Show simple item record

dc.contributor.authorWolfenden, Mark
dc.contributor.authorCousin, Jonathan G.
dc.contributor.authorNangia-Makker, Pratima
dc.contributor.authorRaz, Avraham
dc.contributor.authorCloninger, Mary
dc.date.accessioned2015-10-16T21:20:53Z
dc.date.available2015-10-16T21:20:53Z
dc.date.issued2015-04
dc.identifier.citationWolfenden, Mark, Jonathan Cousin, Pratima Nangia-Makker, Avraham Raz, and Mary Cloninger. "Glycodendrimers and Modified ELISAs: Tools to Elucidate Multivalent Interactions of Galectins 1 and 3." Molecules 20, no. 4 (April 20, 2015): 7059-7096. DOI:https://dx.doi.org/10.3390/molecules20047059.en_US
dc.identifier.issn1420-3049
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/9328
dc.description.abstractMultivalent protein-carbohydrate interactions that are mediated by sugar-binding proteins, i.e., lectins, have been implicated in a myriad of intercellular recognition processes associated with tumor progression such as galectin-mediated cancer cellular migration/metastatic processes. Here, using a modified ELISA, we show that glycodendrimers bearing mixtures of galactosides, lactosides, and N-acetylgalactosaminosides, galectin-3 ligands, multivalently affect galectin-3 functions. We further demonstrate that lactose functionalized glycodendrimers multivalently bind a different member of the galectin family, i.e., galectin-1. In a modified ELISA, galectin-3 recruitment by glycodendrimers was shown to directly depend on the ratio of low to high affinity ligands on the dendrimers, with lactose-functionalized dendrimers having the highest activity and also binding well to galectin-1. The results depicted here indicate that synthetic multivalent systems and upfront assay formats will improve the understanding of the multivalent function of galectins during multivalent protein carbohydrate recognition/interaction.en_US
dc.description.sponsorshipNIH GM62444en_US
dc.rightsCC BY 4.0en_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/legalcodeen_US
dc.titleGlycodendrimers and Modified ELISAs: Tools to Elucidate Multivalent Interactions of Galectins 1 and 3en_US
dc.typeArticleen_US
mus.citation.extentfirstpage7059en_US
mus.citation.extentlastpage7096en_US
mus.citation.issue4en_US
mus.citation.journaltitleMoleculesen_US
mus.citation.volume20en_US
mus.identifier.categoryHealth & Medical Sciencesen_US
mus.identifier.categoryChemical & Material Science
mus.identifier.doi10.3390/molecules20047059en_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.universityMontana State University - Bozemanen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record

CC BY 4.0
Except where otherwise noted, this item's license is described as CC BY 4.0

MSU uses DSpace software, copyright © 2002-2017  Duraspace. For library collections that are not accessible, we are committed to providing reasonable accommodations and timely access to users with disabilities. For assistance, please submit an accessibility request for library material.