著者
Yu Teshigahara Ikuko Kakizaki Wataru Hirao Kanji Tanaka Ryoki Takahashi
出版者
The Japanese Society of Applied Glycoscience
雑誌
Journal of Applied Glycoscience (ISSN:13447882)
巻号頁・発行日
vol.67, no.2, pp.63-66, 2020-05-20 (Released:2020-05-20)
参考文献数
17
被引用文献数
2

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.