Cholinesterases: Tissue and Cellular Distribution of Molecular Forms and Their Physiological Regulation

Toutant, Jean‐Pierre; Massoulié, Jean

doi:10.1007/978-3-642-73220-1_9

Cited by 46 publications

(19 citation statements)

References 266 publications

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“…Section 1734 solely to indicate this fact. 1 The abbreviations used are: AChE, acetylcholinesterase (EC 3.1.1.7); PCR, polymerase chain reaction; RAGE, rapid amplification of genomic ends; RACE, rapid amplification of cDNA ends; kb, kilobase(s); bp, base pair(s); nt, nucleotide(s); SV, simian virus. multiple cloning site, 5Ј position at 551), and pBSK595 (22 nt antisense, nested 5Ј to pBSK551).…”

Section: Methodsmentioning

confidence: 99%

“…The best characterized function of acetylcholinesterase (AChE) 1 is to terminate cholinergic neurotransmission by hydrolyzing synaptic acetylcholine. AChE is expressed in many tissues, in multiple molecular forms (1,2).…”

mentioning

confidence: 99%

“…AChE is expressed in many tissues, in multiple molecular forms (1,2). These molecular forms share identical catalytic properties but differ in hydrodynamic behavior, subunit assembly, and mode of association with the cell surface (2,3).…”

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confidence: 99%

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Novel Messenger RNA and Alternative Promoter for Murine Acetylcholinesterase

Atanasova¹,

Chiappa²,

Wieben³

et al. 1999

Journal of Biological Chemistry

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A portion of the 5-flanking region of murine acetylcholinesterase was cloned from genomic DNA by 5-rapid amplification of genomic ends, identified in a mouse genomic library, and sequenced. Multiple potential binding sites for universal and tissue-specific transcription factors were suggestive of a promoter region within this DNA sequence. Potential promoter activity was confirmed by coupling the new sequence to the open reading frame of a luciferase reporter gene in transient expression experiments with nerve and muscle cells. 5-Rapid amplification of cDNA ends with templates from multiple sources revealed a novel transcription start site (at position ؊626, relative to translation start), located 32 bases downstream from a TATAA sequence. This start site appeared to mark a novel exon (1a) comprising 291 base pairs between positions ؊335 and ؊626, relative to the translation start. Supporting this conclusion, polymerase chain reactions with cDNA from mouse brain, heart, and other tissues, consistently amplified a transcript containing the exon 1a sequence fused to the invariant sequence beginning at position ؊22 in exon 2, but lacking exon 1. Northern blot analyses confirmed the in vivo expression of exon 1a-containing transcripts, especially in heart, brain, liver, and kidney. These results indicate that the murine acetylcholinesterase gene has a functioning alternative promoter that may influence expression of acetylcholinesterase in certain tissues.

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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Novel Messenger RNA and Alternative Promoter for Murine Acetylcholinesterase

Atanasova¹,

Chiappa²,

Wieben³

et al. 1999

Journal of Biological Chemistry

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“…Chez les poissons, comme chez les autres vertébrés, l'innervation motrice des muscles est cholinergique et il existe de nombreuses zones cholinergiques centrales, associées en particulier aux systèmes sensoriels. D'autre part, aux stades précoces du développement, de l'AChE est produite sans rapport avec une quelconque innervation cholinergique (revue dans TOUTANT et MASSOULIÉ, 1988). A ces stades, l'AChE pourrait se comporter non comme une enzyme mais comme une molécule d'adhérence cellulaire par l'intermédiaire d'un domaine de la molécule présentant des homologies avec la glutactine et la neurotactine (KREJCI etal., 1991 ;DARBOUX etal., 1996).…”

Section: Introductionunclassified

L'acétylcholinestérase des poissons, cible des organophosphorés et des carbamates. Caractérisation du gène et des formes moléculaires de l'enzyme chez Danio rerio. Effets des anticholinestérasiques

Castro¹,

Cousin²,

Haubruge

et al. 1998

Bull. Fr. Pêche Piscic.

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“…These are acetylcholinesterase (acetylcholine acetyihydrolase, EC 3.1.1.7, ACHE)' (1) and butyrylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8, CHE [2,3]). Both enzymes can hydrolyze the neurotransmitter acetylcholine (4,5) and both may be found in large amounts in various embryonic and tumor tissues (6), concomitant with cell division and DNA synthesis (7). Using the re-1.…”

Section: Introductionmentioning

confidence: 99%

Acetylcholinesterase and butyrylcholinesterase genes coamplify in primary ovarian carcinomas.

Zakut

Ehrlich²,

Ayalon³

et al. 1990

J. Clin. Invest.

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The genes for acetylcholinesterase (ACHE) and butyrylcholinesterase (CHE) are expressed in multiple tumor tissues, including ovarian carcinomas. Both CHE and ACHE genes coamplify in leukemias. To examine the relationship of gene amplification to the expression of these genes in tumors, ACHE and CHE genes and their expression were studied in primary ovarian carcinomas. DNA blot hybridization demonstrated a significant amplification and mutagenesis of both genes in 6 of 11 malignant tumors studied. This was greater or of the same order of magnitude as the amplification of the oncogenes c-rafi, v-sis, and c-fes in these tumors. No amplification was found in normal ovarian tissues or benign ovarian cysts. Xenopus oocyte microinjections, blot and in situ hybridizations, and immuno-and cytochemical staining revealed translatable CHEmRNA and its active protein product in discrete tumor foci. The frequent coamplification in ovarian carcinomas of ACHE and CHE genes implicates cholinesterases in neoplastic growth and/or proliferation. (J. Clin. Invest. 1990. 86:900-908.)

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Cholinesterases: Tissue and Cellular Distribution of Molecular Forms and Their Physiological Regulation

Cited by 46 publications

References 266 publications

Novel Messenger RNA and Alternative Promoter for Murine Acetylcholinesterase

Novel Messenger RNA and Alternative Promoter for Murine Acetylcholinesterase

L'acétylcholinestérase des poissons, cible des organophosphorés et des carbamates. Caractérisation du gène et des formes moléculaires de l'enzyme chez Danio rerio. Effets des anticholinestérasiques

Acetylcholinesterase and butyrylcholinesterase genes coamplify in primary ovarian carcinomas.

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