期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 81, 期 11, 页码 2098-2104出版社
TAYLOR & FRANCIS LTD
DOI: 10.1080/09168451.2017.1374828
关键词
galectin; elastin; small leucine-rich repeat proteoglycan (SLRP); extracellular matrix (ECM)
类别
资金
- Ministry of Education, Culture, Sports, Science and Technology, Japan [15K06974]
- Grants-in-Aid for Scientific Research [15K06974] Funding Source: KAKEN
We previously reported that galectin-9 (Gal-9), an immunomodulatory animal lectin, could bind to insoluble collagen preparations and exerted direct cytocidal effects on immune cells. In the present study, 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) similar to 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.
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