Arpagaus M

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Full name : Arpagaus Martine

First name : Martine

Mail : INRA, Departement de Physiologie animale, Place Pierre Viala, 34060 Montpellier Cedex 1

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Country : France

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References (38)

Title : Structure and expression of the four acetylcholinesterase genes in the nematode Caenorhabditis elegans. -
Author(s) : Combes D , Fedon Y , Toutant JP , Arpagaus M
Ref : Cholinergic Mechanisms, CRC Press :187 , 2004
PubMedID:

Title : Four acetylcholinesterase genes in the nematode Caenorhabditis elegans: Gene structure and molecular forms -
Author(s) : Arpagaus M , Combes D , Fedon Y , Toutant JP
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :61 , 2004
PubMedID:

Title : Poster (27) Structure of the four acetylcholinesterase genes in the nematode caenorhabditis elegans. -
Author(s) : Combes D , Fedon Y , Toutant JP , Arpagaus M
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :334 , 2004
PubMedID:

Title : Multiple ace genes encoding acetylcholinesterases of Caenorhabditis elegans have distinct tissue expression - Combes_2003_Eur.J.Neurosci_18_497
Author(s) : Combes D , Fedon Y , Toutant JP , Arpagaus M
Ref : European Journal of Neuroscience , 18 :497 , 2003
Abstract : ace-1 and ace-2 genes encoding acetylcholinesterase in the nematode Caenorhabditis elegans present 35% identity in coding sequences but no homology in noncoding regions (introns, 5'- and 3'-untranslated regions). A 5'-region of ace-2 was defined by rescue of ace-1;ace-2 mutants. When green fluorescent protein (GFP) expression was driven by this regulatory region, the resulting pattern was distinct from that of ace-1. This latter gene is expressed in all body-wall and vulval muscle cells (Culetto et al., 1999), whereas ace-2 is expressed almost exclusively in neurons. ace-3 and ace-4 genes are located in close proximity on chromosome II (Combes et al., 2000). These two genes were first transcribed in vivo as a bicistronic messenger and thus constitute an ace-3;ace-4 operon. However, there was a very low level of monocistronic mRNA of ace-4 (the upstream gene) in vivo, and no ACE-4 enzymatic activity was ever detected. GFP expression driven by a 5' upstream region of the ace-3;ace-4 operon was detected in several muscle cells of the pharynx (pm3, pm4, pm5 and pm7) and in the two canal associated neurons (CAN cells). A dorsal row of body-wall muscle cells was intensively labelled in larval stages but no longer detected in adults. The distinct tissue-specific expression of ace-1, ace-2 and ace-3 (coexpressed only in pm5 cells) indicates that ace genes are not redundant.
ESTHER : Combes_2003_Eur.J.Neurosci_18_497
PubMedSearch : Combes_2003_Eur.J.Neurosci_18_497
PubMedID: 12911746

Title : Acetylcholinesterase genes in the nematode Caenorhabditis elegans - Combes_2001_Int.Rev.Cytol_209_207
Author(s) : Combes D , Fedon Y , Toutant JP , Arpagaus M
Ref : International Review of Cytology , 209 :207 , 2001
Abstract : Acetylcholinesterase (AChE, EC 3.1.1.7) is responsible for the termination of cholinergic nerve transmission. It is the target of organophosphates and carbamates, two types of chemical pesticides being used extensively in agriculture and veterinary medicine against insects and nematodes. Whereas there is usually one single gene encoding AChE in insects, nematodes are one of the rare phyla where multiple ace genes have been unambiguously identified. We have taken advantage of the nematode Caenorhabditis elegans model to identify the four genes encoding AChE in this species. Two genes, ace-1 and ace-2, encode two major AChEs with different pharmacological properties and tissue repartition: ace-1 is expressed in muscle cells and a few neurons, whereas ace-2 is mainly expressed in motoneurons. ace-3 represents a minor proportion of the total AChE activity and is expressed only in a few cells, but it is able to sustain double null mutants ace-1; ace-2. It is resistant to usual cholinesterase inhibitors. ace-4 was transcribed but the corresponding enzyme was not detected in vivo.
ESTHER : Combes_2001_Int.Rev.Cytol_209_207
PubMedSearch : Combes_2001_Int.Rev.Cytol_209_207
PubMedID: 11580201

