Arylsulfatase in natural killer cells: its possible role in cytotoxicity.
Ultrastructural cytochemistry of natural killer cells enriched by Percoll gradient centrifugation showed them to possess arylsulfatase (aryl-sulfate sulfohydrolase, EC 3.1.6.1). The enzyme was located in vesicles, granules, and the parallel tubular arrays, organelles characteristic for cytotoxic lymphocytes. Biochemically, peak enzyme activity correlated with the Percoll fractions containing cells with cytotoxicity for melanoma target cells. Treatment of natural killer cells with Na2SO4, a competitive inhibitor of arylsulfatase, suppressed cytotoxicity by almost 50%. Electron microscopy of effector-target cell conjugates, which had been permitted to incubate for only 30 min, disclosed numerous arylsulfatase-positive sites at the points of contact between the effector/target cell membranes. Thus, the enzyme was translocated to the surface before lysis of the target cell was morphologically evident. It is postulated that the parallel tubular arrays play a role in this translocation and that arylsulfatase may function in the degradation of cerebroside sulfate ester components of the target cell membrane to initiate the lytic event.
D001192:Arylsulfatases / Q000378:metabolism*; D003602:Cytotoxicity, Immunologic; D006651:Histocytochemistry; D006801:Humans; D007694:Killer Cells, Natural / Q000201:enzymology / Q000276:immunology* / Q000648:ultrastructure; D007700:Kinetics; D008545:Melanoma / Q000201:enzymology / Q000276:immunology / Q000648:ultrastructure; D008854:Microscopy, Electron; D013429:Sulfatases / Q000378:metabolism*
D013429:Sulfatases; D001192:Arylsulfatases