Toutant JP

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Full name : Toutant Jean-Pierre

First name : Jean-Pierre

Mail : INRA DCC, 2, place Viala, 34060 Montpellier

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Country : France

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References (76)

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 : New biosensors for improved detection of environmental and food contamination by anticholinesterase pesticides -
Author(s) : Toutant JP , Massoulie J , Fournier D , Marty JL , Schmid RD , Pfeiffer D , Selkirk ME , Sussman JL , Silman I , Talesa V , Wodak SJ , Stojan J , Magearu V
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :233 , 2004
PubMedID:

Title : Poster (24) New biosensors for improved detection of environmental contamination by anticholinesterase pesticides -
Author(s) : Toutant JP , Massoulie J , Fournier D , Schmid RD , Pfeiffer D , Selkirk ME , Sussman JL , Silman I , Talesa V , Wodak SJ
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :333 , 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 : Zebrafish acetylcholinesterase is encoded by a single gene localized on linkage group 7. Gene structure and polymorphism\; molecular forms and expression pattern during development - Bertrand_2001_J.Biol.Chem_276_464
Author(s) : Bertrand C , Chatonnet A , Takke C , Yan YL , Postlethwait J , Toutant JP , Cousin X
Ref : Journal of Biological Chemistry , 276 :464 , 2001
Abstract : We cloned and sequenced the acetylcholinesterase gene and cDNA of zebrafish, Danio rerio. We found a single gene (ache) located on linkage group LG7. The relative organization of ache, eng2, and shh genes is conserved between zebrafish and mammals and defines a synteny. Restriction fragment length polymorphism analysis was allowed to identify several allelic variations. We also identified two transposable elements in non-coding regions of the gene. Compared with other vertebrate acetylcholinesterase genes, ache gene contains no alternative splicing at 5' or 3' ends where only a T exon is present. The translated sequence is 60-80% identical to acetylcholinesterases of the vertebrates and exhibits an extra loop specific to teleosts. Analysis of molecular forms showed a transition, at the time of hatching, from the globular G4 form to asymmetric A12 form that becomes prominent in adults. In situ hybridization and enzymatic activity detection on whole embryos confirmed early expression of the acetylcholinesterase gene in nervous and muscular tissues. We found no butyrylcholinesterase gene or activity in Danio. These findings make zebrafish a promising model to study function of acetylcholinesterase during development and regulation of molecular forms assembly in vivo.
ESTHER : Bertrand_2001_J.Biol.Chem_276_464
PubMedSearch : Bertrand_2001_J.Biol.Chem_276_464
PubMedID: 11016933
Gene_locus related to this paper: danre-ACHE , danre-Q6P004

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 : Effects of carbofuran, diuron, and nicosulfuron on acetylcholinesterase activity in goldfish (Carassius auratus) - Bretaud_2000_Ecotoxicol.Environ.Saf_47_117
Author(s) : Bretaud S , Toutant JP , Saglio P
Ref : Ecotoxicology & Environmental Safety , 47 :117 , 2000
Abstract : Juvenile goldfish (Carassius auratus) were exposed to three widely used pesticides; carbofuran, diuron, and nicosulfuron. Acetylcholinesterase (AChE) activity and molecular forms of AChE were first characterized in brain and skeletal muscle of unexposed fish. Skeletal muscle had higher AChE activity than brain (306 and 215 nmol/min/mg protein, respectively). In brain, four molecular forms of AChE were found: A12, G4, G2, and G1. In the muscle, three molecular forms were found A12, A8, and G2. AChE activity was then evaluated in both tissues of fish exposed to different concentration of pesticides (5, 50, and 500 microg/L) for 6, 12, 24, and 48 h. In brain, AChE activity was significantly inhibited during all the periods of exposure in response to 50 microg/L (19-28%) and 500 microg/L (85-87%) carbofuran. Such effect was observed in the muscle only at 500 microg/L (86-92%). Carbofuran had no effect on the distribution of molecular forms. Significant inhibitions (9-12%) of brain AChE activity were also observed in response to diuron and nicosulfuron at 500 microg/L during all periods of exposure and for 50 microg/L nicosulfuron after 24 and 48 h. This study pointed out short-term effects of exposure to sublethal concentrations of the three pesticides, ranging among different chemical families, on brain and muscle AChE in goldfish.
ESTHER : Bretaud_2000_Ecotoxicol.Environ.Saf_47_117
PubMedSearch : Bretaud_2000_Ecotoxicol.Environ.Saf_47_117
PubMedID: 11023689

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 : 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 : Four Acetylcholinesterase Genes in the Nematode Caenorhabditis Elegans - 2 -
Author(s) : Grauso M , Culetto E , Combes D , Fedon Y , Toutant JP
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. :138 , 1998
PubMedID:

Title : Acetylcholinesterase Expression During Development of Danio Rerio -
Author(s) : Bertrand C , Cousin X , Toutant JP , Chatonnet A
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. :141 , 1998
PubMedID:

Title : The OECD Program: Biological Resource Management for Sustainable Agricultural Systems -
Author(s) : Toutant JP , Hokkanen H
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. :477 , 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 : 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 : Decay-accelerating factor (CD55) and membrane inhibitor of reactive lysis (CD59) are released within exosomes during In vitro maturation of reticulocytes - Rabesandratana_1998_Blood_91_2573
Author(s) : Rabesandratana H , Toutant JP , Reggio H , Vidal M
Ref : Blood , 91 :2573 , 1998
Abstract : Exosomes are membrane vesicles released by reticulocytes during their maturation into erythrocytes. They have a clearing function because of their enrichment with some proteins known to decrease or disappear from the cell surface during maturation, eg, acetylcholinesterase (AChE) and transferrin receptor (TfR), respectively. To better understand the molecular events leading to protein sorting in exosomes, we analyzed the expression of glycosylphosphatidylinositol (GPI)-anchored proteins on the exosome surface through a technique involving bead coupling and flow cytometry immunodetection. The presence of AChE, decay-accelerating factor (DAF), membrane inhibitor of reactive lysis (MIRL), and lymphocyte function-associated antigen 3 (LFA-3) on the surface of exosomes obtained from normal and paroxysmal nocturnal hemoglobinuria (PNH) reticulocytes, suggests that (1) the GPI anchor is efficiently sorted during exosome formation, (2) exosome release could account for the observed discrepancy in GPI-protein expression between reticulocytes and erythrocytes from PNH patients, and (3) exosomes could have another physiologic function related to controlling membrane attack complex formation.
ESTHER : Rabesandratana_1998_Blood_91_2573
PubMedSearch : Rabesandratana_1998_Blood_91_2573
PubMedID: 9516159