Title : Four genes encode acetylcholinesterases in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. cDNA sequences, genomic structures, mutations and in vivo expression - Combes_2000_J.Mol.Biol_300_727
Author(s) : Combes D , Fedon Y , Grauso M , Toutant JP , Arpagaus M
Ref : Journal of Molecular Biology , 300 :727 , 2000
Abstract : We report the full coding sequences and the genomic organization of the four genes encoding acetylcholinesterase (AChE) in Caenorhabditis elegans and Caenorhabditis briggsae, in relation to the properties of the encoded enzymes. ace-1 and ace-2, located on chromosome X and I, respectively, encode two AChEs (ACE-1 and ACE-2) that present 35% identity. The C-terminal end of ACE-1 is homologous to the C terminus of T subunits of vertebrate AChEs. ACE-1 oligomerizes into amphiphilic tetramers. ACE-2 has a hydrophobic C terminus of H type. It associates into glycolipid-anchored dimers. In C. elegans and C. briggsae, ace-3 and ace-4 are organized in tandem on chromosome II, with only 356 nt and 369 nt, respectively, between the stop codon of ace-4 (upstream gene) and the ATG of ace-3. ace-3 produces only 5 % of the total AChE activity. It encodes an H subunit that associates into dimers of glycolipid-anchored catalytic subunits, which are highly resistant to the usual AChE inhibitors, and which hydrolyze butyrylthiocholine faster than acetylthiocholine. ACE-4 is closer to ACE-3 (54 % identity) than to ACE-1 or ACE-2. The usual sequence FGESAG surrounding the active serine residue in cholinesterases is changed to FGQSAG in ace-4. ACE-4 was not detected by our current biochemical methods, although the gene is transcribed in vivo. However the level of ace-4 mRNAs is far lower than those of ace-1, ace-2 and ace-3. The ace-2, ace-3 and ace-4 transcripts were found to be trans-spliced by both SL1 and SL2, although these genes are not included in typical operons. The molecular bases of null mutations g72 (ace-2), p1304 and dc2 (ace-3) have been identified.
ESTHER : Combes_2000_J.Mol.Biol_300_727
PubMedSearch : Combes_2000_J.Mol.Biol_300_727
PubMedID: 10891266
Gene_locus related to this paper: caebr-ACHE3 , caebr-ACHE4 , caeel-ACHE2 , caeel-ACHE3 , caeel-ACHE4

Title : Mutations in the dystrophin-like dys-1 gene of Caenorhabditis elegans result in reduced acetylcholinesterase activity - Giugia_1999_FEBS.Lett_463_270
Author(s) : Giugia J , Gieseler K , Arpagaus M , Segalat L
Ref : FEBS Letters , 463 :270 , 1999
Abstract : Mutations of the Caenorhabditis elegans dystrophin/utrophin-like dys-1 gene lead to hyperactivity and hypercontraction of the animals. In addition dys-1 mutants are hypersensitive to acetylcholine and acetylcholinesterase inhibitors. We investigated this phenotype further by assaying acetylcholinesterase activity. Total extracts from three different dys-1 alleles showed significantly less acetylcholinesterase-specific activity than wild-type controls. In addition, double mutants carrying a mutation in the dys-1 gene plus a mutation in either of the two major acetylcholinesterase genes (ace-1 and ace-2) display locomotor defects consistent with a strong reduction of acetylcholinesterases, whereas none of the single mutants does. Therefore, in C. elegans, disruption of the dystrophin/utrophin-like dys-1 gene affects acetylcholinesterase activity.
ESTHER : Giugia_1999_FEBS.Lett_463_270
PubMedSearch : Giugia_1999_FEBS.Lett_463_270
PubMedID: 10606735

Title : Structure and promoter activity of the 5' flanking region of ace-1, the gene encoding acetylcholinesterase of class A in caenorhabditis elegans - Culetto_1999_J.Mol.Biol_290_951
Author(s) : Culetto E , Combes D , Fedon Y , Roig A , Toutant JP , Arpagaus M
Ref : Journal of Molecular Biology , 290 :951 , 1999
Abstract : We report the structure and the functional activity of the promoter region of ace-1, the gene encoding acetylcholinesterase of class A in the nematode Caenorhabditis elegans. We found that ace-1 was trans -spliced to the SL1 spliced leader and that transcription was initiated at a cluster of multiple starts. There was neither a TATA nor a CAAT box at consensus distances from these starts. Interspecies sequence comparison of the 5' regions of ace-1 in C. elegans and in the related nematode Caenorhabditis briggsae identified four blocks of conserved sequences located within a sequence of 2.4 kilobases upstream from the initiator ATG. In vitro expression of CAT reporter genes in mammalian cells allowed the determination of a minimal promoter in the first 288 nucleotides. In phenotype rescue experiments in vivo, the ace-1 gene containing 2.4 kilobases of 5' flanking region of either C. elegans or C. briggsae was found to restore a coordinated mobility to the uncoordinated double mutants ace-1(-);ace-2(-)of C. elegans. This showed that the ace-1 promoter was contained in 2.4 kilobases of the 5' region, and indicated that cis -regulatory elements as well as coding sequences of ace-1 were functionally conserved between the two nematode species. The pattern of ace-1 expression was established through microinjection of Green Fluorescent Protein reporter gene constructs and showed a major mesodermal expression. Deletion analysis showed that two of the four blocks of conserved sequences act as tissue-specific activators. The distal block is a mesodermal enhancer responsible for the expression in body wall muscle cells, anal sphincter and vulval muscle cells. Another block of conserved sequence directs expression in pharyngeal muscle cells pm5 and three pairs of cephalic sensory neurons.
ESTHER : Culetto_1999_J.Mol.Biol_290_951
PubMedSearch : Culetto_1999_J.Mol.Biol_290_951
PubMedID: 10438595

