The novel lectin KM plus detects a specific subset of mannosyl-glycoconjugates in the rat cerebellum

dc.creatorTeixeira, SA
dc.creatorViapiano, MS
dc.creatorGaniko, L
dc.creatorRoque-Barreira, MC
dc.creatorMartins, AR
dc.date2003
dc.date2014-11-15T14:25:17Z
dc.date2015-11-26T16:11:39Z
dc.date2014-11-15T14:25:17Z
dc.date2015-11-26T16:11:39Z
dc.date.accessioned2018-03-28T23:00:08Z
dc.date.available2018-03-28T23:00:08Z
dc.identifierGlycoconjugate Journal. Kluwer Academic Publ, v. 20, n. 41858, n. 501, n. 508, 2003.
dc.identifier0282-0080
dc.identifierWOS:000223360600008
dc.identifier10.1023/B:GLYC.0000038296.79574.c8
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/77835
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/77835
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/77835
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1267139
dc.descriptionKM+ is a D(+) mannose-specific lectin with a carbohydrate structure-affinity relationship different from those of most mannose-binding lectins. KM+ elicits carbohydrate-dependent biological effects in several mammalian cell types, but it has not yet been employed as a probe for the detection of its specific ligands. We show here for the first time the screening and partial identification of cerebellar mannosyl-glycoconjugates recognized by KM+, by means of lectin-histochemistry and lectin-blotting. Biotinylated KM+ stained most cellular structures in the adult rat cerebellum, particularly Purkinje cells bodies and the surface of granule cells, but not cellular processes. Capillaries in the choroid plexus were also strongly decorated, while blood vessels in the cerebellar parenchyma remained unstained. D(+) mannose, but not D(+) galactose, abolished the staining of all cerebellar structures. Higher inhibitory potencies were found for mannosyl-glycans such as mannotriose (man-alpha1,3-[man-alpha1,6]-man) and the biantennary heptasaccharide carried by the enzyme horseradish peroxidase. After separation of cerebellar proteins by SDS-PAGE, KM+ recognized three major unidentified mannosylglycoproteins of 132, 83 and 49 kDa. KM+ also detected high-Mw bands corresponding to the light and heavy chains of Type-I laminin, but not a 160-kDa cleavage product of laminin. We conclude that KM+ binds preferentially to a specific subset of mannose-containing glycoproteins in cerebellar tissue, thus being much more restricted than other mannose-specific lectins. KM+ can be used as a novel probe to screen the central nervous system for this specific subset of complex mannosyl-glycoconjugates.
dc.description20
dc.description41858
dc.description501
dc.description508
dc.languageen
dc.publisherKluwer Academic Publ
dc.publisherDordrecht
dc.publisherHolanda
dc.relationGlycoconjugate Journal
dc.relationGlycoconjugate J.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectKM plus lectin
dc.subjectartocarpin
dc.subjectmannosyl-glycoconjugates
dc.subjectcerebellum
dc.subjectType-I laminin
dc.subjectArtocarpus-integrifolia
dc.subjectPostnatal-development
dc.subjectSoluble Lectin
dc.subjectPurkinje-cells
dc.subjectBinding
dc.subjectMaturation
dc.subjectGlycoproteins
dc.subjectGlycobiology
dc.subjectSynapse
dc.subjectRecognition
dc.titleThe novel lectin KM plus detects a specific subset of mannosyl-glycoconjugates in the rat cerebellum
dc.typeArtículos de revistas


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