The hyaluronidases are a family of enzymes that have, until recently, defied thorough explication. The substrate for these enzymes, hyaluronan, is becoming increasingly important, recognized now as a major participant in such basic processes as cell motility, wound healing, embryogenesis, and implicated in cancer progression. And in those lower life forms that torment human beings, hyaluronidase is associated with mechanisms of entry and spread,
e.g. as a virulence factor for bacteria, for tissue dissection in gas gangrene, as a means of treponema spread in syphilis, and for penetration of skin and gut by nematode parasites. Hyaluronidase also comprises a component of the venom of a wide variety of organisms, including bees, wasps, hornets, spiders, scorpions, fish, snakes and lizards. Of particular interest is the homology between some of these venom hyaluronidases and the enzyme found in the plasma membrane of mammalian spermatozoa, attesting to the ancient nature of the conserved sequence, a 36% identity in a 300 amino acid stretch of the enzyme protein. Clearly, hyaluronidase is of biological interest, being involved in the pathophysiology of so many important human disorders. Greater effort should be made in studying this family of enzymes that have, until recently, been overlooked.
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