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Updated: Dec 2, 2025

Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining
Published on: February 25, 2021
Essential hyaluronan structure for binding with hyaluronan-binding protein (HABP) determined by glycotechnological
Shinichiro Suto1, Ikuko Kakizaki1, Yota Tatara2
1Department of Glycotechnology, Center for Advanced Medical Research, Hirosaki University Graduate School of Medicine, Hirosaki, Japan; Department of Glycobiomedicine, Hirosaki University Graduate School of Medicine, Hirosaki, Japan.
Abstract:
Hyaluronan specifically binds to aggrecan globular domain 1, which is often referred to as just hyaluronan binding protein (HABP), however, the hyaluronan carbohydrate structure recognized by HABP had not been studied in detail. The aim of the present study was to investigate the important structure of hyaluronan for binding to HABP. We prepared hybrid oligosaccharides from hyaluronan and chondroitin, with or without modification of the reducing or non-reducing terminus, as tools to determine the preferred structure of hyaluronan for binding to the HABP by a competitive ELISA-like method. The non-reducing terminal structure was critical, especially, the glucuronic acid (GlcUA) and N-acetylglucosamine (GlcNAc) of the hyaluronan-unit are essential for complete HABP binding activity, and for any HABP binding activity, respectively. It is possible to replace GlcUAβ-1-3GlcNAc of the internal disaccharide units with GlcUAβ-1-3N-acetylgalactosamine (GalNAc), if the chain length is decasaccharide or larger.
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