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Updated: Aug 3, 2026

Detection of Neu1 Sialidase Activity in Regulating TOLL-like Receptor Activation
Published on: September 8, 2010
Human neuraminidase is a 60 kDa-processing product of prosaposin
M Potier1, S Lamontagne, L Michaud
1Service de Génétique Médicale, Hôpital Sainte-Justine, Université de Montréal, Québec, Canada.
Abstract:
Human neuraminidase was purified from placenta as part of a large molecular weight complex with lysosomal beta-galactosidase and carboxypeptidase. Passage of this purified complex through a sialic acid-affinity column (fetuin-agarose) retained a minor 60 kDa protein which was eluted with 100 mM N-acetylneuraminic acid. This 60 kDa protein is recognized in Western blots of the purified complex by an anti-prosaposin antibody which at the same time was able to inhibit neuraminidase activity in the preparation. Furthermore, probing of cultured skin fibroblasts of patients affected with neuraminidase deficiency using the antiprosaposin antibody revealed an abnormal 57 kDa protein. These results indicate that the 60 kDa protein is derived from prosaposin and has the characteristics of a neuraminidase.
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