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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Life Science / Faculty of Advanced Life Science >
Peer-reviewed Journal Articles, etc >
Synthetic Mucin-Like Glycopeptides as Versatile Tools to Measure Effects of Glycan Structure/Density/Position on the Interaction with Adhesion/Growth-Regulatory Galectins in Arrays
| Title: | Synthetic Mucin-Like Glycopeptides as Versatile Tools to Measure Effects of Glycan Structure/Density/Position on the Interaction with Adhesion/Growth-Regulatory Galectins in Arrays |
| Authors: | Artigas, Gerard Browse this author | | Hinou, Hiroshi Browse this author →KAKEN DB | | Garcia-Martin, Fayna Browse this author | | Gabius, Hans-Joachim Browse this author | | Nishimura, Shin-Ichiro Browse this author →KAKEN DB |
| Keywords: | agglutinin | | glycoproteins | | glycosylation | | lectin | | TF antigen |
| Issue Date: | 3-Jan-2017 |
| Publisher: | Wiley-Blackwell |
| Journal Title: | Chemistry-an asian journal |
| Volume: | 12 |
| Issue: | 1 |
| Start Page: | 159 |
| End Page: | 167 |
| Publisher DOI: | 10.1002/asia.201601420 |
| PMID: | 27873468 |
| Abstract: | Functional pairing of cellular glycoconjugates with tissue lectins is a highly selective process, whose determinative factors have not yet been fully delineated. Glycan structure and modes of presentation, that is, its position and density, can contribute to binding, as different members of a lectin family can regulate degrees of responsiveness to these factors. Using a peptide repeat sequence motif of the glycoprotein mucin-1, the principle of introducing synthetic (glyco) peptides with distinct variations in these three parameters to an array-based screening of tissue lectins is illustrated. Interaction profiles of seven adhesion/growth-regulatory galectins cover the range from intense signals with core 2 pentasaccharides and core 1 binding for galectins-3 and -5 to a lack of binding for galectin-1 and also the galectin-related protein, which was included as a negative control. Remarkably, the two tandem-repeat-type galectins-4 and -8 were distinguished by core 1 sialylation, as the two separated domains were. These results encourage further synthetic elaboration of the glycopeptide library and testing of the network of natural galectins and rationally engineered variants of the lectins. |
| Rights: | This is the peer reviewed version of the following article: G. Artigas, H. Hinou, F. Garcia-Martin, H.-J. Gabius, S.-I. Nishimura, Synthetic Mucin-Like Glycopeptides as Versatile Tools to Measure Effects of Glycan Structure/Density/Position on the Interaction with Adhesion/Growth-Regulatory Galectins in Arrays, Chem. Asian J. 2017, 12, 159-167, which has been published in final form at 10.1002/asia.201601420. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/68039 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 比能 洋
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