Title : aCHEdb: the database system for ESTHER, the alpha\/beta fold family of proteins and the Cholinesterase gene server - Cousin_1998_Nucleic.Acids.Res_26_226
Author(s) : Cousin X , Hotelier T , Giles K , Toutant JP , Chatonnet A
Ref : Nucleic Acids Research , 26 :226 , 1998
Abstract : Acetylcholinesterase belongs to a family of proteins, the alpha/beta hydrolase fold family, whose constituents evolutionarily diverged from a common ancestor and share a similar structure of a central beta sheet surrounded by alpha helices. These proteins fulfil a wide range of physiological functions (hydrolases, adhesion molecules, hormone precursors) [Krejci,E., Duval,N., Chatonnet,A., Vincens,P. and Massouli,J. (1991) Proc. Natl. Acad. Sci. USA , 88, 6647-6651]. ESTHER (for esterases, alpha/beta hydrolase enzymes and relatives) is a database aimed at collecting in one information system, sequence data together with biological annotations and experimental biochemical results related to the structure-function analysis of the enzymes of the family. The major upgrade of the database comes from the use of a new database management system: aCHEdb which uses the ACeDB program designed by Richard Durbin and Jean Thierry-Mieg. It can be found at http:\/\/http:bioweb.supagro.inra.fr/ESTHER
ESTHER : Cousin_1998_Nucleic.Acids.Res_26_226
PubMedSearch : Cousin_1998_Nucleic.Acids.Res_26_226
PubMedID: 9399841

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 : The alpha\/beta hydrolase fold family of proteins database and the cholinesterase gene server ESTHER - Cousin_1997_Nucleic.Acids.Res_25_143
Author(s) : Cousin X , Hotelier T , Giles K , Lievin P , Toutant JP , Chatonnet A
Ref : Nucleic Acids Research , 25 :143 , 1997
Abstract : ESTHER (for esterases, alpha/betahydrolase enzyme and relatives) is a database of sequences phylogenetically related to cholinesterases. These sequences define a homogeneous group of enzymes (carboxylesterases, lipases and hormone-sensitive lipases) sharing a similar structure of a central beta-sheet surrounded by alpha-helices. Among these proteins a wide range of functions can be found (hydrolases, adhesion molecules, hormone precursors). The purpose of ESTHER is to help comparison of structures and functions of members of the family. Since the last release, new features have been added to the server. A BLAST comparison tool allows sequence homology searches within the database sequences. New sections are available: kinetics and inhibitors of cholinesterases, fasciculin-acetylcholinesterase interaction and a gene structure review. The mutation analysis compilation has been improved with three-dimensional images. A mailing list has been created.
ESTHER : Cousin_1997_Nucleic.Acids.Res_25_143
PubMedSearch : Cousin_1997_Nucleic.Acids.Res_25_143
PubMedID: 9016525

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 : 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 : A cholinesterase genes server (ESTHER): a database of cholinesterase-related sequences for multiple alignments, phylogenetic relationships,mutations and structural data retrieval. - Cousin_1996_Nucleic.Acids.Res_24_132
Author(s) : Cousin X , Hotelier T , Lievin P , Toutant JP , Chatonnet A
Ref : Nucleic Acids Research , 24 :132 , 1996
Abstract : We have built a database of sequences phylogenetically related to cholinesterases (ESTHER) for esterases, alpha/beta hydrolase enzymes and relatives). These sequences define a homogeneous group of enzymes (carboxylesterases, lipases and hormone-sensitive lipases) with some related proteins devoid of enzymatic activity. The purpose of ESTHER is to help comparison and alignment of any new sequence appearing in the field, to favour mutation analysis of structure-function relationships and to allow structural data recovery. ESTHER is a World Wide Web server with the URL http://www.montpellier.inra.fr:70/cholinesterase.
ESTHER : Cousin_1996_Nucleic.Acids.Res_24_132
PubMedSearch : Cousin_1996_Nucleic.Acids.Res_24_132
PubMedID: 8594562

Title : Solubilization, molecular forms, purification and substrate specificity of two acetylcholinesterases in the medicinal leech (Hirudo medicinalis) - Talesa_1995_Biochem.J_306_687
Author(s) : Talesa V , Grauso M , Giovannini E , Rosi G , Toutant JP
Ref : Biochemical Journal , 306 :687 , 1995
Abstract : Two acetylcholinesterases (AChE) differing in substrate and inhibitor specificities have been characterized in the medical leech (Hirudo medicinalis). A 'spontaneously-soluble' portion of AChE activity (SS-AChE) was recovered from haemolymph and from tissues dilacerated in low-salt buffer. A second portion of AChE activity was obtained after extraction of tissues in low-salt buffer alone or containing 1% Triton X-100 [detergent-soluble (DS-) AChE). Both enzymes were purified to homogeneity by affinity chromatography on edrophonium- and concanavalin A-Sepharose columns. Denaturing SDS/PAGE under reducing conditions gave one band at 30 kDa for purified SS-AChE and 66 kDa for DS-AChE. Sephadex G-200 chromatography indicated a molecular mass of 66 kDa for native SS-AChE and of 130 kDa for DS-AChE. SS-AChE showed a single peak sedimenting at 5.0 S in sucrose gradients with or without Triton X-100, suggesting that it was a hydrophylic monomer (G1). DS-AChE sedimented as a single 6.1-6.5 S peak in the presence of Triton X-100 and aggregated in the absence of detergent. A treatment with phosphatidylinositol-specific phospholipase C suppressed aggregation and gave a 7 S peak. DS-AChE was thus an amphiphilic glycolipid-anchored dimer. Substrate specificities were studied using p-nitrophenyl esters (acetate, propionate and butyrate) and corresponding thiocholine esters as substrates. SS-AChE displayed only limited variations in Km values with charged and uncharged substrates, suggesting a reduced influence of electrostatic interactions in the enzyme substrate affinity. By contrast, DS-AChE displayed higher Km values with uncharged than with charged substrates. SS-AChE was more sensitive to eserine and di-isopropyl fluorophosphate (IC50 5 x 10(-8) and 10(-8) M respectively) than DS-AChE (5 x 10(-7) and 5 x 10(-5) M.
ESTHER : Talesa_1995_Biochem.J_306_687
PubMedSearch : Talesa_1995_Biochem.J_306_687
PubMedID: 7702560

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 : 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 : Butyrylcholinesterase Transcription Start Site and Promoter -
Author(s) : Jbilo O , Toutant JP , Chatonnet A , Lockridge O
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. :23 , 1995
PubMedID:

Title : Acetylcholinesterase in tentacles of Octopus vulgaris (Cephalopoda). Histochemical localization and characterization of a specific high salt-soluble and heparin-soluble fraction of globular forms - Talesa_1995_Neurochem.Int_27_201
Author(s) : Talesa V , Grauso M , Giovannini E , Rosi G , Toutant JP
Ref : Neurochem Int , 27 :201 , 1995
Abstract : Transverse sections of Octopus tentacles were stained for acetylcholinesterase (AChE) activity. An intense staining, that was suppressed by preincubation in 10(-5) M eserine, was detected in a number of neuronal cells, nerve fibres and neuromuscular junctions of intrinsic muscles of the arm. Octopus acetylcholinesterase was found as two molecular forms: an amphiphilic dimeric form (G2) sensitive to phosphatidylinositol phospholipase C and a hydrophilic tetrameric (G4) form. Sequential solubilization revealed that a significant portion of both G2 and G4 forms was recovered only in a high salt-soluble fraction (1 M NaCl, no detergent), Heparin (2 mg/ml) was able to solubilize G2 and G4 forms with the same efficiency than 1 M NaCl. The solubilizing effect of heparin was concentration-dependent and was reduced by protamine (2 mg/ml). This suggests that heparin operates through the dissociation of ionic interactions existing in situ between globular forms of AChE and cellular or extracellular polyanionic components. Interaction of AChE molecular forms with heparin has been reported so far in only a few instances and its physiological meaning is uncertain. G2 and G4 forms, interacting or not with heparin, all belong to a single pharmacological class of AChE. This suggests the existence of a single AChE gene. Amphiphilic and hydrophilic subunits thus likely result either from the processing of a single AChE transcript by alternative splicing (as in vertebrate AChE) or from a post-translation modification of a single catalytic peptide.
ESTHER : Talesa_1995_Neurochem.Int_27_201
PubMedSearch : Talesa_1995_Neurochem.Int_27_201
PubMedID: 7580876

