Identification of an endogenous polypeptide modulating ligand binding sites of insect neuronal acetylcholine receptors

Benke, Dietmar; Breer, Heinz

doi:10.1016/0197-0186(90)90104-2

Cited by 1 publication

(2 citation statements)

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“…Although choline-hydrolyzing activity and non-enzymatic functions of AChE may be mediated by different domains of the AChE protein (the catalytic site and a peripheral anionic region [23]) both the reduction of AChE presence and pharmacological inhibition of its catalytical function interfered with apoptotic cell death in various cell types [23,28,29,[31][32][33]. The present study may suggest that the catalytical activity of AChE promotes apoptosis in locust neurons, since hypoxia-induced cell death was prevented by NSB and TRB, two AChE inhibitors with different molecular structure, both of which have been demonstrated to inhibit insect AChE activity ( [65][66][67][68] and see below for more details). This suggests that functionality of AChE's catalytical site is required for its pro-apoptotic role in locusts.…”

Section: Discussionmentioning

confidence: 64%

“…NSB is a carbamate inhibitor that covalently binds to a serine residue in the catalytic region of AChE. It has been employed in studies with several insects including cockroaches [ 68 ] and locusts [ 66 ]. A recent study demonstrated, that 100 µM, 10 µM and 1 µM NSB inhibited ~ 95%, ~ 75% and ~ 50% of AChE activity in homogenates of larval lepidoptera respectively [ 67 ].…”

Section: Discussionmentioning

confidence: 99%

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Acetylcholinesterase promotes apoptosis in insect neurons

et al. 2020

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Apoptosis plays a major role in development, tissue renewal and the progression of degenerative diseases. Studies on various types of mammalian cells reported a pro-apoptotic function of acetylcholinesterase (AChE), particularly in the formation of the apoptosome and the degradation of nuclear DNA. While three AChE splice variants are present in mammals, invertebrates typically express two ache genes that code for a synaptically located protein and a protein with non-synaptic functions respectively. In order to investigate a potential contribution of AChE to apoptosis in insects, we selected the migratory locust Locusta migratoria. We established primary neuronal cultures of locust brains and characterized apoptosis progression in vitro. Dying neurons displayed typical characteristics of apoptosis, including caspase-activation, nuclear condensation and DNA fragmentation visualized by TUNEL staining. Addition of the AChE inhibitors neostigmine and territrem B reduced apoptotic cell death under normal culture conditions. Moreover, both inhibitors completely suppressed hypoxia-induced neuronal cell death. Exposure of live animals to severe hypoxia moderately increased the expression of ace-1 in locust brains in vivo. Our results indicate a previously unreported role of AChE in insect apoptosis that parallels the pro-apoptotic role in mammalian cells. This similarity adds to the list of apoptotic mechanisms shared by mammals and insects, supporting the hypothesized existence of an ancient, complex apoptosis regulatory network present in common ancestors of vertebrates and insects.

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