Preliminary exploration of the expression of acetylcholinesterase in normal human T lymphocytes and leukemic Jurkat T cells

The classic enzymatic function of acetylcholinesterase (AChE) is the hydrolysis of acetylcholine (ACh) in the neuronal synapse. However, AChE is also present in nonneuronal cells such as lymphocytes. Various studies have proposed the participation of AChE in the development of cancer. The ACHE gene produces three mRNAs (T, H and R). AChE‑T encodes amphiphilic monomers, dimers, tetramers (G₁A, G₂A and G₄A) and hydrophilic tetramers (G₄H). AChE‑H encodes amphiphilic monomers and dimers (G₁A and G₂A). AChE‑R encodes a hydrophilic monomer (G₁H). The present study considered the differences in the mRNA expression (T, H and R) and protein levels of AChE, as well as the molecular forms of AChE, the glycosylation pattern and the enzymatic activity of AChE present in normal T lymphocytes and leukemic Jurkat E6‑1 cells. The results revealed that AChE enzymatic activity was higher in normal T lymphocytes than in Jurkat cells. Normal T cells expressed AChE‑H transcripts, whereas Jurkat cells expressed AChE‑H and AChE‑T. The molecular forms identified in normal T cells were G₂A (5.2 S) and G₁A (3.5 S), whereas those in Jurkat cells were G₂A (5.2 S), G₁A (3.5 S) and G₄H (10.6S). AChE in Jurkat cells showed altered posttranslational maturation since a decrease in the incorporation of galactose and sialic acid into its structure was observed. In conclusion, the content and composition of AChE were altered in Jurkat cells compared with those in normal T lymphocytes. The present study opened new avenues for exploring the development of novel therapeutic strategies against T‑cell leukemia and for identifying potential molecular targets for the early detection of this type of cancer.