Title : Molecular cloning and expression of a full-length cDNA encoding acetylcholinesterase in optic lobes of the squid Loligo opalescens: a new member of the cholinesterase family resistant to diisopropyl fluorophosphate - Talesa_1999_J.Neurochem_72_1250
Author(s) : Talesa V , Grauso M , Arpagaus M , Giovannini E , Romani R , Rosi G
Ref : Journal of Neurochemistry , 72 :1250 , 1999
Abstract : Acetylcholinesterase cDNA was cloned by screening a library from Loligo opalescens optic lobes; cDNA sequence analysis revealed an open reading frame coding for a protein of 610 amino acids that showed 20-41% amino acid identity with the acetylcholinesterases studied so far. The characteristic structure of cholinesterase (the choline binding site, the catalytic triad, and six cysteines that form three intrachain disulfide bonds) was conserved in the protein. The heterologous expression of acetylcholinesterase in COS cells gave a recovery of acetylcholinesterase activity 20-fold higher than in controls. The enzyme, partially purified by affinity chromatography, showed molecular and kinetic features indistinguishable from those of acetylcholinesterase expressed in vivo, which displays a high catalytic efficiency. Both enzymes are true acetylcholinesterase corresponding to phosphatidylinositol-anchored G2a dimers of class I, with a marked substrate specificity for acetylthiocholine. The deduced amino acid sequence may explain some particular kinetic characteristics of Loligo acetylcholinesterase, because the presence of a polar amino acid residue (S313) instead of a nonpolar one [F(288) in Torpedo] in the acyl pocket of the active site could justify the high substrate specificity of the enzyme, the absence of hydrolysis with butyrylthiocholine, and the poor inhibition by the organophosphate diisopropyl fluorophosphate.
ESTHER : Talesa_1999_J.Neurochem_72_1250
PubMedSearch : Talesa_1999_J.Neurochem_72_1250
PubMedID: 10037498
Gene_locus related to this paper: lolop-ACHE1

Title : Four Acetylcholinesterase Genes in the Nematodes caenorhabditis Elegans and Caenorhabditis Briggsae -
Author(s) : Culetto E , Grauso M , Combes D , Fedon Y , Romani R , Toutant JP , Arpagaus M
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :87 , 1998
PubMedID:

Title : Existence of four acetylcholinesterase genes in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae - Grauso_1998_FEBS.Lett_424_279
Author(s) : Grauso M , Culetto E , Combes D , Fedon Y , Toutant JP , Arpagaus M
Ref : FEBS Letters , 424 :279 , 1998
Abstract : Three genes, ace-1, ace-2 and ace-3, respectively located on chromosomes X, I and II, were reported to encode acetylcholinesterases (AChEs) of classes A, B and C in the nematode Caenorhabditis elegans. We have previously cloned and sequenced ace-1 in the two related species C. elegans and C. briggsae. We report here partial sequences of ace-2 (encoding class B) and of two other ace sequences located in close proximity on chromosome II in C. elegans and C. briggsae. These two sequences are provisionally named ace-x and ace-y, because it is not possible at the moment to establish which of these two genes corresponds to ace-3. Ace-x and ace-y are transcribed in vivo as shown by RT-PCR and they are likely to be included in a single operon.
ESTHER : Grauso_1998_FEBS.Lett_424_279
PubMedSearch : Grauso_1998_FEBS.Lett_424_279
PubMedID: 9539167
Gene_locus related to this paper: caebr-ACHE2 , caeel-ACHE2 , caeel-ACHE3 , caeel-ACHE4

Title : Four acetylcholinesterase genes in the nematode Caenorhabditis elegans - Arpagaus_1998_J.Physiol.Paris_92_363
Author(s) : Arpagaus M , Combes D , Culetto E , Grauso M , Fedon Y , Romani R , Toutant JP
Ref : Journal de Physiologie (Paris) , 92 :363 , 1998
Abstract : Whereas a single gene encodes acetylcholinesterase (AChE) in vertebrates and most insect species, four distinct genes have been cloned and characterized in the nematode Caenorhabditis elegans. We found that ace-1 (mapped to chromosome X) is prominently expressed in muscle cells whereas ace-2 (located on chromosome I) is mainly expressed in neurons. Ace-x and ace-y genes are located in close proximity on chromosome II where they are separated by only a few hundred base pairs. The role of these two genes is still unknown.
ESTHER : Arpagaus_1998_J.Physiol.Paris_92_363
PubMedSearch : Arpagaus_1998_J.Physiol.Paris_92_363
PubMedID: 9789838

Title : Four Acetylcholinesterase Genes in the Nematode Caenorhabditis Elegans - 1 -
Author(s) : Combes D , Culetto E , Grauso M , Romani R , Fedon Y , Toutant JP , Arpagaus M
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :136 , 1998
PubMedID:

Title : Molecular Cloning and Characterization of a cDNA Encoding AChE from Optic Lobe of Loligo Opalescences -
Author(s) : Talesa V , Grauso M , Arpagaus M , Giovannini E , Rosi G
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :143 , 1998
PubMedID:

Title : Researches on Cholinesterases and Plant Protection -
Author(s) : Berge JB , Arpagaus M
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :479 , 1998
PubMedID:

Title : Acetylcholinesterase and Insecticide Resistance in the Mosquito Culex Pipiens -
Author(s) : Bourguet D , Fournier D , Toutant JP , Arpagaus M , Raymond M
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :483 , 1998
PubMedID:

Title : Analysis of molecular forms and pharmacological properties of acetylcholinesterase in several mosquito species - Bourguet_1997_Neurochem.Int_31_65
Author(s) : Bourguet D , Roig A , Toutant JP , Arpagaus M
Ref : Neurochem Int , 31 :65 , 1997
Abstract : Two acetylcholinesterases (AChE1 and AChE2) have recently been characterized in the common mosquito Culex pipiens. This situation appeared to be an exception among insects, where only one acetylcholinesterase gene had previously been repeatedly reported. In the present study, acetylcholinesterase was studied in five mosquito species: Aedes aegypti, Anopheles gambiae, Anopheles stephensi, Culiseta longeareolata and Culex hortensis, in order to test whether or not two different acetylcholinesterase enzymes could be detected as occurs in C. pipiens. Molecular forms and catalytic properties of the enzyme show that only one enzyme species was detected in the five species. This suggests that a duplication of a single locus Ace probably occurred recently in the phylogeny tree leading to C. pipiens, and produced two distinct acetylcholinesterases: AchE1 and AChE2.
ESTHER : Bourguet_1997_Neurochem.Int_31_65
PubMedSearch : Bourguet_1997_Neurochem.Int_31_65
PubMedID: 9185166

Title : Sequence comparison of ACE-1, the gene encoding acetylcholinesterase of class A, in the two nematodes Caenorhabditis elegans and Caenorhabditis briggsae - Grauso_1996_DNA.Seq_6_217
Author(s) : Grauso M , Culetto E , Berge JB , Toutant JP , Arpagaus M
Ref : DNA Sequence , 6 :217 , 1996
Abstract : The ace-1 gene, which encodes acetylcholinesterase of class A, has been cloned and sequenced in C. briggsae and compared to its homologue in C. elegans. Both genes present an open reading frame of 1860 nucleotides. The percentages of identity are 80% and 95% at the nucleotide and aminoacid levels respectively. All residues characteristic of an acetylcholinesterase are found in conserved positions in C. briggsae ACE-1. The deduced C-terminus is hydrophilic, thus resembling the catalytic peptide T of vertebrate cholinesterases. Codon usage in both ace-1 genes appears to be lowly biased. This may indicate that these genes are lowly expressed. The splicing sites of the eight introns of ace-1 in C. elegans are conserved in C. briggsae, but introns are shorter in C. briggsae. No homology was found between intronic sequences in both species, except for the consensus border sequences.
ESTHER : Grauso_1996_DNA.Seq_6_217
PubMedSearch : Grauso_1996_DNA.Seq_6_217
PubMedID: 8912924
Gene_locus related to this paper: caebr-ACHE1

Title : Duplication of the Ace.1 locus in Culex pipiens mosquitoes from the Caribbean - Bourguet_1996_Biochem.Genet_34_351
Author(s) : Bourguet D , Raymond M , Bisset J , Pasteur N , Arpagaus M
Ref : Biochemical Genetics , 34 :351 , 1996
Abstract : In Culex pipiens mosquitoes, AChE1 encoded by the locus Ace.1 is the target of organophosphorus and carbamate insecticides. In several resistant strains homozygous for Ace.1RR, insensitive AChE1 is exclusively found. An unusual situation occurs in two Caribbean resistant strains where each mosquito, at each generation, displays a mixture of sensitive and insensitive AChE1. These mosquitoes are not heterozygotes, Ace.1RS, as preimaginal mortalities cannot account for the lethality of both homozygous classes. This situation is best explained by the existence of two Ace.1 loci, coding, respectively, a sensitive and an insensitive AChE1. Thus, we suggest that in the Caribbean a duplication of the Ace.1 locus occurred before the appearance of insecticide resistance at one of the two copies.
ESTHER : Bourguet_1996_Biochem.Genet_34_351
PubMedSearch : Bourguet_1996_Biochem.Genet_34_351
PubMedID: 8978907

Title : Existence of two acetylcholinesterases in the mosquito Culex pipiens (Diptera:Culicidae) - Bourguet_1996_J.Neurochem_67_2115
Author(s) : Bourguet D , Raymond M , Fournier D , Malcolm CA , Toutant JP , Arpagaus M
Ref : Journal of Neurochemistry , 67 :2115 , 1996
Abstract : Two acetylcholinesterases (AChEs), AChE1 and AChE2, differing in substrate specificity and in some aspects of inhibitor sensitivity, have been characterized in the mosquito Culex pipiens. The results of ultracentrifugation in sucrose gradients and nondenaturing gel electrophoresis of AChE activity peak fractions show that each AChE is present as two molecular forms: one amphiphilic dimer possessing a glycolipid anchor and one hydrophilic dimer that does not interact with nondenaturing detergents. Treatment by phosphatidylinositol-specific phospholipase C converts each type of amphiphilic dimer into the corresponding hydrophilic dimer. Molecular forms of AChE1 have a lower electrophoretic mobility than those of AChE2. However, amphiphilic dimers and hydrophilic dimers have similar sedimentation coefficients (5.5S and 6.5S, respectively). AChE1 and AChE2 dimers, amphiphilic or hydrophilic, resist dithiothreitol reduction under conditions that allow reduction of Drosophila AChE dimers. In the insecticide-susceptible strain S-LAB, AChE1 is inhibited by 5 x 10(-4) M propoxur (a carbamate insecticide), whereas AChE2 is resistant. All animals are killed by this concentration of propoxur, indicating that only AChE1 fulfills the physiological function of neurotransmitter hydrolysis at synapses. In the insecticide-resistant strain, MSE, there is no mortality after exposure to 5 x 10(-4) M propoxur: AChE2 sensitivity to propoxur is unchanged, whereas AChE1 is now resistant to 5 x 10(-4) M propoxur. The possibility that AChE1 and AChE2 are products of tissue-specific posttranslational modifications of a single gene is discussed, but we suggest, based on recent results obtained at the molecular level in mosquitoes, that they are encoded by two different genes.
ESTHER : Bourguet_1996_J.Neurochem_67_2115
PubMedSearch : Bourguet_1996_J.Neurochem_67_2115
PubMedID: 8863521

