title: Evidence for sialidase activity in K 562 cells: inhibition by adriamycin treatment.
abstract: Sialidase activity has been studied in the human erythroleukemia K 562 cell line grown in vitro. The total sialidase activity was determined using disialoganglioside GD1a and fetuin as exogenous substrates. The enzymatic activity was stimulated by 0.08% Triton X-100 and reached the highest level at pH 4.0. Results obtained showed that gangliosides are hydrolysed more extensively than glycoproteins by K 562 sialidases. This finding could suggest that endogenous gangliosides may be the main source of metabolically available sialic acid in K 562 cell line. After treatment of K 562 cells by Adriamycin (40 nM), a potent anticancer drug, sialidase activity decreased by 40% as compared to control cells. This decrease occurs early during the first day of incubation with Adriamycin. This inhibition of sialidase activity could explain previous results obtained in our laboratory which show an enhanced sialylation of the membrane glycoconjugates after Adriamycin treatment.
mesh_terms: D002460:Cell Line; D004317:Doxorubicin / Q000494:pharmacology*; D005732:Gangliosides / Q000378:metabolism; D006427:Hemin / Q000494:pharmacology; D006454:Hemoglobins / Q000096:biosynthesis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D004915:Leukemia, Erythroblastic, Acute / Q000201:enzymology*; D009439:Neuraminidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000494:pharmacology; D000509:alpha-Fetoproteins / Q000378:metabolism
chemical_list: D005732:Gangliosides; D006454:Hemoglobins; D000509:alpha-Fetoproteins; D011092:Polyethylene Glycols; D006427:Hemin; D004317:Doxorubicin; D009439:Neuraminidase