https://scholars.lib.ntu.edu.tw/handle/123456789/143985
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.author | Kawasaki, Nobuko | en |
dc.contributor.author | Lin, Chia-Wei | en |
dc.contributor.author | Inoue, Risa | en |
dc.contributor.author | Khoo, Kay-Hooi | en |
dc.contributor.author | Kawasaki, Nana | en |
dc.contributor.author | Ma, Bruce Yong | en |
dc.contributor.author | Oka, Shogo | en |
dc.contributor.author | Ishiguro, Masaji | en |
dc.contributor.author | Sawada, Toshihiko | en |
dc.contributor.author | Ishida, Hideharu | en |
dc.contributor.author | Hashimoto, Tomohiro | en |
dc.contributor.author | Kawasaki, Toshisuke | en |
dc.creator | Kawasaki, Nobuko; Lin, Chia-Wei; Inoue, Risa; Khoo, Kay-Hooi; Kawasaki, Nana; Ma, Bruce Yong; Oka, Shogo; Ishiguro, Masaji; Sawada, Toshihiko; Ishida, Hideharu; Hashimoto, Tomohiro; Kawasaki, Toshisuke | en |
dc.date | 2009 | en |
dc.date.accessioned | 2009-08-05T06:41:34Z | - |
dc.date.accessioned | 2018-07-06T06:27:05Z | - |
dc.date.available | 2009-08-05T06:41:34Z | - |
dc.date.available | 2018-07-06T06:27:05Z | - |
dc.date.issued | 2009 | - |
dc.identifier.uri | http://ntur.lib.ntu.edu.tw//handle/246246/163321 | - |
dc.description.abstract | The serum mannan-binding protein (MBP) is a host defense C-type lectin specific for mannose, N-acetylglucosamine, and fucose residues, and exhibits growth inhibitory activity toward human colorectal carcinoma cells. The MBP-ligand oligosaccharides (MLO) isolated from a human colorectal carcinoma cell line, SW1116, are large, multiantennary N-glycans with highly fucosylated polylactosamine-type structures having Leb Lea or tandem repeats of the Lea structure at their nonreducing ends. In this study, we isolated the major MBP-ligand glycoproteins from SW1116 cell lysates with an MBP column and identified them as CD26/dipeptidyl peptidase IV (DPPIV) (110 kDa) and CD98 heavy chain (CD98hc)/4F2hc (82 kDa). Glycosidase digestion revealed that CD26 contained such complex-type N-glycans that appear to mediate the MBP binding. MALDI-MS of the N-glycans released from CD26 by PNGase F demonstrated conclusively that CD26 is the major MLO-carrying protein. More interestingly, a comparison of the N-glycans released from the MBP-binding and non-MBP-binding glycopeptides suggested that complex-type N-glycans carrying a minimum of 4 Lea/ Leb epitopes arranged either as multimeric tandem repeats or terminal epitopes on multiantennary structures are critically important for the high affinity binding to MBP. Analysis of the N-glycan attachment sites demonstrated that the high affinity MLO was expressed preferentially at some N-glycosylation sites, but this site preference was not so stringent. Finally, hypothetical 3D models of tandem repeats of the Lea epitope and the MBP-Lewis oligosaccharide complex were presented. ? The Author 2009. Published by Oxford University Press. All rights reserved. | - |
dc.language.iso | en_US | - |
dc.relation | Glycobiology 19 (4): 437-450 | en |
dc.relation.ispartof | Glycobiology | en_US |
dc.subject | CD26; Lea epitope; Mannan-binding lectin; Mannan-binding protein; SW1116 | - |
dc.subject.classification | [SDGs]SDG3 | - |
dc.subject.other | CD98 antigen; dipeptidyl peptidase IV; glycan; glycosidase; ligand; mannan binding lectin; antigen specificity; article; binding affinity; cancer cell culture; colorectal carcinoma; controlled study; enzyme metabolism; epitope mapping; human; human cell; ligand binding; molecular weight; priority journal; protein analysis; protein expression; protein function; protein glycosylation; protein isolation; protein localization; protein structure; tandem repeat; Antigens, CD26; Antigens, CD98 Heavy Chain; Cell Line, Tumor; Colorectal Neoplasms; Epitopes; Fucose; Glycosylation; Humans; Ligands; Mannose-Binding Lectin; Models, Molecular; Neoplasm Proteins; Oligosaccharides; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; Structure-Activity Relationship | - |
dc.title | Highly fucosylated N-glycan ligands for mannan-binding protein expressed specifically on CD26 (DPPVI) isolated from a human colorectal carcinoma cell line, SW1116 | en |
dc.identifier.doi | 10.1093/glycob/cwn158 | - |
dc.relation.pages | 437-450 | - |
item.fulltext | no fulltext | - |
item.languageiso639-1 | en_US | - |
item.grantfulltext | none | - |
顯示於: | 生化科學研究所 |
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