Title : Properties of Class a Acetylcholinesterase, the Enzyme Encoded by ACE-1 in Caenorhabditis elegans -
Author(s) : Arpagaus M , Schirru N , Culetto E , Talesa V , Cousin X , Chatonnet A , Fedon Y , Berge JB , Fournier D , Toutant JP
Ref : In Enzyme of the Cholinesterase Family - Proceedings of Fifth International Meeting on Cholinesterases , (Quinn, D.M., Balasubramanian, A.S., Doctor, B.P., Taylor, P., Eds) Plenum Publishing Corp. :7 , 1995
PubMedID:

Title : A Database of Sequences Related to AcetylcholinesteraselLipase\/alpha:beta Hydrolase Superfamily with Public Access on Internet -
Author(s) : Cousin X , Hotelier T , Mazzoni C , Arpagaus M , Toutant JP , Chatonnet A
Ref : In Enzyme of the Cholinesterase Family - Proceedings of Fifth International Meeting on Cholinesterases , (Quinn, D.M., Balasubramanian, A.S., Doctor, B.P., Taylor, P., Eds) Plenum Publishing Corp. :489 , 1995
PubMedID:

Title : Characterization of a null mutation in ace-1, the gene encoding class A acetylcholinesterase in the nematode Caenorhabditis elegans - Talesa_1995_FEBS.Lett_357_265
Author(s) : Talesa V , Culetto E , Schirru N , Bernardi H , Fedon Y , Toutant JP , Arpagaus M
Ref : FEBS Letters , 357 :265 , 1995
Abstract : Two genes (ace-1 and ace-2) encode two major classes (A and B) of acetylcholinesterase (AChE) in the nematode Caenorhabditis elegans. A null mutation in ace-1 (allele p1000) suppresses all acetylcholinesterase activity of class A. We have identified an opal mutation TGG (W99)-->TGA (Stop) as the only alteration in the mutated gene. This leads to a truncated protein (98 instead of 620 amino acids) with no enzymatic activity. The mutation also reduces the level of ace-1 transcripts to only 10% of that in wild-type animals. This most likely results from a destabilization of mRNA containing the nonsense message. In contrast, compensation of class B by class A AChE in the null mutant strain ace-2 takes place with unchanged ace-1 mRNA level and enzymatic activity similar to class A AChE.
ESTHER : Talesa_1995_FEBS.Lett_357_265
PubMedSearch : Talesa_1995_FEBS.Lett_357_265
PubMedID: 7835425
Gene_locus related to this paper: caeel-ACHE1

Title : cDNA sequence, gene structure, and in vitro expression of ace-1, the gene encoding acetylcholinesterase of class A in the nematode Caenorhabditis elegans - Arpagaus_1994_J.Biol.Chem_269_9957
Author(s) : Arpagaus M , Fedon Y , Cousin X , Chatonnet A , Berge JB , Fournier D , Toutant JP
Ref : Journal of Biological Chemistry , 269 :9957 , 1994
Abstract : Three genes, ace-1, ace-2, and ace-3, encode three acetylcholinesterase classes (A, B, and C) in the nematode Caenorhabditis elegans. A fragment of genomic DNA was amplified by a polymerase chain reaction (PCR) using degenerate oligonucleotides based on sequences conserved in the cholinesterase family. This fragment mapped to chromosome X at a position that perfectly matched the location of ace-1 previously determined by genetic methods. Comparison of genomic and cDNA sequences showed that the open reading frame was interrupted by eight introns. The product of ace-1 (ACE-1, 620 amino acids) presented 42% identity with Torpedo and human acetylcholinesterases, 41% with human butyrylcholinesterase, and 35% with Drosophila acetylcholinesterase. The overall structure of cholinesterases was conserved in ACE-1 as indicated by the conserved sequence positions of Ser-216, His-468, and Glu-346 (S200, H440, E327 in Torpedo (AChE) as components of the catalytic triad, of the six cysteines which form three intrachain disulfide bonds, and of Trp-99(84), a critical side chain in the choline binding site. Spodoptera Sf9 cells were infected by a recombinant baculovirus containing ace-1 cDNA. The secreted enzyme was active and existed as hydrophilic 5 and 11.5 S molecular forms. It hydrolyzed both acetylthiocholine and butyrylthiocholine and was inhibited by acetylthiocholine above 10 mM.
ESTHER : Arpagaus_1994_J.Biol.Chem_269_9957
PubMedSearch : Arpagaus_1994_J.Biol.Chem_269_9957
PubMedID: 8144590
Gene_locus related to this paper: caeel-ACHE1

