Diversity and Processing of Acetylcholinesterase

Massoulié, Jean; Anselmet, Alain; Bon, Suzanne; Krejci, Éric; Legay, Claire; Mayat, Ebrahim; Morel, Nathalie; Simon, Stéphanie

doi:10.1007/978-1-4899-1540-5_2

Cited by 5 publications

(4 citation statements)

References 90 publications

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“…In the absence of this enzyme in humans no detrimental effects are observed except when exposed to succinylcholine 79. A prominent feature of BChE, as of AChE, is its extremely rich variety of molecular forms, which has been the focus of many review papers 72,75,76,79–83…”

Section: Enzymes Involved In the Bioconversion Of Ester Prodrugsmentioning

confidence: 99%

Enzymes involved in the bioconversion of ester-based prodrugs

Liederer

Borchardt

2006

Journal of Pharmaceutical Sciences

333

238

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Section: Enzymes Involved In the Bioconversion Of Ester Prodrugsmentioning

confidence: 99%

Enzymes involved in the bioconversion of ester-based prodrugs

Liederer

Borchardt

2006

Journal of Pharmaceutical Sciences

333

238

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“…AChE-S (tailed isoform), AChE-E (erythtocytic isoform) and AChE-R (read-through isoform) [4]. Recently, several reports have shown that AChE is involved in many non-cholinergic functions, such as cell adhesion, proliferation, neurite outgrowth and regulation of apoptosis [5 -9].…”

Section: Introductionmentioning

confidence: 99%

The JNK/AP1/ATF2 pathway is involved in H2O2-induced acetylcholinesterase expression during apoptosis

Zhang

Jiang

Gao

et al. 2008

Cell. Mol. Life Sci.

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We show that H2O2 increases acetylcholinesterase (AChE) expression via transcriptional activation through c-Jun N-terminal kinase (JNK), since the JNK inhibitor SP600125, but not the extracellular signal-regulated kinase (ERK) pathway inhibitor PD98059 or p38 kinase inhibitor SB203580, attenuated H2O2-induced AChE expression and its promoter activity. Overexpression of hemagglutinin (HA)-JNK increases H2O2-induced AChE expression and its promoter activity, whereas the dominant negative mutant form of JNK suppressed H2O2-induced AChE expression and promoter activity. Mutation analysis indicates that the major response elements for JNK in the AChE promoter are the AP1-like element (TGAGTCT) site, located within the -1565/-1569 region of the AChE promoter, and the ATF2 element (CCACGTCA), within the -2185/-2177 region. The AP1-like element binds to the transcription factors, c-jun and ATF2, while the ATF2 element binds mainly ATF2. Taken together, our results strongly suggest that H2O2 induces AChE expression via the JNK/AP1/ ATF2 signaling pathway.

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“…Previously, we isolated 2 genes (Dv-sace-1 and Dvsace-2) from D. viviparus which encode secreted AChEs (Lazari et al 2003). In this case, the enzyme exhibits sequence properties distinct from the GPIanchored form of the enzyme and has the sequence characteristics of an AChE analogous to the ' tailed ' (T) subunit AChE of vertebrates (Massoulié et al 1998) and to ACE-1 from C. elegans (Arpagaus et al 1994). These observations were substantiated after we characterized the corresponding recombinant proteins (Lazari et al 2003).…”

Section: Introductionmentioning

confidence: 99%

“…In the current study, we describe the isolation and characterization of a cDNA encoding a second class of neuromuscular AChE from D. viviparus. In this case, the enzyme exhibits sequence properties distinct from the GPIanchored form of the enzyme and has the sequence characteristics of an AChE analogous to the ' tailed ' (T) subunit AChE of vertebrates (Massoulié et al 1998) and to ACE-1 from C. elegans (Arpagaus et al 1994).…”

mentioning

confidence: 99%

A tryptophan amphiphilic tetramerization domain-containing acetylcholinesterase from the bovine lungworm,Dictyocaulus viviparus

et al. 2006

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Acetylcholine (ACh) is one of an array of neurotransmitters used by invertebrates and, analogous to vertebrate nervous systems, acetylcholinesterase (AChE) regulates synaptic levels of this transmitter. Similar to other invertebrates, nematodes possess several AChE genes. This is in contrast to vertebrates, which have a single AChE gene, transcripts of which are alternatively spliced to produce different types of the enzyme which vary at their C-termini. Parasitic nematodes have a repertoire of AChE genes which include those encoding neuromuscular AChEs and those genes which code for secreted AChEs. The latter proteins exist as soluble monomers released by the parasite during infection and these AChE are distinct from those enzymes which the nematodes use for synaptic transmission in their neuromuscular system. Thus far, Dictyocaulus viviparus is the only animal-parasitic nematode for which distinct genes that encode both neuromuscular and secreted AChEs have been defined. Here, we describe the isolation and characterization of a cDNA encoding a putative neuromuscular AChE from D. viviparus which contains a tryptophan amphiphilic tetramerization (WAT) domain at its C-terminus analogous to the common 'tailed' AChE form found in the neuromuscular systems of vertebrates and in the ACE-1 AChE from Caenorhabditis elegans. This enzyme differs from the previously isolated, D. viviparus neuromuscular AChE (Dv-ACE-2), which is a glycosylphosphatidylinositol-anchored variant analogous to vertebrate 'hydrophobic' AChE.

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Diversity and Processing of Acetylcholinesterase

Cited by 5 publications

References 90 publications

Enzymes involved in the bioconversion of ester-based prodrugs

Enzymes involved in the bioconversion of ester-based prodrugs

The JNK/AP1/ATF2 pathway is involved in H2O2-induced acetylcholinesterase expression during apoptosis

A tryptophan amphiphilic tetramerization domain-containing acetylcholinesterase from the bovine lungworm,Dictyocaulus viviparus

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