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 : Acetylcholinesterase and Butyrylcholinesterase Expression in Adult Rabbit Tissues and during Development -
Author(s) : Jbilo O , L'Hermite Y , Talesa V , 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. :49 , 1995
PubMedID:

Title : Acetylcholinesterase from Octopus vulgaris (Cephalopoda) -
Author(s) : Talesa V , Grauso M , Giovannini E , Rosi G , 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. :127 , 1995
PubMedID:

Title : Molecular Polymorphism of Acetylcholinesterase in Hirudo medicinalis -
Author(s) : Talesa V , Grauso M , Giovannini E , Rosi G , 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. :128 , 1995
PubMedID:

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 : Promoter and transcription start site of human and rabbit butyrylcholinesterase genes - Jbilo_1994_J.Biol.Chem_269_20829
Author(s) : Jbilo O , Toutant JP , Vatsis KP , Chatonnet A , Lockridge O
Ref : Journal of Biological Chemistry , 269 :20829 , 1994
Abstract : Two kilobase segments of the 5'-untranslated regions of the human and rabbit butyrylcholinesterase (BCHE) genes were characterized. The sequences shared extensive identity except for a 333-base pair (bp) Alu repeat present only in human BCHE. One single transcription start site was found in both genes with the techniques of primer extension, amplification of the 5'-end of mRNA, and RNase protection. Cap sites in human and rabbit BCHE genes were found in strictly homologous positions. In human BCHE, the transcription start site was found 157 bp upstream of Met-28, the translation start site. Potential regulatory elements in both promoters included one AP1 site and multiple sites for topoisomerase, Oct-1 and PEA-3. Transient expression of BCHE-reporter gene constructs showed that a 194-bp fragment of the 5'-flanking region of human BCHE and a 570-bp fragment of rabbit BCHE were sufficient for promoting chloramphenicol acetyltransferase activity in HeLa cells. No consensus TATA and CAAT boxes were found. However, the sequence around the transcription start site exhibited homology with initiator elements found in other TATA-less promoters in developmentally regulated genes.
ESTHER : Jbilo_1994_J.Biol.Chem_269_20829
PubMedSearch : Jbilo_1994_J.Biol.Chem_269_20829
PubMedID: 8063698

Title : Acetylcholinesterase and butyrylcholinesterase expression in adult rabbit tissues and during development - Jbilo_1994_Eur.J.Biochem_225_115
Author(s) : Jbilo O , L'Hermite Y , Talesa V , Toutant JP , Chatonnet A
Ref : European Journal of Biochemistry , 225 :115 , 1994
Abstract : A large cDNA fragment covering the complete sequence of the mature catalytic subunit of rabbit acetylcholinesterase (AChE) has been cloned and sequenced. This sequence was compared to that of rabbit butyrylcholinesterase [BChE; Jbilo, O. & Chatonnet, A. (1990) Nucleic Acids Res. 18, 3990]. Amino acid sequences of AChE and BChE have 51% identity. They both possessed a choline-binding site W84, a catalytic triad S200-H440-E327 and six cysteine residues (positions 67-94, 254-265, 402-521) in conserved sequence positions to those that form three intrachain disulfide bonds in all cholinesterases (by convention, numbering of amino acids is that used for Torpedo AChE). Rabbit AChE had a larger number of aromatic residues lining the active-site gorge than rabbit BChE (14 compared to 8, respectively) and a smaller number of potential N-glycosylation sites (3 compared to 8, respectively). Both catalytic subunits have a hydrophilic C-terminus (catalytic subunits of type T). Expression of acetylcholinesterase and butyrylcholinesterase genes (ACHE and BCHE) was studied in rabbit tissues and during development by a correlation of Northern-blot analysis and enzymic activities. This correlation was rendered difficult by the presence of an eserine-resistant esterase active on butyrylthiocholine in serum, liver and lung. When the contribution of this carboxylesterase was taken into account, brain was found as the richest source of BChE followed by lung and heart. Rabbit liver had a very low content of BChE that correlated with the low BChE activity in plasma. During development, BCHE transcripts were detected as early as day 10 post coitum, whereas ACHE transcripts appeared only on day 12.
ESTHER : Jbilo_1994_Eur.J.Biochem_225_115
PubMedSearch : Jbilo_1994_Eur.J.Biochem_225_115
PubMedID: 7925428
Gene_locus related to this paper: rabit-ACHE , rabit-BCHE

Title : The molecular forms of acetylcholinesterase from Necator americanus (Nematoda), a hookworm parasite of the human intestine - Pritchard_1994_Eur.J.Biochem_219_317
Author(s) : Pritchard DI , Brown A , Toutant JP
Ref : European Journal of Biochemistry , 219 :317 , 1994
Abstract : Necator americanus (Nematoda: Strongyloidea), a human hookworm parasite, is known to release considerable amounts of acetylcholinesterase (AChE) [Pritchard, D. I., Leggett K. V., Rogan, M. T., McKean, P. G. & Brown, A. (1991) Necator americanus secretory acetylcholinesterase and its purification from excretory/secretory products by affinity chromatography, Parasite Immunol. 13, 187-199]. The present study deals with AChE activity recovered in sequential somatic extracts, and excretory/secretory products, of the adult stage of the parasite. 97% of AChE was extractable in low-salt and high-salt detergent-free buffers, and only 3% was solubilised by a further extraction in the presence of Triton X-100. AChE in all three extracts was affected by the AChE inhibitors eserine, bis(4-allyldimethylammoniumphenyl)pentan-3-one dibromide and edrophonium chloride, but was resistant to the effects of tetramonoisopropylpyrophosphortetramide, a butyrylcholinesterase inhibitor. Sucrose density centrifugation revealed that AChE in all somatic extracts (low-salt, high-salt and detergent) resolved almost exclusively as a single peak between 6.9-7.5 S, while excretory/secretory products resolved at 8.2 S. These values are all compatible with dimers of catalytic subunits and no evidence was found for the presence of higher oligomers such as asymmetric forms. The only sample to show a shift in sedimentation following the inclusion of detergent (Triton X-100, Brij 96) in the gradient was a component of the detergent-soluble extract, indicating the existence of a minor amphiphilic form. In low-salt-soluble and high-salt-soluble extracts, AChE was solubilised as a hydrophilic globular form, probably a dimeric G2. The analysis of diisopropylfluorophosphate-labelled extracts by SDS/PAGE, and unlabelled extracts by immunoblotting using a polyvalent antiserum to N. americanus AChE, indicated that the AChE isolated in each extract was biochemically and immunologically similar. The banding patterns obtained were comparable to that seen when purified AChE was analysed by SDS/PAGE and immunoblotted. This suggests that the basic catalytic subunit has a mass of 66-70 kDa with the active site being located in a 30-kDa domain. All experimental data indicate the existence of only one AChE class in Necator homologous to AChE of class B from Caenorhabditis elegans. The solubility characteristics and globular nature of this hookworm AChE suggest that its major function is as an excretory or secretory product. This again raises the question of the true biological function of this 'non-cholinergenic' nematode secretion.
ESTHER : Pritchard_1994_Eur.J.Biochem_219_317
PubMedSearch : Pritchard_1994_Eur.J.Biochem_219_317
PubMedID: 8306998

