Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Acetylcholinesterase exists predominantly as a secreted enzyme which remains cell-associated at specific extracellular locations. Its extensive structural diversity appears responsible for the unique cellular disposition of the enzyme. To examine the molecular basis of the structural divergence of acetylcholinesterase species, we hybridized total RNA from Torpedo californica electric organ with restriction fragments from a cDNA encoding the catalytic subunits of asymmetric species of acetylcholinesterase. Multiple RNA species up to 14 kilobases in length can be detected on Northern blots using a full-length cDNA for hybridization. Each of these RNA species also hybridizes with smaller restriction fragments within the open reading frame and 3'-untranslated region of the cDNA. This indicates that the entire open reading frame plus the 3'-untranslated region is contained in the large RNA species. RNase protection experiments revealed at least three points of divergence for the message species. One occurs within the COOH-terminal portion of the open reading frame at a position just 5' to the TGA stop codon. This divergence accounts for the two classes of acetylcholinesterase found in abundance in Torpedo. The site of splicing has been further defined by isolating a genomic clone containing the exon serving as the potential splice donor. We find a divergence between the cDNA and genomic DNA at the position estimated by the protection experiments. A less abundant divergence in mRNA can also be detected in the 3'-untranslated region. Another divergence occurs as a deleted sequence within the 5'-noncoding region and may be important for controlling translation efficiency. Since it is hypothesized that a single gene encodes acetylcholinesterase, the divergences in the very 3' region of the open reading frame and the 5'-noncoding region correspond to presumed splice junction boundaries where alternative RNA splicing occurs.
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PMID:Multiple messenger RNA species give rise to the structural diversity in acetylcholinesterase. 319 6

Serum levels of various hydrolytic enzymes in prostatic cancer patients with or without bone metastasis were compared with those in patients with prostatic hypertrophy and in the control subjects. The enzymes tested included 11 aminopeptidases, 2 endopeptidases, dipeptidyl carboxypeptidase, esterase, acetyl cholinesterase, and RNase. Although most of the enzymatic levels tended to be decreased in the cancer patients without bone metastasis, they tended to be increased in those with metastasis as well as in the patients with prostatic hypertrophy. Thus, bone metastasis is an important factor affecting the serum levels of hydrolytic enzymes in cancer patients. Of the enzymes tested, RNase was unique in that its serum levels were significantly increased regardless of the existence of bone metastasis. This enzyme may become a marker of malignancy.
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PMID:Different tendencies of changes in hydrolytic enzyme activities in sera from prostatic cancer patients with or without bone metastasis. 608 28

The 5'-untranslated region of the mouse acetylcholinesterase gene has been characterized structurally by RNase protection, primer extension, and sequencing. Evidence has been obtained for the use of two alternative promoters in brain. Tissue-specific splicing to alternative acceptor sites in the 5'-untranslated exons occurs in brain, muscle, and erythropoietic cells. cis elements 5' of the cap site that is predominantly used in these tissues and cells have been analyzed by deletion analysis of promoter-reporter gene constructs and by site-specific mutagenesis. The cap site is found 107 base pairs (bp) 5' of the translation start site. This region is devoid of CAAT or TATA sequences; further in the 5' direction 50 and 70 bp are tandem Egr-1 sites. The putative promoter has been coupled to the open reading frame of a luciferase reporter gene. Deletion analysis shows that this region largely accounts for tissue-specific transcription seen upon transfection of neuronal and muscle cells. Mutagenesis of the Egr-1 sites results in a marked loss of reporter gene activity, further substantiating the importance of this region in the control of transcription. cis elements in the promoter differ from those found for the genes encoding the various subunits of the nicotinic acetylcholine receptor, and distinct differences in control of transcription are evident when the respective reporter genes are transfected into C2 muscle cells.
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PMID:Promoter elements and transcriptional control of the mouse acetylcholinesterase gene. 842 32

L-type Ca2+ channels play critical roles in achieving stabilization of acetylcholinesterase (AChe) mRNA during myogenesis in C2-C12 skeletal muscle cells. To ascertain the importance of this signaling pathway in AChE expression during skeletal muscle development in the animal, we examined AChE mRNA levels in skeletal muscle and heart from control (+/+) and muscular dysgenic (mdg/mdg) mice that lack the skeletal, but not the cardiac, muscle L-type Ca2+ channels. RNase protection analysis showed 40-60% reductions in content of AChE mRNA in leg muscle, but not heart, from newborn and day 18 embryonic dysgenic mice. AChE activity was also reduced uniquely in skeletal muscle. In contrast to AChE transcripts, mRNA levels of the alpha-subunit of the nicotinic acetylcholine receptors (nAChRs) were increased in dysgenic skeletal muscle. Similar alterations in activity and mRNA levels of AChE were also observed form skeletal muscle cell lines derived from mdg mice. Because run-on transcription revealed no corresponding decrease in transcription rate, the decrease in mRNA content is likely a consequence of the inability of the dysgenic muscle cells to stabilize AChE mRNA during differentiation. These findings indicate that L-type Ca2+ channels play an important role in regulation of AChE expression during skeletal muscle development in vivo. The differential influence of muscle dysgenesis on mRNA levels of AChE and nAChRs provides additional evidence for distinct mechanisms of regulation of these two proteins.
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PMID:Acetylcholinesterase and nicotinic acetylcholine receptor expression diverge in muscular dysgenic mice lacking the L-type calcium channel. 866 81