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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Life Science / Faculty of Advanced Life Science >
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Pathophysiological Significance of Dermatan Sulfate Proteoglycans Revealed by Human Genetic Disorders
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| Title: | Pathophysiological Significance of Dermatan Sulfate Proteoglycans Revealed by Human Genetic Disorders |
| Authors: | Mizumoto, Shuji Browse this author | | Kosho, Tomoki Browse this author | | Yamada, Shuhei Browse this author | | Sugahara, Kazuyuki Browse this author →KAKEN DB |
| Keywords: | biglycan | | carbohydrate sulfotransferase 14 | | decorin | | chondroitin sulfate | | dermatan sulfate | | dermatan sulfate epimerase | | dermatan 4-O-sulfotransferase | | Ehlers-Danlos syndrome | | glycosaminoglycan | | proteoglycan | | spondyloepimetaphyseal dysplasia |
| Issue Date: | Jun-2017 |
| Publisher: | MDPI |
| Journal Title: | Pharmaceuticals |
| Volume: | 10 |
| Issue: | 2 |
| Start Page: | 34 |
| Publisher DOI: | 10.3390/ph10020034 |
| Abstract: | The indispensable roles of dermatan sulfate-proteoglycans (DS-PGs) have been demonstrated in various biological events including construction of the extracellular matrix and cell signaling through interactions with collagen and transforming growth factor- , respectively. Defects in the core proteins of DS-PGs such as decorin and biglycan cause congenital stromal dystrophy of the cornea, spondyloepimetaphyseal dysplasia, and Meester-Loeys syndrome. Furthermore, mutations in human genes encoding the glycosyltransferases, epimerases, and sulfotransferases responsible for the biosynthesis of DS chains cause connective tissue disorders including Ehlers-Danlos syndrome and spondyloepimetaphyseal dysplasia with joint laxity characterized by skin hyperextensibility, joint hypermobility, and tissue fragility, and by severe skeletal disorders such as kyphoscoliosis, short trunk, dislocation, and joint laxity. Glycobiological approaches revealed that mutations in DS-biosynthetic enzymes cause reductions in enzymatic activities and in the amount of synthesized DS and also disrupt the formation of collagen bundles. This review focused on the growing number of glycobiological studies on recently reported genetic diseases caused by defects in the biosynthesis of DS and DS-PGs. |
| Rights: | http://creativecommons.org/licenses/by/4.0/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/67053 |
| 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: 菅原 一幸
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