Journal article

Publication year: 2002

Pages: 275-280

Journal: Cell and Tissue Research

Volume number: 307

Issue number: 3

ISSN: 0302-766X

DOI Link: https://doi.org/10.1007/s00441-002-0520-4

Publisher: Springer

Abstract: 
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.

Harvard Citation style: Lips, K., Pfeil, U., Haberberger, R. and Kummer, W. (2002) Localisation of the high-affinity choline transporter-1 in the rat skeletal motor unit, Cell and Tissue Research, 307(3), pp. 275-280. https://doi.org/10.1007/s00441-002-0520-4

APA Citation style: Lips, K., Pfeil, U., Haberberger, R., & Kummer, W. (2002). Localisation of the high-affinity choline transporter-1 in the rat skeletal motor unit. Cell and Tissue Research. 307(3), 275-280. https://doi.org/10.1007/s00441-002-0520-4