Hyaluronoglucosaminidase (HYAL)

Hyaluronoglucosaminidase, more commonly known as hyaluronidase, is a family of enzymes (EC 3.2.1.35) that catalyze the degradation of hyaluronic acid (HA), a major structural polysaccharide in the extracellular matrix. By cleaving the beta-1,4-glycosidic bonds in HA, these enzymes reduce the viscosity of connective tissue and significantly increase tissue permeability. This biological property led to their characterization as 'spreading factors,' which facilitate the movement of fluids and molecules through the interstitial space. In therapeutic settings, hyaluronidases are primarily used to enhance the dispersion and absorption of co-administered injectable drugs, such as local anesthetics and monoclonal antibodies, and to manage the extravasation of fluids. Beyond its clinical utility in drug delivery, the enzyme plays vital roles in physiological processes including fertilization, where it enables sperm to penetrate the cumulus oophorus, and in tissue remodeling. Aberrant hyaluronidase activity is implicated in the progression of various diseases, notably cancer, where it can promote tumor cell migration and metastasis by modifying the tumor microenvironment.

Other names

HyaluronidaseHyaluronate 4-glycanohydrolaseSpreading factorHyaluronoglucosidaseSperm adhesion molecule 1 (SPAM1)PH-20

Catalyzes the random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate, reducing its molecular weight and decreasing the viscosity of the extracellular matrix to increase tissue permeability for the absorption of fluids and co-administered drugs.