Title : cDNA sequence, gene structure, and cholinesterase-like domains of an esterase from Caenorhabditis elegans mapped to chromosome V - Fedon_1993_DNA.Seq_3_347
Author(s) : Fedon Y , Cousin X , Toutant JP , Thierry-Mieg D , Arpagaus M
Ref : DNA Sequence , 3 :347 , 1993
Abstract : The structure of an esterase gene from Caenorhabditis elegans has been determined by comparison of the sequences in genomic and cDNA clones. The gene was mapped close to the center of chromosome V (1.7 centimorgans to the left of dpy-11) and is therefore distinct from the gut esterase gene ges-1. It possessed 7 short introns. The 5' splice site of intron 3 presented the sequence GC instead of the usual GT that was found in the other six introns. The cDNA was trans-spliced with the short leader SL1. The open reading frame indicated that a protein of 557 aminoacids was encoded. The deduced aminoacid sequence did not present a signal peptide at the N-terminal but a potential N-myristoylation site (GXXXS) provided that the initiator methionine was removed. This protein should therefore remain intracellular. Comparison of this C. elegans sequence to other protein sequences in databases, as well as the analysis of the secondary structure in the protein showed that it belongs to the subgroup of esterases in the alpha/beta hydrolase fold family.
ESTHER : Fedon_1993_DNA.Seq_3_347
PubMedSearch : Fedon_1993_DNA.Seq_3_347
PubMedID: 8219278
Gene_locus related to this paper: caeel-ester

Title : Acetylcholinesterases of the nematode Steinernema carpocapsae. Characterization of two types of amphiphilic forms differing in their mode of membrane association - Arpagaus_1992_Eur.J.Biochem_207_1101
Author(s) : Arpagaus M , Richier P , Berge JB , Toutant JP
Ref : European Journal of Biochemistry , 207 :1101 , 1992
Abstract : We analyzed the molecular forms of acetylcholinesterase (AChE) in the nematode Steinernema carpocapsae. Two major AChEs are involved in acetylcholine hydrolysis. The first class of AChE is highly sensitive to eserine (IC50 = 0.05 microM). The corresponding molecular forms are: an amphiphilic 14S form converted into a hydrophilic 14.5S form by mild proteolysis and two hydrophilic 12S and 7S forms. Reduction of the amphiphilic 14S form with 10 mM dithiothreitol produces hydrophilic 7S and 4S forms, indicating that it is an oligomer of hydrophilic catalytic subunits linked by disulfide bond(s) to a hydrophobic structural element that confers the amphiphilicity to the complex. Sedimentation coefficients suggest that 4S, 7S, 12S forms correspond to hydrophilic monomer, dimer, tetramer and that the 14S form is also a tetramer linked to one structural element. The second class of AChE is less sensitive to eserine (IC50 = 0.1 mM). Corresponding molecular forms are hydrophilic and amphiphilic 4S forms (monomers) and a major amphiphilic 7S form converted into a hydrophilic dimer by Bacillus thuringiensis phosphatidylinositol-specific phospholipase C. This amphiphilic 7S form thus possesses a glycolipid anchor. It appears that Steinernema (a very primitive invertebrate) presents AChEs with two types of membrane association that closely resemble those described for amphiphilic G2 and G4 forms of AChE in more evolved animals.
ESTHER : Arpagaus_1992_Eur.J.Biochem_207_1101
PubMedSearch : Arpagaus_1992_Eur.J.Biochem_207_1101
PubMedID: 1323459

Title : Glycolipid-anchored acetylcholinesterases from rabbit lymphocytes and erythrocytes differ in their sensitivity to phosphatidylinositol- specific phospholipase C - Richier_1992_Biochim.Biophys.Acta_1112_83
Author(s) : Richier P , Arpagaus M , Toutant JP
Ref : Biochimica & Biophysica Acta , 1112 :83 , 1992
Abstract : The type of membrane association of acetylcholinesterase (AChE, EC 3.1.1.7) was studied in rabbit lymphocytes and erythrocytes. In both cases, the unique AChE molecular form was an amphiphilic dimer (referred to as G2a) anchored in the membrane by a glycosylphosphatidylinositol. In lymphocytes, G2a AChE was directly converted into its hydrophilic G2h counterpart by a treatment with Bacillus thuringiensis phosphatidylinositol-phospholipase C (PI-PLC, EC 3.1.4.10). In erythrocytes, AChE was resistant to PI-PLC but was rendered sensitive by a prior deacylation with alkaline hydroxylamine. This observation suggests that, as previously reported for human erythrocyte AChE, an acylation of the inositol ring in the glycolipid anchor of rabbit erythrocyte AChE (that does not occur in lymphocytes) prevents the cleavage.
ESTHER : Richier_1992_Biochim.Biophys.Acta_1112_83
PubMedSearch : Richier_1992_Biochim.Biophys.Acta_1112_83
PubMedID: 1329966

