著者
Ikuko Kakizaki Yoji Kato
出版者
The Japanese Society of Applied Glycoscience
雑誌
Journal of Applied Glycoscience (ISSN:13447882)
巻号頁・発行日
pp.jag.JAG-2021_0016, (Released:2022-03-18)

Over the past 10 years, many products utilizing the functionality of salmon cartilage proteoglycan have come on the market, and consumer awareness of proteoglycan has increased. During this period, the biggest issue has been how to evaluate the amount and quality of proteoglycan in the cartilage extract blended in the products. In this study, we propose an immunological method that can easily evaluate the amount and quality of proteoglycan in the proteoglycan-containing compositions. By the present method, it is possible to evaluate not only the retention of the functional domains of the core protein of proteoglycan, but also that of chondroitin sulfate chains linked to the core protein. Furthermore, the binding activity of proteoglycan to hyaluronan can be evaluated if hyaluronan is used as a probe instead of an antibody. This method is expected to be useful for proteoglycan quality evaluation during the manufacturing process and product storage.
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.