On the activation of plasma membrane ecto-enzymes by treatment with neuraminidase

It had been proposed that sialyl-residues on the surface of the cell control the activity of certain plasma membrane ecto-enzymes. We have tested the effects of several established (or presumptive) ecto-enzymes in tissue cultures of CNS-derived cells. Application of neuraminidases to cultured mouse neuroblastoma (N-18), neonatal Syrian hamster astrocytes (NN), human astrocytoma (Cox clone) and two lines of primary mouse astroblasts failed to change the activity of ecto-ATPase and 5'-nucleotidase. Only two of the seven neuraminidase preparations produced marked or moderate increases in inorganic pyrophosphatase, p-nitrophenylphosphatase and cholinesterase. We have concluded that the stimulation of these enzymes was not due to removal of sialyl-residues. We suggest that contaminants (haemolysins?) in neuraminidase preparations of Clostridium perfringens increased membrane permeability and facilitated substrate-product translocation.