文章基本信息

标题：A Chondroitin Sulfate Chain of Urinary Trypsin Inhibitor Enhances Protease Inhibitory Activity of the Core Protein
本地全文：下载
作者：Yu Teshigahara ; Ikuko Kakizaki ; Wataru Hirao 等
期刊名称：Journal of Applied Glycoscience
印刷版ISSN：1344-7882
电子版ISSN：1880-7291
出版年度：2020
卷号：67
期号：2
页码：63-66
DOI：10.5458/jag.jag.JAG-2019_0021
出版社：The Japanese Society of Applied Glycoscience
摘要：Human urinary trypsin inhibitor (UTI) is a proteoglycan composed of one core protein covalently linked to one glycosaminoglycan, which is a low sulfated chondroitin 4-sulfate. It is used as an anti-inflammatory medicine based on the protease inhibitory activity of the core protein. However, functions of the chondroitin sulfate have not been clarified. Recently, we succeeded in remodeling the UTI chondroitin sulfate to hyaluronan to create hyaluronan hybrid UTI, without changing the core protein. Here, we investigated the effect of the remodeled chondroitin sulfate on the activities of serine proteases. Native UTI showed stronger protease inhibitory activity than hyaluronan hybrid UTI or hydrolyzed glycosaminoglycan UTI. Chondroitin 4-sulfate chains with a small peptide derived from the native UTI did not show any protease inhibitory activity. These results suggest that the chondroitin sulfate chain linked covalently to core protein enhances protease inhibitor activity of UTI although the chondroitin sulfate chain itself does not.
关键词：urinary trypsin inhibitor;glycosaminoglycan;chondroitin sulfate;hyaluronan;serine protease;hyaluronidase