Title : Tissue distribution of human acetylcholinesterase and butyrylcholinesterase messenger RNA - Jbilo_1994_Toxicon_32_1445
Author(s) : Jbilo O , Bartels CF , Chatonnet A , Toutant JP , Lockridge O
Ref : Toxicon , 32 :1445 , 1994
Abstract : Cholinesterase inhibitors occur naturally in the calabar bean (eserine), green potatoes (solanine), insect-resistant crab apples, the coca plant (cocaine) and snake venom (fasciculin). There are also synthetic cholinesterase inhibitors, for example man-made insecticides. These inhibitors inactivate acetylcholinesterase and butyrylcholinesterase as well as other targets. From a study of the tissue distribution of acetylcholinesterase and butyrylcholinesterase mRNA by Northern blot analysis, we have found the highest levels of butyrylcholinesterase mRNA in the liver and lungs, tissues known as the principal detoxication sites of the human body. These results indicate that butyrylcholinesterase may be a first line of defense against poisons that are eaten or inhaled.
ESTHER : Jbilo_1994_Toxicon_32_1445
PubMedSearch : Jbilo_1994_Toxicon_32_1445
PubMedID: 7886701

Title : Butyrylcholinesterase amphiphilic forms of the mucosal cells of rat intestine bind heparin - Sine_1994_Biochem.Biophys.Res.Commun_201_1376
Author(s) : Sine JP , Toutant JP , Colas B
Ref : Biochemical & Biophysical Research Communications , 201 :1376 , 1994
Abstract : Mucosal cells of rat intestine express amphiphilic monomer (G1) and dimer (G2) as well as hydrophilic tetramer (G4) of butyrylcholinesterase (BChE). After incubation with heparin (3 and 15 microM), amphiphilic G2 form showed decreased migrations in nondenaturing electrophoresis whereas in these conditions, the mobility of hydrophilic forms from rat and human serum BChEs was unchanged. Sucrose gradient sedimentation and chromatography performed on HPLC gel filtration and on heparin-Sepharose confirmed that amphiphilic G1 and G2 forms were able to bind heparin. Increasing concentrations of heparin resulted in higher sizes of heparin-BChE complex. These properties of intestinal BChE may be related to the possible occurrence of endogenous heparin in this tissue.
ESTHER : Sine_1994_Biochem.Biophys.Res.Commun_201_1376
PubMedSearch : Sine_1994_Biochem.Biophys.Res.Commun_201_1376
PubMedID: 8024582

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 : Amphiphilic forms of butyrylcholinesterase in mucosal cells of rat intestine - Sine_1992_Biochemistry_31_10893
Author(s) : Sine JP , Toutant JP , Weigel P , Colas B
Ref : Biochemistry , 31 :10893 , 1992
Abstract : The properties of a cholinesterase from mucosal cells of rat intestine have been characterized. The enzyme was identified as butyrylcholinesterase because it was more sensitive to iso-OMPA (IC50 = 1.0 x 10(-6) M) than to BW284C51 (IC50 = 5.5 x 10(-5) M) and was not inhibited by substrate excess. It displayed a higher affinity for acetylthiocholine than for butyrylthiocholine. A major molecular form was observed sedimenting at 5.9 S. Two other minor molecular forms were identified as a hydrophilic tetramer (G4, sedimenting at 10.5 S) and a monomer (G1, sedimenting at 4.3 S). The 5.9 S component was referred to as "G" form (G for globular) and not "G2" as usual dimers for the following reasons: (i) the G form was unaffected by the reducing agents, beta-mercaptoethanol and dithiothreitol, which converted disulfide-linked dimers of acetylcholinesterase into monomers, (ii) the G form was shifted from 5.9 to 3.4 S when the sucrose gradient contained Triton X-100. This value of 3.4 S (in Triton X-100) appeared too low for a typical G2 form. The shift in the S value was partly reversible: the 3.4 S form resedimented at 5.2 S in the absence of detergent. The behavior of the G form in sucrose gradients indicated that it was amphiphilic. This was confirmed in nondenaturing electrophoreses and also by quantitative binding of the G form to octyl-Sepharose. The hydrophobic domain of the G form was not a glycolipid, as shown by its insensitivity to Bacillus thuringiensis phosphatidylinositol-specific phospholipase C and its nonaggregating properties in the absence of nondenaturing detergent.
ESTHER : Sine_1992_Biochemistry_31_10893
PubMedSearch : Sine_1992_Biochemistry_31_10893
PubMedID: 1420201

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 : 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: 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 : Amphiphilic G1 and G2 Forms of Acetylcholinesterase: Sensitivity or Resistance to Phosphatidylinositol-Specific Phospholipase C -
Author(s) : Toutant JP , Murray NR , Krall JA , Richards MK , Rosenberry TL
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 :12 , 1991
PubMedID:

Title : Structure and Function of Cholinesterase from Amphioxus -
Author(s) : Pezzementi L , Sanders M , Jenkins T , Holliman D , Toutant JP , Bradley RJ
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 :24 , 1991
PubMedID:

Title : Rapid analysis of glycolipid anchors in amphiphilic dimers of acetylcholinesterases - Toutant_1991_Cell.Mol.Neurobiol_11_219
Author(s) : Toutant JP , Krall JA , Richards MK , Rosenberry TL
Ref : Cellular Molecular Neurobiology , 11 :219 , 1991
Abstract : 1. We describe two simple procedures for the rapid identification of certain structural features of glycolipid anchors in acetylcholinesterases (AChEs). 2. Treatment with alkaline hydroxylamine (that cleaves ester-linked acyl chains but not ether-linked alkyl chains) converts molecules possessing a diacylglycerol, but not those with an alkylacylglycerol, into hydrophilic derivatives. AChEs in human and bovine erythrocytes possess an alkylacylglycerol (Roberts et al., J. Biol. Chem. 263:18766-18775, 1988; Biochem. Biophys. Res. Commun. 150:271-277, 1988) and are not converted to hydrophilic dimers by alkaline hydroxylamine. Amphiphilic dimers of AChE from Drosophila, from mouse erythrocytes, and from the human erythroleukaemia cell line K562 also resist the treatment with hydroxylamine and likely possess a terminal alkylacylglycerol. This indicates that the cellular pool of free glycolipids used as precursors of protein anchors is distinct from the pool of membrane phosphatidylinositols (which contain diacylglycerols). 3. Pretreatment with alkaline hydroxylamine is required to render the amphiphilic AChE from human erythrocytes susceptible to digestion by Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (PI-PLC) (Toutant et al., Eur. J. Biochem. 180:503-508, 1989). We show here that this is also the case for the AChE from mouse erythrocytes, which therefore likely possesses an additional acyl chain in the anchor that prevents the action of PI-PLC. 4. In two sublines of K562 cells (48 and 243), we observed that AChE either was directly susceptible to PI-PLC (243) or required a prior deacylation by alkaline hydroxylamine (48). This suggests that glycolipid anchors in AChE of K562-48 cells, but not those in AChE of K562-243 cells, contain the additional acylation demonstrated in AChE from human erythrocytes. These observations illustrate the cell specificity (and the lack of species-specificity) of the structure of glycolipid anchors.
ESTHER : Toutant_1991_Cell.Mol.Neurobiol_11_219
PubMedSearch : Toutant_1991_Cell.Mol.Neurobiol_11_219
PubMedID: 1849455

Title : Molecular forms of acetylcholinesterase in two sublines of human erythroleukemia K562 cells. Sensitivity or resistance to phosphatidylinositol-specific phospholipase C and biosynthesis - Toutant_1990_Eur.J.Biochem_187_31
Author(s) : Toutant JP , Richards MK , Krall JA , Rosenberry TL
Ref : European Journal of Biochemistry , 187 :31 , 1990
Abstract : Acetylcholinesterase (AChE) in K562 cells exists in two molecular forms. The major form, an amphiphilic dimer (G2a) which sediments at 5.3 S, and the minor form, an amphiphilic monomer (G1a) which sediments at 3.5 S. Extraction in the presence of the sulfhydryl alkylating agent N-ethylmaleimide was required to preserve the G2a form. In Triton X-100 extracts of the subline K562-243, phosphatidylinositol-specific phospholipase C (PtdIns-PLC) from Bacillus thuringiensis converted most of the G2a AChE into a hydrophilic dimer (G2h), indicating that the G2a form possessed a hydrophobic glycoinositol phospholipid that mediated its attachment to the membrane. Treatment of intact K562-243 cells with PtdIns-PLC released approximately 60% of the total AChE activity and provided an estimate of the externally exposed AChE. The direct conversion from an amphiphilic to a hydrophilic dimeric form by PtdIns-PLC was not obtained in extracts or intact cells of the subline K562-48. Instead, pretreatment with alkaline hydroxylamine was necessary to render the amphiphilic G2 form of this subline susceptible to digestion by the phospholipase. In this respect, the amphiphilic dimer of K562-48 AChE resembles the G2a form of human erythrocyte AChE, which is resistant to PtdIns-PLC because of the direct palmitoylation of an inositol hydroxyl group in the anchor [Roberts et al. (1988) J. Biol. Chem. 263, 18766-18775]. Release of this acyl chain by hydroxylamine renders the enzyme susceptible to PtdIns-PLC [Toutant et al. (1989) Eur. J. Biochem. 180, 503-508]. In both K562 sublines, sialidase decreased the migration of the G2a form but not of the G1a form of AChE. G1a forms thus appear to represent an intracellular pool of newly synthesized molecules residing in a compartment proximal to the trans-Golgi apparatus. The sialidase-resistant G1a molecules were also resistant to PtdIns-PLC digestion; possible explanations for this resistance are presented.
ESTHER : Toutant_1990_Eur.J.Biochem_187_31
PubMedSearch : Toutant_1990_Eur.J.Biochem_187_31
PubMedID: 2298208

Title : Conversion of human erythrocyte acetylcholinesterase from an amphiphilic to a hydrophilic form by phosphatidylinositol-specific phospholipase C and serum phospholipase D - Toutant_1989_Eur.J.Biochem_180_503
Author(s) : Toutant JP , Roberts WL , Murray NR , Rosenberry TL
Ref : European Journal of Biochemistry , 180 :503 , 1989
Abstract : Each catalytic subunit in the amphiphilic dimer of human erythrocyte acetylcholinesterase (AChE) is anchored in the plasma membrane exclusively by a glycoinositol phospholipid. In contrast to erythrocyte AChEs in other mammalian species, the human enzyme is resistant to direct cleavage by phosphatidylinositol-specific phospholipase C (PtdIns-specific PLC). The resistance is due to the existence of an additional fatty acyl chain on the inositol ring which blocks the action of PtdIns-specific PLC [Roberts et al. (1988) J. Biol. Chem. 263, 18766-18775]. In this report, nondenaturing polyacrylamide gel electrophoresis was applied to permit rapid and unambiguous distinction between amphiphilic AChE, in which each catalytic subunit binds one nonionic detergent micelle, and hydrophilic AChE, which does not interact with detergent. Deacylation of human erythrocyte AChE by an alkaline treatment with hydroxylamine rendered the amphiphilic AChE susceptible to PtdIns-specific PLC with the consequent release of hydrophilic AChE. Although serum anchor-specific phospholipase D (PLD) cleaves the intact human erythrocyte AChE anchor, this treatment, as judged by nondenaturing electrophoresis, did not release hydrophilic AChE. Hydroxylamine treatment before or after PLD digestion was necessary to achieve the conversion. These observations indicate that binding of a single detergent micelle was maintained when any of the three fatty acyl or alkyl groups in the human erythrocyte AChE anchor phospholipid were retained. For proteins that can be identified following nondenaturing gel electrophoresis, these procedures provide methods both for detecting glycoinositol phospholipid anchors resistant to PtdIns-specific PLC and for indicating fatty acyl and/or alkyl chains in these anchors.
ESTHER : Toutant_1989_Eur.J.Biochem_180_503
PubMedSearch : Toutant_1989_Eur.J.Biochem_180_503
PubMedID: 2540962

Title : Insect acetylcholinesterase: catalytic properties, tissue distribution and molecular forms -
Author(s) : Toutant JP
Ref : Prog Neurobiol , 32 :423 , 1989
PubMedID: 2660188

Title : Identification and analysis of glycoinositol phospholipid anchors in membrane proteins -
Author(s) : Rosenberry TL , Toutant JP , Haas R , Roberts WL
Ref : Methods Cell Biol , 32 :231 , 1989
PubMedID: 2481801

