Sequencing the Dermatan Sulfate Chain of Decorin
| Autor: | Fuming Zhang, I. Jonathan Amster, Toshihiko Toida, Hong Zhang, Jiana Duan, Yanlei Yu, Franklin E. Leach, Kyohei Higashi, Robert J. Linhardt |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Glycosylation Swine Decorin Glycoconjugate Dermatan Sulfate Biochemistry Article Catalysis Dermatan sulfate Glycomics 03 medical and health sciences chemistry.chemical_compound symbols.namesake Colloid and Surface Chemistry Animals Chondroitin sulfate Structural motif chemistry.chemical_classification General Chemistry Golgi apparatus carbohydrates (lipids) 030104 developmental biology chemistry symbols Algorithms |
| Zdroj: | Journal of the American Chemical Society. 139:16986-16995 |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/jacs.7b10164 |
| Popis: | Glycomics represents one of the last frontiers and most challenging in omic analysis. Glycosylation occurs in the endoplasmic reticulum and the Golgi organelle and its control is neither well-understood nor predictable based on proteomic or genomic analysis. One of the most structurally complex classes of glycoconjugates is the proteoglycans (PGs) and their glycosaminoglycan (GAG) side chains. Previously, our laboratory solved the structure of the chondroitin sulfate chain of the bikunin PG. The current study examines the much more complex structure of the dermatan sulfate GAG chain of decorin PG. By utilizing sophisticated separation methods followed by compositional analysis, domain mapping, and tandem mass spectrometry coupled with analysis by a modified genetic algorithm approach, the structural motif for the decorin dermatan sulfate chain was determined. This represents the second example of a GAG with a prominent structural motif, suggesting that the structural variability of this class of glycoconjugates is somewhat simpler than had been expected. |
| Databáze: | OpenAIRE |
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