Small leucine-rich repeat proteoglycans associated with mature insoluble elastin serve as binding sites for galectins

2017 Fiscal Year Final Research Report

• Project/Area Number: 15K06974
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Kagawa University
• Principal Investigator: Nishi Nozomu 香川大学, 総合生命科学研究センター, 准教授 (10145047)
• Co-Investigator(Renkei-kenkyūsha): NONAKA Yasuhiro 香川大学, 医学部, 助教 (50569217)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: galectin / elastin / oligosaccharide / SLRPs / lumican / mimecan / prolargin / fibromodulin

Outline of Final Research Achievements

We found that mature insoluble elastin is capable of binding Gal-9 and other members of the human galectin family. Lectin blot analysis of a series of commercial water-soluble elastin preparations, PES-(A) ~ PES-(E), revealed that only PES-(E) contained substances recognized by Gal-9. Gal-9-interacting substances in PES-(E) were affinity-purified, digested with trypsin and then analyzed by reversed-phase HPLC. Peptide fragments derived from five members of the small leucine-rich repeat proteoglycan family, versican, lumican, osteoglycin/mimecan, prolargin and fibromodulin, were identified by N-terminal amino acid sequence analysis. The results indicate that Gal-9 and possibly other galectins recognize glycans attached to small leucine-rich repeat proteoglycans associated with insoluble elastin and also indicate the possibility that mature insoluble elastin serves as an extracellular reservoir for galectins.

Free Research Field

生化学