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proteins. Page last changed on 19 Dec 2016.
HYAL4, hyaluronidase-4, hyaluronidase IV
This gene encodes a protein which is similar in structure to hyaluronidases. 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. However, this protein has not yet been shown to have hyaluronidase activity. [provided by RefSeq, Jul 2008] (from
Lindblad-Toh et al., Uppsala, Sweden. In Plos Genet, Nov 2015
In addition, disease associated haplotypes harbouring the hyaluronidase genes HYAL1, HYAL2 and HYAL3 on cfa20 and HYAL4, SPAM1 and HYALP1 on cfa14 were identified as separate risk factors in European and US golden retrievers, respectively, suggesting that turnover of hyaluronan plays an important role in the development of CMCT.
Schmechel et al., Minneapolis, United States. In Cancer, 2014
Hyaluronan (HA) is a high molecular weight polyanionic carbohydrate produced by synthases (HAS1 through HAS3) and fragmented by oxidative/nitrosative stress and hyaluronidases (HYAL1 through HYAL4, SPAM1) common in PCa microenvironments.
Subsequently, we confirmed well-characterized oncogenes among tumor-related loci (such as EGFR and KIT) and detected novel genes that gained chromosome sequences (such as AASS, HYAL4, NDUFA5 and SPAM1) in both LGG and HGG.
Triggs-Raine et al., Winnipeg, Canada. In Matrix Biol, 2008
In humans, six paralogous genes encoding hyaluronidase-like sequences have been identified on human chromosomes 3p21.3 (HYAL2-HYAL1-HYAL3) and 7q31.3 (SPAM1-HYAL4-HYALP1). Mutations in one of these genes, HYAL1, were reported in a patient with mucopolysaccharidosis (MPS) IX.
Byers et al., Adelaide, Australia. In Matrix Biol, 2006
In mineralising MG63 cells a 62-fold increase in hyaluronidase 2, a 13-fold increase in hyaluronidase 3, and a 3-fold increase in hyaluronidase 4 expression were observed when compared to non-mineralising cells; hyaluronidase 1 and PH20 expression was not detected.
Zou et al., Orsay, France. In J Biochem Biophys Methods, 2000
A potential N-glycosylation site (site 1) with similar tripeptide patterns was observed at the same position in human plasma (HYAL1), human lysosomes (HYAL2) and in two newly reported hyaluronidases (HYAL4 and HYALP1).