| ID | Sequence | Length | GC content |
|---|---|---|---|
| CCUUCCUCCAGGAGUCUCUGGUGCAGCUGGGGUGGAAUCUGGCCAGGCC… | 2031 nt | 0.5736 | |
| AGAUGUGGGGAGCGCCUCUGCCCUGUCGCCCCGUCCGGGAUGUGAGGAG… | 2325 nt | 0.5755 | |
| CCUUCCUCCAGGAGUCUCUGGUGCAGCUGGGGUGGAAUCUGGCCAGGCC… | 1941 nt | 0.5714 | |
| CCUUCCUCCAGGAGUCUCUGGUGCAGCUGGGGUGGAAUCUGGCCAGGCC… | 1674 nt | 0.5663 | |
| CCUUCCUCCAGGAGUCUCUGGUGCAGCUGGGGUGGAAUCUGGCCAGGCC… | 1256 nt | 0.5446 |
This gene encodes a lysosomal hyaluronidase. Hyaluronidases intracellularly degrade hyaluronan, one of the major glycosaminoglycans of the extracellular matrix. Hyaluronan is thought to be involved in cell proliferation, migration and differentiation. This enzyme is active at an acidic pH and is the major hyaluronidase in plasma. Mutations in this gene are associated with mucopolysaccharidosis type IX, or hyaluronidase deficiency. The gene is one of several related genes in a region of chromosome 3p21.3 associated with tumor suppression. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
A study in rats demonstrated that the HYAL1 mRNA expression was significantly suppressed in both triolein injection and femoral fracture groups at 20 hours post-procedure, indicating its role as an indicator of vascular endothelial damage in a fat embolism model [Kuwata DOI:10.1016/J.Legalmed.2024.102531]. In a separate study, the orthologue of the HYAL1 was found to be up-regulated in both human and rat skin following UVB-induced inflammation, with a fold change of 20.5 in human and 6.2 in rat skin, highlighting its involvement in extracellular matrix degradation during inflammatory hyperalgesia [Dawes et al. DOI:10.1371/journal.pone.0093338].