Hyaluronidases Have Strong Hydrolytic Activity toward Chondroitin 4-Sulfate Comparable to that for Hyaluronan
| العنوان: | Hyaluronidases Have Strong Hydrolytic Activity toward Chondroitin 4-Sulfate Comparable to that for Hyaluronan |
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| المؤلفون: | Kazuyuki Sugahara, Tomoyuki Kaneiwa, Tomoko Honda, Shuji Mizumoto, Shuhei Yamada |
| المصدر: | Biomolecules, Vol 2, Iss 4, Pp 549-563 (2012) Biomolecules; Volume 2; Issue 4; Pages: 549-563 Biomolecules |
| بيانات النشر: | MDPI AG, 2012. |
| سنة النشر: | 2012 |
| مصطلحات موضوعية: | 2AB: 2-aminobenzamide, CS: chondroitin sulfate, lcsh:QR1-502, hyaluronidase, Biochemistry, Article, lcsh:Microbiology, hyaluronan, chemistry.chemical_compound, Hydrolysis, glycosaminoglycan, Chondroitin, Chondroitin sulfate, Chn: chondroitin, HA: hyaluronan, HPLC: high performance liquid chromatography, Molecular Biology, chondroitin sulfate, chemistry.chemical_classification, Catabolism, Substrate (chemistry), Enzyme, chemistry, hydrolase, Testicular hyaluronidase, Chondroitin 4 sulfate |
| الوصف: | 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. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e19b2adef969d55719c52aeb097e8560 http://www.mdpi.com/2218-273X/2/4/549 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....e19b2adef969d55719c52aeb097e8560 |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |