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Open AccessArticle

Hyaluronidases Have Strong Hydrolytic Activity toward Chondroitin 4-Sulfate Comparable to that for Hyaluronan

1
Laboratory of Proteoglycan Signaling and Therapeutics, Hokkaido University Graduate School of Life Science, Sapporo 001-0021, Japan
2
Department of Pathobiochemistry, Faculty of Pharmacy, Meijo University, Nagoya 468-8503, Japan
*
Author to whom correspondence should be addressed.
Biomolecules 2012, 2(4), 549-563; https://doi.org/10.3390/biom2040549
Received: 13 October 2012 / Revised: 22 October 2012 / Accepted: 8 November 2012 / Published: 12 November 2012
(This article belongs to the Special Issue Challenges in Glycan, Glycoprotein and Proteoglycan Research)
Chondroitin sulfate (CS) chains are involved in the regulation of various biological processes. However, the mechanism underlying the catabolism of CS is not well understood. Hyaluronan (HA)-degrading enzymes, the hyaluronidases, are assumed to act at the initial stage of the degradation process, because HA is similar in structure to nonsulfated CS, chondroitin (Chn). Although human hyaluronidase-1 (HYAL1) and testicular hyaluronidase (SPAM1) can degrade not only HA but also CS, they are assumed to digest CS to only a limited extent. In this study, the hydrolytic activities of HYAL1 and SPAM1 toward CS-A, CS-C, Chn, and HA were compared. HYAL1 depolymerized CS-A and HA to a similar extent. SPAM1 degraded CS-A, Chn, and HA to a similar extent. CS is widely distributed from very primitive organisms to humans, whereas HA has been reported to be present only in vertebrates with the single exception of a mollusk. Therefore, a genuine substrate of hyaluronidases appears to be CS as well as HA. View Full-Text
Keywords: 2AB: 2-aminobenzamide; Chn: chondroitin; CS: chondroitin sulfate; HA: hyaluronan; HPLC: high performance liquid chromatography 2AB: 2-aminobenzamide; Chn: chondroitin; CS: chondroitin sulfate; HA: hyaluronan; HPLC: high performance liquid chromatography
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Honda, T.; Kaneiwa, T.; Mizumoto, S.; Sugahara, K.; Yamada, S. Hyaluronidases Have Strong Hydrolytic Activity toward Chondroitin 4-Sulfate Comparable to that for Hyaluronan. Biomolecules 2012, 2, 549-563.

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