Journal
GLYCOBIOLOGY
Volume 25, Issue 5, Pages 557-569Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwu186
Keywords
chondroitin sulfate; collagen; epiphycan; glycosaminoglycan; proteoglycan
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [23570157]
- Hirosaki University Grant for Exploratory Research by Young Scientists
- Sunstar Inc. (Takatsuki, Japan)
- Grants-in-Aid for Scientific Research [23570157] Funding Source: KAKEN
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Epiphycan (EPY) from salmon nasal cartilage has a glycosaminoglycan (GAG) domain that is heavily modified by chondroitin 4-sulfate and chondroitin 6-sulfate. The functional role of the GAG domain has not been investigated. The interaction of EPY with collagen was examined in vitro using surface plasmon resonance analysis. EPY was found to bind to type I collagen via clustered chondroitin sulfate (CS), while a single chain of CS was unable to bind. Types I, Ill, VII, VIII and X collagen showed high binding affinity with EPY, whereas types 11, IV, V, VI and IX showed low binding affinities. Chemical modification of lysine residues in collagen decreased the affinity with the clustered CS. These results suggest that lysine residues of collagen are involved in the interaction with the clustered CS, and the difference in lysine modification defines the binding affinity to EPY. The clustered CS was also involved in an inter-saccharide interaction, and formed self-associated EPY. CS of EPY promoted fibril formation of type I collagen.
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