Title : Amphiphilic and nonamphiphilic forms of Torpedo cholinesterases: I. Solubility and aggregation properties - Bon_1988_J.Neurochem_51_776
Author(s) : Bon S , Toutant JP , Meflah K , Massoulie J
Ref : Journal of Neurochemistry , 51 :776 , 1988
Abstract : We report an analysis of the solubility and hydrophobic properties of the globular forms of acetylcholinesterase (AChE) and butyrylcholinesterase (BCHE) from various Torpedo tissues. We distinguish globular nonamphiphilic forms (Gna) from globular amphiphilic forms (Ga). The Ga forms bind micelles of detergent, as indicated by the following properties. They are converted by mild proteolysis into nonamphiphilic derivatives. Their Stokes radius in the presence of Triton X-100 is approximately 2 nm greater than that of their lytic derivatives. The G2a forms fall in two classes. Class I contains molecules that aggregate in the absence of detergent, when mixed with an AChE-depleted Triton X-100 extract from electric organ. AChE G2a forms from electric organs, nerves, skeletal muscle, and erythrocyte membranes correspond to this type, which is also detectable in detergent-soluble (DS) extracts of electric lobes and spinal cord. Class II forms never aggregate but only present a slight shift in sedimentation coefficient, in the presence or absence of detergent. This class contains the AChE G2a forms of plasma and of the low-salt-soluble (LSS) fractions from spinal cord and electric lobes. The heart possesses a BCHE G2a form of class II in LSS extracts, as well as a similar G1a form. G4a forms of AChE, which are solubilized only in the presence of detergent and aggregate in the absence of detergent, represent a large proportion of cholinesterase in DS extracts of nerves and spinal cord, together with a smaller component of G4a BCHE. These forms may be converted to nonamphiphilic derivatives by Pronase. Nonaggregating G4a forms exist at low levels in the plasma (BCHE) and in LSS extracts of nerves (BCHE) and spinal cord (AChE).
ESTHER : Bon_1988_J.Neurochem_51_776
PubMedSearch : Bon_1988_J.Neurochem_51_776
PubMedID: 3411326

Title : Amphiphilic and nonamphiphilic forms of Torpedo cholinesterases: II. Electrophoretic variants and phosphatidylinositol phospholipase C-sensitive and -insensitive forms - Bon_1988_J.Neurochem_51_786
Author(s) : Bon S , Toutant JP , Meflah K , Massoulie J
Ref : Journal of Neurochemistry , 51 :786 , 1988
Abstract : We report an electrophoretic analysis of the hydrophobic properties of the globular forms of acetylcholinesterase (AChE) and butyrylcholinesterase (BCHE) from various Torpedo tissues. In charge-shift electrophoresis, the rate of electrophoretic migration of globular amphiphilic forms (Ga) is increased at least twofold when the anionic detergent deoxycholate is added to Triton X-100, whereas that of globular nonamphiphilic forms (Gna) is not modified. The G2a forms of the first class, as defined by their aggregation properties, are converted to nonamphiphilic derivatives by phosphatidylinositol phospholipase C (PI-PLC) and human serum phospholipase D (PLD). AChE G2a forms from electric organs, nerves, skeletal muscle, and erythrocyte membranes correspond to this type, which also exists in very small quantities in detergent-solubilized extracts of electric lobes and spinal cord. They present different electrophoretic mobilities, so that each of these tissues contains a distinct "electromorph," or two in the case of electric organs. The G2a forms of the second class (AChE in plasma, BCHE in heart), as well as G4a forms of AChE and BCHE, are insensitive to PI-PLC and PLD but may be converted to nonamphiphilic derivatives by Pronase.
ESTHER : Bon_1988_J.Neurochem_51_786
PubMedSearch : Bon_1988_J.Neurochem_51_786
PubMedID: 3411327

Title : Expression of asymmetric forms of acetylcholinesterase during myogenesis in vitro - Toutant_1988_Rep.Nutr.Dev_28_693
Author(s) : Toutant JP
Ref : Reproduction, Nutrition, Developpement , 28 :693 , 1988
Abstract : Chick muscle cells differentiating in vitro in the absence of nerve cells produce asymmetric forms of acetylcholinesterase (AChE) only if they originate from muscles which accumulate these forms in ovo (i.e. after embryonic day 5). The presence of nerve cells does not induce the synthesis of A forms in cultures of 5 day-old myoblasts and does not increase their proportion in cultures of 7 day-old myoblasts. Thus, the capacity to synthesize (or assemble) the complex polymeric forms of AChE does not reflect a direct neural influence but might rather be considered as an intrinsic property of the "late" categories of myoblasts that sequentially occur during the differentiation of leg muscles. We studied the synthesis of ChE molecular forms in the mouse muscle C2 cell line. From these experiments we suggest that the synthesis of A forms (or their assembly) can take place as soon as the cells are withdrawn from the cell cycle, but does not require cell fusion by itself. These observations are related to other recent studies that challenge the validity of A forms as topographical/physiological markers of neuromuscular interactions.
ESTHER : Toutant_1988_Rep.Nutr.Dev_28_693
PubMedSearch : Toutant_1988_Rep.Nutr.Dev_28_693
PubMedID: 3187181

Title : Acetylcholinesterase from Apis mellifera head. Evidence for amphiphilic and hydrophilic forms characterized by Triton X-114 phase separation - Belzunces_1988_Biochem.J_255_463
Author(s) : Belzunces LP , Toutant JP , Bounias M
Ref : Biochemical Journal , 255 :463 , 1988
Abstract : The polymorphism of bee acetylcholinesterase was studied by sucrose-gradient-sedimentation analysis and non-denaturing electrophoretic analysis of fresh extracts. Lubrol-containing extracts exhibited only one form, which sedimented at 5 S when analysed on high-salt Lubrol-containing gradients and 6 S when analysed on low-salt Lubrol-containing gradients. The 5 S/6 S form aggregated upon removal of the detergent when sedimented on detergent-free gradients and was recovered in the detergent phase after Triton X-114 phase separation. Thus the 5 S/6 S enzyme corresponds to an amphiphilic acetylcholinesterase form. In detergent-free extracts three forms, whose apparent sedimentation coefficients are 14 S, 11 S and 7 S, were observed when sedimentations were performed on detergent-free gradients. Sedimentation analyses on detergent-containing gradients showed only a 5 S peak in high-salt detergent-free extracts and a 6 S peak, with a shoulder at about 7 S, in low-salt detergent-free extracts. Electrophoretic analysis in the presence of detergent demonstrated that the 14 S and 11 S peaks corresponded to aggregates of the 5 S/6 S form, whereas the 7 S peak corresponded to a hydrophilic acetylcholinesterase form which was recovered in the aqueous phase following Triton X-114 phase separation. The 5 S/6 S amphiphilic form could be converted into a 7.1 S hydrophilic form by phosphatidylinositol-specific phospholipase C digestion.
ESTHER : Belzunces_1988_Biochem.J_255_463
PubMedSearch : Belzunces_1988_Biochem.J_255_463
PubMedID: 2849414

Title : Vertebrate Cholinesterases: Structure and Types of Interaction -
Author(s) : Massoulie J , Toutant JP
Ref : Handbook of Experimental Pharmacology , 86 :167 , 1988
PubMedID:

Title : Cholinesterases: Tissue and Cellular Distribution of Molecular Forms and Their Physiological Regulation -
Author(s) : Toutant JP , Massoulie J
Ref : Handbook of Experimental Pharmacology , 86 :225 , 1988
PubMedID:

