Inhibition of acid sialidase by inorganic sulfate.
Sulfated glycosaminoglycans are known to inhibit mammalian acid-active sialidase. Although the inhibition depends clearly on the presence of sulfate groups on these macromolecules, there was no information on the intrinsic inhibitory potency of inorganic sulfate. In this study, we demonstrate that inorganic sulfates inhibit acid-active Mu-Neu5Ac sialidase of U937 cells. This inhibition was found to be reversible and it appeared to be of the mixed competitive type. Sulfate-induced inhibition was also observed in other cells as well as with other substrates such as sialyl lactose and bovine mixed brain gangliosides. We conclude that the intrinsic inhibitory potency of sulfate groups may be significantly involved in the inhibition of acid-active sialidase by sulfated glycosaminoglycans. In addition, inorganic sulfate by its apparent potency to selectively inhibit acid sialidases might constitute an interesting tool for the characterisation of the minor forms of sialidases occurring in mammalian cells.
Greffard
A
A
Inserm U139, Institut Mondor de Médecine Moléculaire (IM3), Hopital Henri Mondor, Créteil, France.
Trabelsi
N
N
Terzidis
H
H
Bignon
J
J
Jaurand
M C
MC
Pilatte
Y
Y
D000645:Ammonium Sulfate / Q000494:pharmacology; D002809:Chondroitin Sulfates / Q000494:pharmacology; D006801:Humans; D016403:Lymphoma, Large B-Cell, Diffuse; D009439:Neuraminidase / Q000037:antagonists & inhibitors*; D013347:Subcellular Fractions; D013431:Sulfates / Q000494:pharmacology*; D014407:Tumor Cells, Cultured
D013431:Sulfates; D002809:Chondroitin Sulfates; D009439:Neuraminidase; D000645:Ammonium Sulfate