Small leucine-rich repeat proteoglycans associated with mature insoluble elastin serve as binding sites for galectins
Small leucine-rich repeat proteoglycans associated with mature insoluble elastin serve as binding sites for galectins
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与成熟不溶性弹性蛋白相关的富含亮氨酸的小重复蛋白多糖作为半乳糖凝集素的结合位点
DOI:
10.1080/09168451.2017.1374828
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发表时间:
2017
期刊:
影响因子:
--
通讯作者:
N.
中科院分区:
文献类型:
--
作者:
Itoh;A.;Nonaka;Y.;Ogawa;T.;Nakamura;T.;Nishi;N.
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) ~ 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.