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

Title : Polymorphism of pseudocholinesterase in Torpedo marmorata tissues: comparative study of the catalytic and molecular properties of this enzyme with acetylcholinesterase - Toutant_1985_J.Neurochem_44_580
Author(s) : Toutant JP , Massoulie J , Bon S
Ref : Journal of Neurochemistry , 44 :580 , 1985
Abstract : We report the existence, in Torpedo marmorata tissues, of a cholinesterase species (sensitive to 10(-5) M eserine) that differs from acetylcholinesterase (AChE, EC 3.1.1.7) in several respects: (a) The enzyme hydrolyzes butyrylthiocholine (BuSCh) at about 30% of the rate at which it hydrolyzes acetylthiocholine (AcSCh), whereas Torpedo AChE does not show any activity on BuSCh. (b) It is not inhibited by 10(-5) M BW 284C51, but rapidly inactivated by 10(-8) M diisopropylfluorophosphonate. (c) It does not exhibit inhibition by excess substrate up to 5 X 10(-3) M AcSCh. (d) It does not cross-react with anti-AChE antibodies raised against purified Torpedo AChE. This enzyme is obviously homologous to the "nonspecific" or pseudocholinesterase (pseudo-ChE, EC 3.1.1.8) that exists in other species, although it is closer to "true" AChE than classic pseudo-ChE in several respects. Thus, it shows the highest Vmax with acetyl-, and not propionyl- or butyrylthiocholine, and it is not specifically sensitive to ethopropazine. Pseudo-ChE is apparently absent from the electric organs, but represents the only cholinesterase species in the heart ventricle. Pseudo-ChE and AChE coexist in the spinal cord and in blood plasma, where they contribute to AcSCh hydrolysis in comparable proportions. Pseudo-ChE exists in several molecular forms, including collagen-tailed forms, which can be considered as homologous to those of AChE. In the heart the major component of pseudo-ChE appears to be a soluble monomeric form (G1). This form is inactivated by Triton X-100 within days.
ESTHER : Toutant_1985_J.Neurochem_44_580
PubMedSearch : Toutant_1985_J.Neurochem_44_580
PubMedID: 2578181

Title : Poster 11 Acetylcholinesterase molecular forms in Torpedo marmorata: Tissue specificity and hydrophobic character -
Author(s) : Toutant JP , Bon S
Ref : In: Cholinesterases, fundamental and applied aspects : proceedings of the Second International Meeting on Cholinesterases , (Brzin M, Barnard EA, Sket D, Eds) De Gruyter , 1984
PubMedID:

Title : Poster 26. BIochemical, evidences for two types of myoblastes during chick embryogenesis -
Author(s) : Toutant JP , Toutant M
Ref : In: Cholinesterases, fundamental and applied aspects : proceedings of the Second International Meeting on Cholinesterases , (Brzin M, Barnard EA, Sket D, Eds) De Gruyter , 1984
PubMedID:

Title : The polymorphism of cholinesterases: classification of molecular forms\; Interactions and solubilization characteristics metabolic relationships and regulations -
Author(s) : Massoulie J , Bon S , Lazar M , Grassi J , Marsh D , Meflah K , Toutant JP , Vallette FM , Vigny M
Ref : In: Cholinesterases, fundamental and applied aspects : proceedings of the Second International Meeting on Cholinesterases , (Brzin M, Barnard EA, Sket D, Eds) De Gruyter :73 , 1984
PubMedID:

Title : Potential phasic and tonic muscles express a common set of fast and slow myosin light chains and fast tropomyosin during early development of chick embryo - Toutant_1983_Biochimie_65_637
Author(s) : Toutant M , Toutant JP , Montarras D , Fiszman MY
Ref : Biochimie , 65 :637 , 1983
Abstract : We investigated the expression of myosin light chains and tropomyosin subunits during chick embryonic development of the anterior (ALD) and posterior (PLD) parts of the latissimus dorsi muscles. As early as day 8 in ovo, both muscles accumulate a common set of myosin light chains (LC) in similar ratios (LC1F: 55 per cent; LC2S: 25 per cent; LC2F: 12 per cent; LC1S: 8 per cent) and a common set of tropomyosin (TM) subunits (beta 2, beta 1, alpha 2F). Later during development, the slow components of the LC regularly disappear in the PLD and the fast components of the LC and the alpha 2FTM disappear in the ALD, so that the adult pattern is almost established at the time of hatching. Thus, early in development, the two muscles accumulate a common set of fast and slow myosin light chains and fast tropomyosin and some isoforms are repressed at a later stage during development. These data might suggest that during development, the regulatory mechanisms of muscle specific isoform expression differ from one contractile protein to another.
ESTHER : Toutant_1983_Biochimie_65_637
PubMedSearch : Toutant_1983_Biochimie_65_637
PubMedID: 6673743

Title : Histochemical properties and innervation pattern of fast and slow-tonic fibre types of the anterior latissimus dorsi muscle of the chick - Rouaud_1982_Histochem.J_14_415
Author(s) : Rouaud T , Toutant JP
Ref : Histochemical Journal , 14 :415 , 1982
Abstract : The anterior latissimus dorsi muscle of the chick is largely composed of slow-tonic fibres but contains a few fast fibres defined by their acid-labile, alkali-stable myofibrillar ATPase activity. These fibres are referred to as alpha fibres. Differing from the slow-tonic (alpha' and beta') fibres which are multiply innervated with en grappe endings, the alpha (fast) fibres are innervated by typical en plaque endings. The innervation of thirty-two alpha fibres were studied closely and it was concluded that about a half of the alpha fibres were focally innervated whereas a half were innervated in two distinct loci by en plaque endings. In only one case, a fast fibre with three widely spaced en plaque endings was observed. The mean intersynaptic length was significantly larger on alpha fibres than on alpha' and beta' fibres. No variation in the histochemical properties of myofibrillar ATPase was observed either along the entire length of singly and dually innervated alpha fibres, or along alpha' and beta' fibres. It is concluded that the three extrafusal fibre types of the anterior latissimus dorsi muscle maintain uniform histochemical characteristics along their length in spite of a possible innervation by several motoneurons.
ESTHER : Rouaud_1982_Histochem.J_14_415
PubMedSearch : Rouaud_1982_Histochem.J_14_415
PubMedID: 6214527

Title : [Effect of the type of muscle fiber innervation on the acquisition of myofibrillar ATPase properties] - Toutant_1982_Reprod.Nutr.Dev_22_243
Author(s) : Toutant JP
Ref : Reprod Nutr Dev , 22 :243 , 1982
Abstract : We present some observations differing from the idea that neurons precisely control the differentiation of muscle fibre histochemical properties and show that, in a few cases, innervation does not influence the development of myofibrillar ATPase properties. Moreover, we report that a regional variation of the acid stability of myofibrillar ATPase may occur in the polar zone of intrafusal fibres in chick PLD muscle spindles, a zone devoid of innervation. This observation is related to a similar variation in the polar zone of rat intrafusal fibres (Kucera et al., 1978). New examples are presented supporting the conclusion that the differentiation of the properties of ATPase activity, and thus of fibre types, takes place, at least in some cases, independently of the type of innervation received.
ESTHER : Toutant_1982_Reprod.Nutr.Dev_22_243
PubMedSearch : Toutant_1982_Reprod.Nutr.Dev_22_243
PubMedID: 6218548

