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Two distinct acetylcholinesterases possessing almost identical enzymatic activity in the damselfly Vestalis gracilis
Most insects possess two different acetylcholinesterases (AChEs) (i.e., AChE1 and AChE2). It has been recently reported that both AChEs are equally active in a damselfly species, providing a unique example of the incomplete specialization of one AChE function after duplication (Kim and Lee, 2013). In this study, we investigated the tissue distribution patterns and the molecular and inhibitory properties of two AChEs (i.e., VgAChE1 and VgAChE2) from the Vestalis gracilis damselfly. VgAChEs exhibited almost identical catalytic activity and were expressed in the central nervous system (CNS). The most predominant molecular form of both VgAChEs was a disulfide-bridged dimer, which is associated with the cell membrane via a glycosylphosphatidylinositol anchor. In an inhibition assay, however, VgAChE1 and VgAChE2 exhibited different sensitivities to organophosphate and carbamate insecticides depending on the structure of the inhibitors. These findings suggest that both VgAChEs have neuronal functions. In addition, soluble monomeric and cleaved molecular forms were detected in both the CNS and peripheral nervous system tissues by an AChE2-specific antibody, implying that VgAChE2 probably shares both neuronal and non-neuronal physiological functions in V. gracilis. Our results support the notion that both VgAChEs, paralogous of each other, are involved in synaptic transmission, with VgAChE2 being in the early stage of acquiring non-neuronal functions.
