dc.contributorUniversidade de São Paulo (USP)
dc.contributorUniversidade Federal de São Paulo (UNIFESP)
dc.creatorGaniko, L.
dc.creatorMartins, A. R.
dc.creatorFreymuller, E.
dc.creatorMortara, R. A.
dc.creatorRoque-Barreira, M. C.
dc.date.accessioned2016-01-24T12:37:36Z
dc.date.accessioned2022-10-07T20:51:42Z
dc.date.available2016-01-24T12:37:36Z
dc.date.available2022-10-07T20:51:42Z
dc.date.created2016-01-24T12:37:36Z
dc.date.issued2005-01-18
dc.identifierBiochimica Et Biophysica Acta-general Subjects. Amsterdam: Elsevier B.V., v. 1721, n. 1-3, p. 152-163, 2005.
dc.identifier0304-4165
dc.identifierhttp://repositorio.unifesp.br/handle/11600/28115
dc.identifier10.1016/j.bbagen.2004.10.012
dc.identifierWOS:000226422500018
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/4023978
dc.description.abstractThe 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.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBiochimica Et Biophysica Acta-general Subjects
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.rightsAcesso restrito
dc.subjectlectin
dc.subjectArtocarpus integrifolia
dc.subjectneutrophil haptotaxis
dc.subjectextracellular matrix
dc.subjectlaminin
dc.subjecthaptotactic gradient
dc.titleLectin KM+-induced neutrophil haptotaxis involves binding to laminin
dc.typeArtigo


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