Characterization of "fetal-type" acetylcholinesterase in hemin-treated K562 cell culture.
The alteration of acetylcholinesterase (ACHE) activity, a marker enzyme of erythroid differentiation, was studied during the hemin-induced erythroid differentiation of K562 human leukemia cells in suspension culture. The kinetics of postinduction differentiation was followed by determining the hemoglobin (Hb) content and the ACHE activity of cells. Embryonic hemoglobins as well as small quantities of fetal Hb (HbF) were synthetized by stimulated cells. The peaks of ACHE activity preceded the highest level of Hb content and, following induction, reached their pinnacles at 72 and 120 hours, respectively. These data indicate that ACHE activity is an earlier and more sensitive marker for hemin-induced erythroid differentiation of K562 cells than is elevated Hb content. Electrophoretic mobility of ACHE from hemin-treated cells proved to be the fetal type, but after incubation with neuraminidase, the rate of migration decreased to the level of the adult type enzyme.
D000110:Acetylcholinesterase / Q000378:metabolism*; D002460:Cell Line; D005333:Fetus; D006418:Heme / Q000494:pharmacology*; D006454:Hemoglobins / Q000096:biosynthesis; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D007951:Leukemia, Myeloid
D006454:Hemoglobins; D007527:Isoenzymes; D006418:Heme; D000110:Acetylcholinesterase