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Hyaluronidase is an enzyme that catalyzes the hydrolysis of hyaluronic acid—a key component of the extracellular matrix—by cleaving its glycosaminidic bonds. This action lowers the viscosity of tissue and increases permeability by breaking down the structural integrity provided by hyaluronic acid[1][5][8]. Clinically, it is used to facilitate subcutaneous fluid administration (hypodermoclysis), enhance absorption and dispersion of other injected drugs (such as local anesthetics), promote resorption of radiopaque agents in subcutaneous urography, manage extravasation injuries from certain drugs or solutions (including vinca alkaloids), and dissolve dermal fillers composed of cross-linked hyaluronic acid[1][4][5][8]. It is also used to increase absorption rates for parenterally administered fluids and as an adjunct in ophthalmic surgery. The mechanism involves enzymatic cleavage at specific sites on the polysaccharide chain of hyaluronic acid. Multiple recombinant forms exist; some are derived from human or animal sources. Developed by Halozyme Therapeutics.
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