Description
Title: Characterization of the Chondroitin Sulfate Catabolic Enzyme Hyaluronidase 4
Abstract: Endo-beta-N-acetylhexosaminidases called hyaluronidases (HYALs) depolymerize chondroitin sulfate (CS) as well as hyaluronan as the first stage of their catabolism. While HYAL1 hydrolyzes both CS and HA, HYAL4 is an endoglycosidase that only hydrolyzes CS. It has been reported that HYAL4 is substrate-specific and that the amino acid residues necessary for its enzymatic activity have been identified. In this study, we used cultured cells as well as mouse tissues to characterize the properties of HYAL4, including the expression levels in different tissues, cellular localization, and effects of its overexpression on intracellular CS catabolism. It has been shown that the mouse’s HYAL4 mRNA and protein are widely expressed in a variety of organs. Rat skeletal muscle myoblast L6 cells were found to contain the HYAL4 protein in their lysosomes as well as on their cell surfaces. The total amount of CS was reduced when HYAL4 was overexpressed in Chinese hamster ovary cells, indicating that it participates in the catabolism of CS within the cells. In summary, HYAL4 may be widely used.
Keywords: chondroitin sulfate; glycosaminoglycan; hyaluronidase; hydrolase
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Chemistry
Writer Experience: 20+ Years
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