Abstract: 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.
Keywords: 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.
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(4):549-563.
Honda, Tomoko; Kaneiwa, Tomoyuki; Mizumoto, Shuji; Sugahara, Kazuyuki; Yamada, Shuhei. 2012. "Hyaluronidases Have Strong Hydrolytic Activity toward Chondroitin 4-Sulfate Comparable to that for Hyaluronan." Biomolecules 2, no. 4: 549-563.