Note | HYAL1 is a secreted somatic tissue hyaluronidase, and the predominant hyaluronidase in human plasma. Although HYAL1 is predominantly secreted, it has an acid pH optimum in vitro. HYAL1 can degrade high molecular weight hyaluronan to small oligomers, primarily to tetrasaccharides, whereas HYAL2 (the other major human hyaluronidase) high molecular mass hyaluronan to an approximately 20 kDa product (approximatively 50 saccharide units). |
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Description | Size: 435 amino acids; Molecular mass: 48368 Da. The enzyme belongs to the group of carbohydrate-active enzymes (CASy), termed glycosyl hydrolase 56 family. |
Expression | HYAL1 is highly expressed in liver, kidney and heart and weakly expressed in lung, placenta and skeletal muscle. No expression is detected in adult brain. Isoform 1 is expressed only in bladder and prostate cancer cells, G2/G3 bladder tumor tissues and lymph node specimens showing tumor invasive tumors cells. Isoform 3, isoform 4, isoform 5 and isoform 6 are expressed in normal bladder and bladder tumor tissues. HYAL1 expression has been described in squamous cell carcinoma, in small cell lung cancer and glioma lines. |
Localisation | It is a secreted enzyme found in plasma and it is also present in lysosomes. |
Function | It is a hydrolytic enzyme (endo-beta-acetyl-D-hexosaminidase) with optimum pH about 3.7, acting on hyaluronan, chondroitin and chondroitin sulphate. It possesses also transglycosidase activity using hyaluronan and chondroitin sulphate or chondroitin as substrates. This reaction is not well understood, and the precise enzymatic mechanism is not known. |
Homology | The enzyme possesses 70-80 % homology to orthologue hyaluronidases, 40% homology to paralogue hyaluronidases of the human and high homology with HYAL1 of other species. |
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HYAL2, a human gene expressed in many cells, encodes a lysosomal hyaluronidase with a novel type of specificity. |
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PMID 9712871 |
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Mutations in HYAL1, a member of a tandemly distributed multigene family encoding disparate hyaluronidase activities, cause a newly described lysosomal disorder, mucopolysaccharidosis IX. |
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