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2005 | 12 Pages |
Abstract
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 Manα1-3[Manα1-6]Man or 10 μM 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.
Keywords
ECMArtocarpus integrifolia2-MEs.e.fMLPMIP-1αPECAM-1ICAMIL-8PMSFCRDPAGEMCP-1EHSHRPSDSPVPPBSDIC2-mercaptoethanolBSAbovine serum albuminEDTAEthylenediaminetetraacetic acidpolyacrylamide gel electrophoresisimmunoglobulin Interleukin-8analysis of varianceANOVAstandard error of the meancarbohydrate recognition domainsodium dodecyl sulfateFormyl-methionyl-leucyl-phenylalaninephenylmethylsulfonyl fluorideLamininLectinExtracellular matrixPhosphate-buffered salineintercellular adhesion moleculeAntibodyHorseradish peroxidaseMacrophage inflammatory protein-1αmonocyte chemoattractant protein-1polyvinylpyrrolidonedifferential interference contrast
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Authors
Luciane Ganiko, Antônio R. Martins, Edna Freymüller, Renato A. Mortara, Maria-Cristina Roque-Barreira,