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A Biologically Active Sequence of the Laminin alpha 2 Large Globular 1 Domain Promotes Cell Adhesion through Syndecan-1 by Inducing Phosphorylation and Membrane Localization of Protein Kinase C delta
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jung, Sung Youn | - |
dc.contributor.author | Kim, Jin-Man | - |
dc.contributor.author | Jang, Da Hyun | - |
dc.contributor.author | Kang, Hyun Ki | - |
dc.contributor.author | Min, Byung-Moo | - |
dc.date.accessioned | 2013-01-14T06:02:52Z | - |
dc.date.available | 2013-01-14T06:02:52Z | - |
dc.date.issued | 2009-11-13 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, Vol.284, No.46, pp.31764-31775 | ko_KR |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://hdl.handle.net/10371/80384 | - |
dc.description.abstract | Laminin-2 promotes basement membrane assembly and peripheral myelinogenesis; however, a receptor-binding motif within laminin-2 and the downstream signaling pathways for motif-mediated cell adhesion have not been fully established. The human laminin-2 alpha 2 chain cDNAs cloned from human keratinocytes and fibroblasts correspond to the laminin alpha 2 chain variant sequence from the human brain. Individually expressed recombinant large globular (LG) 1 protein promotes cell adhesion and has heparin binding activities. Studies with synthetic peptides delineate the DLTIDDSYWYRI motif (Ln2-P3) within the LG1 as a major site for both heparin and cell binding. Cell adhesion to LG1 and Ln2-P3 is inhibited by treatment of heparitinase I and chondroitinase ABC. Syndecan-1 from PC12 cells binds to LG1 and Ln2-P3 and colocalizes with both molecules. Suppression of syndecan-1 with RNA interference inhibits cell adhesion to LG1 and Ln2-P3. The binding of syndecan-1 with LG1 and Ln2-P3 induces the recruitment of protein kinase C delta (PKC delta) into the membrane and stimulates its tyrosine phosphorylation. A decrease in PKC delta activity significantly reduces cell adhesion to LG1 and Ln2-P3. Taken together, these results indicate that the Ln2-P3 motif and LG1 domain, containing the motif, within the human laminin-2 alpha 2 chain are major ligands for syndecan-1, which mediates cell adhesion through the PKC delta signaling pathway. | ko_KR |
dc.description.sponsorship | This work was supported by grants from the Korea Science and Engineering Foundation through the Intellectual Biointerface Engineering Center at Seoul National University (to B.-M. M.). | - |
dc.language.iso | en | ko_KR |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | ko_KR |
dc.title | A Biologically Active Sequence of the Laminin alpha 2 Large Globular 1 Domain Promotes Cell Adhesion through Syndecan-1 by Inducing Phosphorylation and Membrane Localization of Protein Kinase C delta | ko_KR |
dc.type | Article | ko_KR |
dc.contributor.AlternativeAuthor | 정성윤 | - |
dc.contributor.AlternativeAuthor | 김진만 | - |
dc.contributor.AlternativeAuthor | 장다현 | - |
dc.contributor.AlternativeAuthor | 강현기 | - |
dc.contributor.AlternativeAuthor | 민병무 | - |
dc.identifier.doi | 10.1074/jbc.M109.038547 | - |
dc.citation.journaltitle | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.description.tc | 3 | - |
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