http://purl.uniprot.org/citations/17623663 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17623663 | http://www.w3.org/2000/01/rdf-schema#comment | "The syndecans comprise a family of cell surface heparan sulfate proteoglycans exhibiting complex biological functions involving the interaction of heparan sulfate side chains with a variety of soluble and insoluble heparin-binding extracellular ligands. Here we demonstrate an inverse correlation between the expression level of syndecan-2 and the metastatic potential of three clones derived from Lewis lung carcinoma 3LL. This correlation was proved to be a causal relationship, because transfection of syndecan-2 into the higher metastatic clone resulted in the suppression of both spontaneous and experimental metastases to the lung. Although the expression levels of matrix metalloproteinase-2 (MMP-2) and its cell surface activators, such as membrane-type 1 matrix metalloproteinase and tissue inhibitor of metalloproteinase-2, were similar regardless of the metastatic potentials of the clones, elevated activation of MMP-2 was observed in the higher metastatic clone. Removal of heparan sulfate from the cell surface of low metastatic cells by treatment with heparitinase-I promoted MMP-2 activation, and transfection of syndecan-2 into highly metastatic cells suppressed MMP-2 activation. Furthermore, transfection of mutated syndecan-2 lacking glycosaminoglycan attachment sites into highly metastatic cells did not have any suppressive effect on MMP-2 activation, suggesting that this suppression was mediated by the heparan sulfate side chains of syndecan-2. Actually, MMP-2 was found to exhibit a strong binding ability to heparin, the dissociation constant value being 62 nM. These results indicate a novel function of syndecan-2, which acts as a suppressor for MMP-2 activation, causing suppression of metastasis in at least the metastatic system used in the present study."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m609812200"xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/author | "Koyama Y."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/author | "Nakanishi H."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/author | "Miyazaki K."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/author | "Nishiyama A."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/author | "Ishimaru T."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/author | "Oguri K."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/author | "Munesue S."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/author | "Kusano Y."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/author | "Okayama M."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/author | "Yoshitomi Y."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/author | "Miyaura S."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/pages | "28164-28174"xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/title | "A novel function of syndecan-2, suppression of matrix metalloproteinase-2 activation, which causes suppression of metastasis."xsd:string |
http://purl.uniprot.org/citations/17623663 | http://purl.uniprot.org/core/volume | "282"xsd:string |
http://purl.uniprot.org/citations/17623663 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17623663 |
http://purl.uniprot.org/citations/17623663 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17623663 |
http://purl.uniprot.org/uniprot/#_E9PBI9-mappedCitation-17623663 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17623663 |
http://purl.uniprot.org/uniprot/#_A0A1B0GS88-mappedCitation-17623663 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17623663 |
http://purl.uniprot.org/uniprot/#_B4DQ56-mappedCitation-17623663 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17623663 |
http://purl.uniprot.org/uniprot/#_P34741-mappedCitation-17623663 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17623663 |