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Complete sequence of a cDNA encoding an active rat choline acetyltransferase: A tool to investigate the plasticity of cholinergic phenotype expression

Complete sequence of a cDNA encoding an active rat choline acetyltransferase: A tool to... A cDNA clone encoding the complete sequence of an active, rat choline acetyltransferase (ChoAcTase; acetyl‐CoA:choline O‐acetyltransferase, EC 2.3.1.6) has been isolated. Analysis of the deduced amino acid sequence reveals 85% and 31% identity with the porcine and Drosophila melanogaster enzymes, respectively. To further elucidate the molecular basis of neurotransmitter‐related phenotypic plasticity, the expression of ChoAcTase mRNA was compared with that of tyrosine hydroxylase (TH; tyrosine 3‐monooxygenase, L‐tyrosine, tetrahydropteridine: oxygen oxidoreductase (3‐hydroxylating), EC 1.14.16.2), in neurons from superior cervical ganglia grown in the following conditions: (1) normal medium, (2) high K+ medium, and (3) normal medium supplemented with 50% muscle‐conditioned medium (CM). TH mRNA was expressed in all three media; its level rose in high K+ and decreased strikingly in the presence of CM. ChoAcTase mRNA could be visualized in CM, but fell to undetectable levels in normal and high K+ media. These results suggest that translational or post‐translational mechanisms do not play a major role for the modulation of neurotransmitter‐associated phenotype. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Neuroscience Research Wiley

Complete sequence of a cDNA encoding an active rat choline acetyltransferase: A tool to investigate the plasticity of cholinergic phenotype expression

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References (34)

Publisher
Wiley
Copyright
Copyright © 1989 Alan R. Liss, Inc.
ISSN
0360-4012
eISSN
1097-4547
DOI
10.1002/jnr.490230304
pmid
2570161
Publisher site
See Article on Publisher Site

Abstract

A cDNA clone encoding the complete sequence of an active, rat choline acetyltransferase (ChoAcTase; acetyl‐CoA:choline O‐acetyltransferase, EC 2.3.1.6) has been isolated. Analysis of the deduced amino acid sequence reveals 85% and 31% identity with the porcine and Drosophila melanogaster enzymes, respectively. To further elucidate the molecular basis of neurotransmitter‐related phenotypic plasticity, the expression of ChoAcTase mRNA was compared with that of tyrosine hydroxylase (TH; tyrosine 3‐monooxygenase, L‐tyrosine, tetrahydropteridine: oxygen oxidoreductase (3‐hydroxylating), EC 1.14.16.2), in neurons from superior cervical ganglia grown in the following conditions: (1) normal medium, (2) high K+ medium, and (3) normal medium supplemented with 50% muscle‐conditioned medium (CM). TH mRNA was expressed in all three media; its level rose in high K+ and decreased strikingly in the presence of CM. ChoAcTase mRNA could be visualized in CM, but fell to undetectable levels in normal and high K+ media. These results suggest that translational or post‐translational mechanisms do not play a major role for the modulation of neurotransmitter‐associated phenotype.

Journal

Journal of Neuroscience ResearchWiley

Published: Jul 1, 1989

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