Preliminary exploration of the expression of acetylcholinesterase in normal human T lymphocytes and leukemic Jurkat T cells
Por:
Gómez-Olivares, JL, López-Durán, RM, Enríquez-Flores, S, López-Velázquez, G, de la Mora, ID, García-Torres, I, Viedma-Rodríguez, R, Valencia-Quintana, R, Milic, M, Flores-López, LA
Publicada:
1 nov 2024
Resumen:
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.
Filiaciones:
Metropolitan Autonomous Univ Iztapalapa Campus, Dept Hlth Sci, Biomembranes Lab, Mexico City 09310, Mexico
Minist Hlth, Natl Inst Pediat, Biomol & Infant Hlth Lab, Mexico City 04530, Mexico
Univ Nacl Autonoma Mexico, Fac Higher Studies Iztacala, Morphophysiol Unit, Tlalnepantla 54090, Mexico
Autonomous Univ Tlaxcala, Fac Agrobiol, Rafael Villalobos Pietrini Lab Genom Toxicol & Env, Tlaxcala 90120, Mexico
Inst Med Res & Occupat Hlth, Mutagenesis Unit, Zagreb 10000, Croatia
Minist Hlth, CONAHCYT Natl Inst Pediat, Biomol & Infant Hlth Lab, Ave Insurgentes Sur 3700 Letra C, Mexico City 04530, Mexico
gold, All Open Access; Gold Open Access
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