Title : Nematode Acetylcholinesterases: Several Genes and Molecular Forms of Their Products -
Author(s) : Arpagaus M , Richier P
Ref : In Multidisciplinary approaches to cholinesterase functions - Proceedings of Fourth International Meeting on Cholinesterases , (Shafferman, A. and Velan, B., Eds) Plenum Press, New York :65 , 1992
PubMedID:

Title : Poster: Phylogeny of cholinesterases inferred by maximum parsimony method or distance matrix methods (Fitch-Margoliash and Neighbor Joining Methods) -
Author(s) : Cousin X , Toutant JP , Jbilo O , Chatonnet A , Arpagaus M
Ref : In: Cholinesterases: Structure, Function, Mechanism, Genetics, and Cell Biology , (Massoulie J, Barnard EA, Chatonnet A, Bacou F, Doctor BP, Quinn DM) American Chemical Society, Washington, DC :195 , 1991
PubMedID:

Title : Poster: Use of the polymerase chain reaction for homology probing of butyrylchoIinesterase (BCHE) in several animal species -
Author(s) : Arpagaus M , Vaughan TA , La Du BN , Lockridge O , Masson P , Chatonnet A , Newton M , Taylor P
Ref : In: Cholinesterases: Structure, Function, Mechanism, Genetics, and Cell Biology , (Massoulie J, Barnard EA, Chatonnet A, Bacou F, Doctor BP, Quinn DM) American Chemical Society, Washington, DC :194 , 1991
PubMedID:

Title : Poster: Nomenclature for human butyrylcholinesterase genetic variants identified by DNA sequencing -
Author(s) : Lockridge O , Bartels CF , Nogueira CP , Arpagaus M , Adkins S , La Du BN
Ref : In: Cholinesterases: Structure, Function, Mechanism, Genetics, and Cell Biology , (Massoulie J, Barnard EA, Chatonnet A, Bacou F, Doctor BP, Quinn DM) American Chemical Society, Washington, DC :193 , 1991
PubMedID:

Title : Poster: Search for alternative splicing of butyrylcholinesterase transcripts -
Author(s) : Jbilo O , Chatonnet A , Arpagaus M , Lockridge O
Ref : In: Cholinesterases: Structure, Function, Mechanism, Genetics, and Cell Biology , (Massoulie J, Barnard EA, Chatonnet A, Bacou F, Doctor BP, Quinn DM) American Chemical Society, Washington, DC :187 , 1991
PubMedID:

Title : Proposed nomenclature for human butyrylcholinesterase genetic variants identified by DNA sequencing - La Du_1991_Cell.Mol.Neurobiol_11_79
Author(s) : La Du BN , Bartels CF , Nogueira CP , Arpagaus M , Lockridge O
Ref : Cellular Molecular Neurobiology , 11 :79 , 1991
Abstract : 1. New information identifying nucleotide alterations of human butyrylcholinesterase allows the use of more specific nomenclature for the variants commonly known as atypical, fluoride, silent, and K variant. 2. In addition to suggesting a system of trivial names and abbreviations, we provide a list of formal names that follow the guidelines of the Committee for Human Gene Nomenclature. 3. It is suggested that formal names be included in publications whenever possible.
ESTHER : La Du_1991_Cell.Mol.Neurobiol_11_79
PubMedSearch : La Du_1991_Cell.Mol.Neurobiol_11_79
PubMedID: 2013061

Title : Use of the polymerase chain reaction for homology probing of butyrylcholinesterase from several vertebrates - Arpagaus_1991_J.Biol.Chem_266_6966
Author(s) : Arpagaus M , Chatonnet A , Masson P , Newton M , Vaughan TA , Bartels CF , Nogueira CP , La Du BN , Lockridge O
Ref : Journal of Biological Chemistry , 266 :6966 , 1991
Abstract : Genomic blots from man, monkey, cow, sheep, pig, rabbit, dog, rat, mouse, guinea pig, and chicken DNA were hybridized with probes derived from the four exons of the human butyrylcholinesterase gene (BCHE) (Arpagaus, M., Kott, M., Vatsis, K. P., Bartels, C. F., La Du, B. N., and Lockridge, O. (1990) Biochemistry 29, 124-131). Results showed that the BCHE gene was present in a single copy in the genome of all these vertebrates. The polymerase chain reaction was used to amplify genomic DNA from these animals with oligonucleotides derived from the human BCHE coding sequence. The amplified segment contained 423 bp of BCHE sequence including the active site serine of the enzyme (amino acid 198) and a component of the anionic site, aspartate 70. Amplification was successful for monkey, pig, cow, dog, sheep, and rabbit DNA, but unsuccessful for rat, guinea pig, mouse, and chicken DNA. Amplified segments were cloned in M13 and sequenced. The mouse sequence was obtained by sequencing a genomic clone. The highest identity of the human amino acid sequence was found with monkey (100%) and the lowest with mouse (91.5%). The sequence around the active site serine 198, Phe-Gly-Glu-Ser-Ala-Gly-Ala, was conserved in all eight animals as was the anionic site component, aspartate 70. A phylogenetic tree of mammalian butyrylcholinesterases was constructed using the partial BCHE sequences.
ESTHER : Arpagaus_1991_J.Biol.Chem_266_6966
PubMedSearch : Arpagaus_1991_J.Biol.Chem_266_6966
PubMedID: 2016308
Gene_locus related to this paper: bovin-BCHE , canfa-BCHE , macmu-BCHE , pig-BCHE , sheep-BCHE

