title: Chondroitin sulfate cluster of epiphycan from salmon nasal cartilage defines binding specificity to collagens.
abstract: 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, III, VII, VIII and X collagen showed high binding affinity with EPY, whereas types II, 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.
authors.affiliation: Department of Glycotechnology, Center for Advanced Medical Research, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan Department of Glycobiomedicine, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan ytatara@cc.hirosaki-u.ac.jp.
authors.forename: Yota
authors.initials: Y
authors.lastname: Tatara
authors.affiliation: Department of Glycotechnology, Center for Advanced Medical Research, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan Department of Glycobiomedicine, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan.
authors.forename: Ikuko
authors.initials: I
authors.lastname: Kakizaki
authors.affiliation: Department of Glycotechnology, Center for Advanced Medical Research, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan Department of Glycobiomedicine, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan.
authors.forename: Shinichiro
authors.initials: S
authors.lastname: Suto
authors.affiliation: Department of Glycotechnology, Center for Advanced Medical Research, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan Department of Glycobiomedicine, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan.
authors.forename: Haruna
authors.initials: H
authors.lastname: Ishioka
authors.affiliation: Department of Glycotechnology, Center for Advanced Medical Research, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan Department of Glycobiomedicine, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan.
authors.forename: Mika
authors.initials: M
authors.lastname: Negishi
authors.affiliation: Department of Glycobiomedicine, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan.
authors.forename: Masahiko
authors.initials: M
authors.lastname: Endo
mesh_terms: D000818:Animals; D002809:Chondroitin Sulfates / Q000378:metabolism*; D003094:Collagen / Q000378:metabolism*; D055171:Nasal Cartilages / Q000378:metabolism*; D011485:Protein Binding; D011509:Proteoglycans / Q000378:metabolism*; D012474:Salmon
chemical_list: D011509:Proteoglycans; D002809:Chondroitin Sulfates; D003094:Collagen
keywords: chondroitin sulfate; collagen; epiphycan; glycosaminoglycan; proteoglycan