| http://purl.uniprot.org/citations/17170110 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17170110 | http://www.w3.org/2000/01/rdf-schema#comment | "Hyaluronic acid (HA) is a high molecular weight glycosaminoglycan involved in a wide variety of cellular functions. However, its turnover in living cells remains largely unknown. In this study, CD44, a receptor for HA, and hyaluronidase-1, -2, and -3 (Hyal-1, -2 and -3) were stably expressed in HEK 293 cells and the mechanism of HA catabolism was systematically investigated using fluorescein-labeled HA. CD44 was essential for HA degradation by both endogenous and exogenously expressed hyaluronidases. Hyal-1 was not able to cleave HA in living cells in the absence of CD44. Intracellular HA degradation was predominantly mediated by Hyal-1 after incorporation of HA by CD44. Although Hyal-1 was active only in intracellular space in vivo, a certain amount of the enzyme was secreted to extracellular space. This extracellular Hyal-1 was found to be incorporated by cells and such uptake of Hyal-1 was, in part, involved in the intracellular degradation of HA. Hyal-2 was involved in the extracellular degradation of HA. Hyal-2 activity was also dependent on the expression of CD44 in both living cells and enzyme assays. Immunofluorescent microscopy demonstrated that both Hyal-2 and CD44 are present on the cell surface. Without CD44 expression, Hyal-2 existed in a granular pattern, and did not show hyaluronidase activity, suggesting that localization change could contribute to Hyal-2 function. A convenient and quantitative enzyme assay was established for the measurement of Hyal-2 activity. Hyal-2 activity was detected in the membrane fraction of cells co-expressing Hyal-2 and CD44. The pH optimum for Hyal-2 was 6.0-7.0. The membrane fraction of cells expressing Hyal-2 alone did not show hyaluronidase activity. Hyal-3 did not show any hyaluronidase activity in our experimental conditions. Based on these findings, Hyal-1 and -2 contribute to intracellular and extracellular catabolism of HA, respectively, in a CD44-dependent manner, and their HA degradation occurs independently from one another."xsd:string |
| http://purl.uniprot.org/citations/17170110 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m608358200"xsd:string |
| http://purl.uniprot.org/citations/17170110 | http://purl.uniprot.org/core/author | "Takahashi M."xsd:string |
| http://purl.uniprot.org/citations/17170110 | http://purl.uniprot.org/core/author | "Harada H."xsd:string |
| http://purl.uniprot.org/citations/17170110 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17170110 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/17170110 | http://purl.uniprot.org/core/pages | "5597-5607"xsd:string |
| http://purl.uniprot.org/citations/17170110 | http://purl.uniprot.org/core/title | "CD44-dependent intracellular and extracellular catabolism of hyaluronic acid by hyaluronidase-1 and -2."xsd:string |
| http://purl.uniprot.org/citations/17170110 | http://purl.uniprot.org/core/volume | "282"xsd:string |
| http://purl.uniprot.org/citations/17170110 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17170110 |
| http://purl.uniprot.org/citations/17170110 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17170110 |
| http://purl.uniprot.org/uniprot/P16070#attribution-FD2E9EC6B1323433F606081878C3B88E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17170110 |
| http://purl.uniprot.org/uniprot/Q12891#attribution-FD2E9EC6B1323433F606081878C3B88E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17170110 |
| http://purl.uniprot.org/uniprot/Q12794#attribution-FD2E9EC6B1323433F606081878C3B88E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17170110 |
| http://purl.uniprot.org/uniprot/O43820#attribution-FD2E9EC6B1323433F606081878C3B88E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17170110 |