Title : Poster: Drosophila Acetylcholinesterase in wild type flies and in thermosensitive or nonconditional mutants of the Ace locus -
Author(s) : Toutant JP , Arpagaus M
Ref : In: Cholinesterases: Structure, Function, Mechanism, Genetics, and Cell Biology , (Massoulie J, Barnard EA, Chatonnet A, Bacou F, Doctor BP, Quinn DM) American Chemical Society, Washington, DC :52 , 1991
PubMedID:

Title : Structure of the gene for human butyrylcholinesterase. Evidence for a single copy - Arpagaus_1990_Biochemistry_29_124
Author(s) : Arpagaus M , Kott M , Vatsis KP , Bartels CF , La Du BN , Lockridge O
Ref : Biochemistry , 29 :124 , 1990
Abstract : We have isolated five genomic clones for human butyrylcholinesterase (BChE), using cDNA probes encoding the catalytic subunit of the hydrophilic tetramer [McTiernan et al. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 6682-6686]. The BChE gene is at least 73 kb long and contains four exons. Exon 1 contains untranslated sequences and two potential translation initiation sites at codons -69 and -47. Exon 2 (1525 bp) contains 83% of the coding sequence for the mature protein, including the N-terminal and the active-site serine, and a third possible translation initiation site (likely functional), at codon -28. Exon 3 is 167 nucleotides long. Exon 4 (604 bp) codes for the C-terminus of the protein and the 3' untranslated region where two polyadenylation signals were identified. Intron 1 is 6.5 kb long, and the minimal sizes of introns 2 and 3 are estimated to be 32 kb each. Southern blot analysis of total human genomic DNA is in complete agreement with the gene structure established by restriction endonuclease mapping of the genomic clones: this strongly suggests that the BChE gene is present in a single copy.
ESTHER : Arpagaus_1990_Biochemistry_29_124
PubMedSearch : Arpagaus_1990_Biochemistry_29_124
PubMedID: 2322535

Title : Identification of a frameshift mutation responsible for the silent phenotype of human serum cholinesterase, Gly 117 (GGT----GGAG) - Nogueira_1990_Am.J.Hum.Genet_46_934
Author(s) : Nogueira CP , McGuire MC , Graeser C , Bartels CF , Arpagaus M , van der Spek AF , Lightstone H , Lockridge O , La Du BN
Ref : American Journal of Human Genetics , 46 :934 , 1990
Abstract : A frameshift mutation that causes a silent phenotype for human serum cholinesterase was identified in the DNA of seven individuals of two unrelated families. The mutation, identified using the polymerase chain reaction, causes a shift in the reading frame from Gly 117, where GGT (Gly)----GGAG (Gly+ 1 base) to a new stop codon created at position 129. This alteration is upstream of the active site (Ser 198), and, if any protein were made, it would represent only 22% of the mature enzyme found in normal serum. Results of analysis of the enzymatic activities in serum agreed with the genotypes inferred from the nucleotide sequence. Rocket immunoelectrophoresis using alpha-naphthyl acetate to detect enzymatic activity showed an absence of cross-reactive material, as expected. One additional individual with a silent phenotype did not show the same frameshift mutation. This was not unexpected, since there must be considerable molecular heterogeneity involved in causes for the silent cholinesterase phenotype. This is the first report of a molecular mechanism underlying the silent phenotype for serum cholinesterase. The analytical approach used was similar to the one we recently employed to identify the mutation that causes the atypical cholinesterase variant.
ESTHER : Nogueira_1990_Am.J.Hum.Genet_46_934
PubMedSearch : Nogueira_1990_Am.J.Hum.Genet_46_934
PubMedID: 2339692

Title : Native molecular forms of head acetylcholinesterase from adult Drosophila melanogaster: quaternary structure and hydrophobic character - Toutant_1988_J.Neurochem_50_209
Author(s) : Toutant JP , Arpagaus M , Fournier D
Ref : Journal of Neurochemistry , 50 :209 , 1988
Abstract : The native molecular forms of acetylcholinesterase (AChE) present in adult Drosophila heads were characterized by sedimentation analysis in sucrose gradients and by nondenaturing electrophoresis. The hydrophobic properties of AChE forms were studied by comparing their migration in the presence of Triton X100, 10-oleyl ether, or sodium deoxycholate, or in the absence of detergent. We examined the polymeric structure of AChE forms by disulfide bridge reduction. We found that the major native molecular form is an amphiphilic dimer which is converted into hydrophilic dimer and monomer on autolysis of the extracts, or into a catalytically active amphiphilic monomer by partial reduction. The latter component exists only as trace amounts in the native enzyme. Two additional minor native forms were identified as hydrophilic dimer and monomer. Although a significant proportion of AChE was only solubilized in high salt, following extractions in low salt, this high salt-soluble fraction contained the same molecular forms as the low salt-soluble fractions: thus, we did not detect any molecular form resembling the asymmetric forms of vertebrate cholinesterases.
ESTHER : Toutant_1988_J.Neurochem_50_209
PubMedSearch : Toutant_1988_J.Neurochem_50_209
PubMedID: 3121787