Acetylcholinesterase (AChE) hydrolyzes acetylcholine at cholinergic synapses, and which has various isoforms of AChE, i.e. AChER, AChEH and AChET, deriving from single gene. AChEH exists as a glycophosphatidylinositol (GPI)-linked dimer (G2), presents mainly in plasma membrane of mammalian erythrocyte. Transgenic mice with ACHE gene depletion were employed here to investigate the possible role of AChE in blood cell formation. ACHE knock-out mice were found to suffer normocytic anemia. In erythrocyte of ACHE-/- mice, the amount of hemoglobin, especially alpha-globin, was found to be markedly reduced. In addition, the number of erythrocyte and hematocrit of ACHE-/- mice were significantly lowered. To probe the role of AChE isoforms in erythroid differentiation, erythroblast-like cells (TF-1) over-expressed with different AChE isoforms were induced to differentiate by erythropoietin (EPO): this differentiation induced the expression of each AChE isoform. Only in the TF-1cells over-expressed with AChEH, the EPO-induced transcriptions and protein expressions of alpha- and beta-globins could be significantly enhanced, which therefore suggested that AChEH might regulate the responsiveness of TF-1cells to EPO. The alternation of EPO-induced downstream signaling might be accounted by association of AChE with EPO receptor in cell surface. The findings indicated the significance of AChE in erythroblast maturation, which provided an insight in elucidating possible mechanisms in regulating erythropoiesis.
        
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Xu ML, Luk WKW, Liu EYL, Kong XP, Wu KQY, Xia YJ, Dong TTX, Tsim KWK (2019) Differentiation of erythroblast requires the dimeric form of acetylcholinesterase: Interference with erythropoietin receptor Chemico-Biological Interactions308: 317-322
Xu ML, Luk WKW, Liu EYL, Kong XP, Wu KQY, Xia YJ, Dong TTX, Tsim KWK (2019) Chemico-Biological Interactions308: 317-322