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Localisation of the high-affinity choline transporter-1 in the rat skeletal motor unit.

Authors: Lips, KS  Pfeil, U  Haberberger, RV  Kummer, W 
Citation: Lips KS, etal., Cell Tissue Res 2002 Mar;307(3):275-80. Epub 2002 Feb 14.
Pubmed: (View Article at PubMed) PMID:11904763
DOI: Full-text: DOI:10.1007/s00441-002-0520-4

The rate-limiting step in neuronal acetylcholine (ACh) synthesis is the uptake of choline via a high-affinity transporter. We have generated antisera against the recently identified transporter CHT1 to investigate its distribution in rat motor neurons and skeletal muscle and have used these antisera in combination with (1) antisera against the vesicular acetylcholine transporter (VAChT) to identify cholinergic synapses and (2) Alexa-488-labelled alpha-bungarotoxin to identify motor endplates. In the motor unit, immunohistochemistry and RT-PCR have demonstrated that CHT1 is restricted to motoneurons and absent from the non-neuronal ACh-synthesizing elements, e.g. skeletal muscle fibres. In addition, CHT1 is also present in parasympathetic neurons of the tongue, as evidenced by immunohistochemistry and RT-PCR. CHT1 immunoreativity is principally found at all segments (perikaryon, dendrites, axon) of the motoneuron but is enriched at neuro-neuronal and neuro-muscular synapses. This preferential localisation matches well with its anticipated pivotal role in synaptic transmitter recycling and synthesis.


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RGD Object Information
RGD ID: 1299242
Created: 2004-06-01
Species: All species
Last Modified: 2006-04-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.