Sequence analysis and domain motifs in the decorin glycosaminoglycan chain

Authors
Zhao, Xue
Yang, Bo
Solakyildirim, Kemal
Joo, Eun Ji
Toida, Toshihiko
Higashi, Kyohei
Linhardt, Robert J.
Li, Lingyun
ORCID
https://orcid.org/0000-0003-2219-5833
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Issue Date
2013-10-11
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Terms of Use
Attribution 3.0 United States
CC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
Full Citation
Sequence analysis and domain motifs in the decorin glycosaminoglycan chain, X. Zhao, B. Yang, K. Solakylidirim, E.-J. Joo, T. Toida, K. Higashi, R. J. Linhardt, L. Li, Journal of Biological Chemistry, 288, 9226-9237, 2013.
Abstract
Decorin proteoglycan is comprised of a core protein containing a single O-linked dermatan sulfate/chondroitin sulfate glycosaminoglycan (GAG) chain. Although the sequence of the decorin core protein is determined by the gene encoding its structure, the structure of its GAG chain is determined in the Golgi. The recent application of modern MS to bikunin, a far simpler chondroitin sulfate proteoglycans, suggests that it has a single or small number of defined sequences. On this basis, a similar approach to sequence the decorin of porcine skin much larger and more structurally complex dermatan sulfate/chondroitin sulfate GAG chain was undertaken. This approach resulted in information on the consistency/variability of its linkage region at the reducing end of the GAG chain, its iduronic acid-rich domain, glucuronic acid-rich domain, and non-reducing end. A general motif for the porcine skin decorin GAG chain was established. A single small decorin GAG chain was sequenced using MS/MS analysis. The data obtained in the study suggest that the decorin GAG chain has a small or a limited number of sequences.
Description
Journal of Biological Chemistry, 288, 9226-9237
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
The American Society for Biochemistry and Molecular Biology (ASBMB) and Elsevier
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Journal of Biological Chemistry
https://harc.rpi.edu/
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A full text version is available in DSpace@RPI
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