Human hyaluronidases: electrophoretic multiple forms in somatic tissues and body fluids. Evidence for conserved hyaluronidase potential N-glycosylation sites in different mammalian species.

Some properties of the multiple forms of human hyaluronidases in somatic tissues and in body fluids were investigated. Liver and placenta exhibited seven hyaluronidase forms when analyzed electrophoretically on a polyacrylamide-hyaluronan gel. Ovary, breast, myometrium, endometrium, skin, leukocytes and platelets displayed distinct patterns of enzymatic micropolydispersity. The most acidic forms of hyaluronidase were in synovial fluid and serum, some serum exhibited an additional basic form. Following sialidase treatment, the number of forms decreased to two in placenta, three in liver and to a broad basic form in serum. The native serum and placental hyaluronidases remained fully active after thermal inactivation but desialylated hyaluronidase was inactivated slowly in serum, and quickly in placenta suggesting a higher overall glycosylation of the plasma enzyme. Potential N-glycosylation sites were searched in the amino acid sequences of six human hyaluronidases and several hyaluronidases from different mammalian species using the motif database. 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). The same site was also present in mouse plasma (HYAL1) and mouse lysosomes (HYAL2), and in rat lysosomes (HYAL2). This site was absent in human HYAL3 and in all sperm hyaluronidases (PH-20) studied (human, macaque, mouse, guinea pig, rabbit and fox). A second potential N-glycosylation site was observed at a location further in the polypeptide chain. This site is present in all mammalian hyaluronidase isoenzymes reported in the present study whatever the species and organ localization. The pattern at site 2 is NVT for all hyaluronidases except for hyaluronidases of lysosomal origin where it is NVS. Such conserved sites strongly suggest that they may represent actual N-glycosylation sites.

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