Title : Effects of spinal cord stimulation on the differentiation of posterior latissimus dorsi nerve in the chick embryo -
Author(s) : Toutant M , Toutant JP , Renaud D , Le Douarin GH
Ref : Experimental Neurology , 72 :267 , 1981
PubMedID: 7238689

Title : Histochemical properties of the biventer cervicis muscle of the chick: a relationship between multiple innervation and slow-tonic fibre types - Toutant_1981_Histochem.J_13_481
Author(s) : Toutant JP , Rouaud T , Le Douarin GH
Ref : Histochemical Journal , 13 :481 , 1981
Abstract : Chick biventer cervicis muscle fibres have been studied histochemically. Fast-twitch, focally innervated (alpha) fibres represent 70-80% of the total fibres in this muscles. Two histochemical profiles of slow-tonic multi-innervated (beta) fibres have been observed from embryonic life the adult (three-months) stage. These two slow-tonic types differ in the activity of their histochemically demonstrated myofibrillar ATPase after either acid or alkaline preincubation, and after formalin fixation. Both slow-tonic fibre types have a high oxidative metabolism and are PAS-negative. They are referred as to beta 1 and beta 2R fibre types (slow-tonic oxidative) in an expansion of Ashmore's nomenclature, and compared to avian slow-tonic sub-types that have been described in recent reports. beta 1 and beta 2 fibre types exhibit a similar pattern of innervation. Possible explanations of the origin of histochemical heterogeneity in multiple innervated fibres are discussed.
ESTHER : Toutant_1981_Histochem.J_13_481
PubMedSearch : Toutant_1981_Histochem.J_13_481
PubMedID: 6166596

Title : Morphological and histochemical differentiation of intrafusal fibres in the posterior latissimus dorsi muscle of the developing chick - Toutant_1981_Anat.Embryol.(Berl)_162_325
Author(s) : Toutant M , Bourgeois JP , Rouaud T , Toutant JP
Ref : Anatomy & Embryology (Berl) , 162 :325 , 1981
Abstract : Morphological and histochemical differentiation of neuromuscular spindles was studied in the posterior latissimus dorsi (PLD) of the chick during embryonic and post-hatching development. A rapid increase in the number of spindles takes place between the 13th and 15th of embryonic life. By the 15th day in ovo, the spindle capsule appears filled with numerous contiguous cells. Large sensory endings and small primitive motor endings are observed on intrafusal fibres. Ultrastructural observations of the nerve supply of the spindles confirm that each developing spindle receives one thick Ia axon with one to three thin gamma axons. The intracapsular space differentiates by the 17th day of embryonic development. All intrafusal fibres are morphologically of the nuclear-chain type, while two fibre types are distinguished as early as the 14th day of embryonic life, when myofibrillar ATPase activity is demonstrated after acid preincubation. These two histochemical types of intrafusal fibres are also described in the adult. The relation between these two histochemical types and different functional activity of intrafusal fibres is suggested.
ESTHER : Toutant_1981_Anat.Embryol.(Berl)_162_325
PubMedSearch : Toutant_1981_Anat.Embryol.(Berl)_162_325
PubMedID: 6455939

Title : [Effects of chronic medullary stimulation on the total number of sites of acetylcholinesterase activity of the posterior latissimus dorsi muscle of chick embryo]. [French] - Toutant_1981_C.R.Acad.Sci.III_292_771
Author(s) : Toutant M , Toutant JP , Renaud D , Le Douarin GH , Changeux JP
Ref : Comptes Rendus de l Academie des Sciences , 292 :771 , 1981
Abstract : From incubation day 10 to 15, the spinal cord of Chick embryos are electrically stimulated in ovo at 0.5 Hz at the level of the motor roots innervating the latissimus dorsi muscles. As a consequence, the total number of spots of acetylcholinesterase determined on serial sections of posterior latissimus dorsi muscle increased 2.3 fold. This increase parallels that of acetylcholine receptor clusters, supporting the interpretation that these clusters are of synaptic origin.
ESTHER : Toutant_1981_C.R.Acad.Sci.III_292_771
PubMedSearch : Toutant_1981_C.R.Acad.Sci.III_292_771
PubMedID: 6788396

Title : Chronic stimulation of the spinal cord in developing chick embryo causes the differentiation of multiple clusters of acetylcholine receptor in the posterior latissimus dorsi muscle -
Author(s) : Toutant M , Bourgeois JP , Toutant JP , Renaud D , Le Douarin GH , Changeux JP
Ref : Developmental Biology , 76 :384 , 1980
PubMedID: 7390009

Title : Histochemical differentiation of extrafusal muscle fibres of the anterior latissimus dorsi in the chick - Toutant_1980_Cell.Differentiation_9_305
Author(s) : Toutant JP , Toutant M , Renaud D , Le Douarin GH
Ref : Cell Differentiation , 9 :305 , 1980
Abstract : Histochemical differentiation of the chick anterior latissimus dorsi (ALD) muscle was studied during embryonic development and after hatching. The two types of adult ALD tonic fibres (alpha' and beta') differentiate from a pool of acid and alkali-stable myofibrillar ATPase fibres. Intermediate stages of the transformation from beta' to alpha' were observed. At all developmental stages studied, a low percentage of formalin-resistant, alkali-stable and acid-labile ATPase fibres were observed. Such fibres have the histochemical properties of the alpha R or fast oxidative-glycolytic fibres and are assumed to be focally innervated.
ESTHER : Toutant_1980_Cell.Differentiation_9_305
PubMedSearch : Toutant_1980_Cell.Differentiation_9_305
PubMedID: 6449292

Title : Effect of heterotopic innervation on the development of synaptic pattern in chick embryo muscles - Khaskiye_1980_Arch.Anat.Micro.Morphol.Exp_69_135
Author(s) : Khaskiye A , Toutant JP , Toutant M , Renaud D , Le Douarin GH
Ref : Archives d Anatomie Microscopique et de Morphologie Experimentale , 69 :135 , 1980
Abstract : Heterotopic transplantations of fragments of neural tube have been performed in the chick embryo on stage 22 somites. Brachial motor centres were replaced by a posterior segment of spinal cord. As a result, synpatic patterns of Posterior Latissimus Dorsi (PLD) and Anterior Latissimus Dorsi (ALD) were modified : PLD exhibited numerous muscle fibers with a distributed innervation and ALD fibers had a large variability of intersynaptic lengths. Histochemical properties of myofibrillar ATPase activity in ALD and PLD muscles were close to those in controls, in spite of change in the innervation supply.
ESTHER : Khaskiye_1980_Arch.Anat.Micro.Morphol.Exp_69_135
PubMedSearch : Khaskiye_1980_Arch.Anat.Micro.Morphol.Exp_69_135
PubMedID: 6449906

Title : Enzymatic differentiation of muscle fibre types in embryonic latissimus dorsii of the chick: effects of spinal cord stimulation -
Author(s) : Toutant JP , Toutant M , Renaud D , Le Douarin GH
Ref : Cell Differentiation , 8 :375 , 1979
PubMedID: 160288