Sequence Analysis and Domain Motifs in the Porcine Skin Decorin Glycosaminoglycan Chain


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ZHAO X., Yang B., Solakylidirim K., Joo E. J. , Toida T., Higashi K., ...More

JOURNAL OF BIOLOGICAL CHEMISTRY, vol.288, no.13, pp.9226-9237, 2013 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 288 Issue: 13
  • Publication Date: 2013
  • Doi Number: 10.1074/jbc.m112.437236
  • Journal Name: JOURNAL OF BIOLOGICAL CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.9226-9237
  • Erzincan Binali Yildirim University Affiliated: No

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.