| http://purl.uniprot.org/citations/11971863 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11971863 | http://www.w3.org/2000/01/rdf-schema#comment | "Human galectin-9 is a beta-galactoside-binding protein consisting of two carbohydrate recognition domains (CRDs) and a linker peptide. We have shown that galectin-9 represents a novel class of eosinophil chemoattractants (ECAs) produced by activated T cells. A previous study demonstrated that the carbohydrate binding activity of galectin-9 is indispensable for eosinophil chemoattraction and that the N- and C-terminal CRDs exhibit comparable ECA activity, which is substantially lower than that of full-length galectin-9. In this study, we investigated the roles of the two CRDs in ECA activity in conjunction with the sugar-binding properties of the CRDs. In addition, to address the significance of the linker peptide structure, we compare the three isoforms of galectin-9, which only differ in the linker peptide region, in terms of ECA activity. Recombinant proteins consisting of two N-terminal CRDs (galectin-9NN), two C-terminal CRDs (galectin-9CC), and three isoforms of galectin-9 (galectin-9S, -9M, and -9L) were generated. All the recombinant proteins had hemagglutination activity comparable to that of the predominant wild-type galectin-9 (galectin-9M). Galectin-9NN and galectin-9CC induced eosinophil chemotaxis in a manner indistinguishable from the case of galectin-9M. Although the isoform of galectin-9 with the longest linker peptide, galectin-9L, exhibited limited solubility, the three isoforms showed comparable ECA activity over the concentration range tested. The interactions between N- and C-terminal CRDs and glycoprotein glycans and glycolipid glycans were examined using frontal affinity chromatography. Both CRDs exhibited high affinity for branched complex type sugar chain, especially for tri- and tetraantennary N-linked glycans with N-acetyllactosamine units, and the oligosaccharides inhibited the ECA activity at low concentrations. These results suggest that the N- and C-terminal CRDs of galectin-9 interact with the same or a closely related ligand on the eosinophil membrane when acting as an ECA and that ECA activity does not depend on a specific structure of the linker peptide."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.org/dc/terms/identifier | "doi:10.1093/glycob/12.3.191"xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/author | "Hata Y."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/author | "Hirabayashi J."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/author | "Nakamura T."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/author | "Sato M."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/author | "Seki M."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/author | "Suzuki S."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/author | "Shoji H."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/author | "Nishi N."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/author | "Hirashima M."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/author | "Hashidate T."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/author | "Kasai Ki K."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/name | "Glycobiology"xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/pages | "191-197"xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/title | "Functional analysis of the carbohydrate recognition domains and a linker peptide of galectin-9 as to eosinophil chemoattractant activity."xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://purl.uniprot.org/core/volume | "12"xsd:string |
| http://purl.uniprot.org/citations/11971863 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11971863 |
| http://purl.uniprot.org/citations/11971863 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11971863 |
| http://purl.uniprot.org/uniprot/#_J3KSY2-mappedCitation-11971863 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11971863 |
| http://purl.uniprot.org/uniprot/#_Q6DKI2-mappedCitation-11971863 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11971863 |
| http://purl.uniprot.org/uniprot/Q6DKI2 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11971863 |
| http://purl.uniprot.org/uniprot/J3KSY2 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11971863 |