Synthesizing enzymes for four neuroactive substances in motor neurons and neuromuscular junctions: Light and electron microscopic immunocytochemistry

V. Chan-Palay, Andrew G Engel, S. L. Palay, J. Y. Wu

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Abstract

Immunocytochemical evidence is presented for the existence of choline acetyltransferase (ChoAcTase), cysteine sulfinic acid decarboxylase (CSADCase), tyrosine hydroxylase (TyrOHase), and glutamic acid decarboxylase (GluDCase) in large motor neurons of the hypoglossal nucleus and the spinal cord and in nerve terminals of motor end plates in tongue and skeletal muscle of five mammalian species, including man. These enzymes, which are responsible for the synthesis of acetylcholine (AcCho), taurine, dopamine, and γ-aminobutyrate (GABA), respectively, were detected by immunocytochemical studies with monoclonal or polyclonal antibodies raised against the enzymes. Electron microscopy of the neuromuscular junctions showed that the immunoreactivity in each case was confined to the cytoplasmic matrix of presynaptic nerve terminals. Immunoreactivity obtained for each enzyme antibody varied with the species. It was highest in fresh, unfixed muscle and lowest in aldehyde-fixed specimens. Negative controls were obtained with preimmune sera and antisera preabsorbed with pure ChoAcTase, CSADCase, or GluDCase antigen. Double-labeling studies with ChoAcTase antibodies and acetylcholinesterase (AcChoEase) antibodies, AcChoEase enzyme activity, or α-bungarotoxin binding indicated that ChoAcTase, AcChoEase, and AcCho receptors were colocalized at the same end plates.

Original languageEnglish (US)
Pages (from-to)6717-6721
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume79
Issue number21 I
StatePublished - 1982
Externally publishedYes

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Choline O-Acetyltransferase
Neuromuscular Junction
Motor Neurons
sulfoalanine decarboxylase
Immunohistochemistry
Electrons
Light
Glutamate Decarboxylase
Antibodies
Enzymes
Motor Endplate
Aminobutyrates
Bungarotoxins
Taurine
Presynaptic Terminals
Tyrosine 3-Monooxygenase
Cholinergic Receptors
Acetylcholinesterase
Tongue
Aldehydes

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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title = "Synthesizing enzymes for four neuroactive substances in motor neurons and neuromuscular junctions: Light and electron microscopic immunocytochemistry",
abstract = "Immunocytochemical evidence is presented for the existence of choline acetyltransferase (ChoAcTase), cysteine sulfinic acid decarboxylase (CSADCase), tyrosine hydroxylase (TyrOHase), and glutamic acid decarboxylase (GluDCase) in large motor neurons of the hypoglossal nucleus and the spinal cord and in nerve terminals of motor end plates in tongue and skeletal muscle of five mammalian species, including man. These enzymes, which are responsible for the synthesis of acetylcholine (AcCho), taurine, dopamine, and γ-aminobutyrate (GABA), respectively, were detected by immunocytochemical studies with monoclonal or polyclonal antibodies raised against the enzymes. Electron microscopy of the neuromuscular junctions showed that the immunoreactivity in each case was confined to the cytoplasmic matrix of presynaptic nerve terminals. Immunoreactivity obtained for each enzyme antibody varied with the species. It was highest in fresh, unfixed muscle and lowest in aldehyde-fixed specimens. Negative controls were obtained with preimmune sera and antisera preabsorbed with pure ChoAcTase, CSADCase, or GluDCase antigen. Double-labeling studies with ChoAcTase antibodies and acetylcholinesterase (AcChoEase) antibodies, AcChoEase enzyme activity, or α-bungarotoxin binding indicated that ChoAcTase, AcChoEase, and AcCho receptors were colocalized at the same end plates.",
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T1 - Synthesizing enzymes for four neuroactive substances in motor neurons and neuromuscular junctions

T2 - Light and electron microscopic immunocytochemistry

AU - Chan-Palay, V.

AU - Engel, Andrew G

AU - Palay, S. L.

AU - Wu, J. Y.

PY - 1982

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N2 - Immunocytochemical evidence is presented for the existence of choline acetyltransferase (ChoAcTase), cysteine sulfinic acid decarboxylase (CSADCase), tyrosine hydroxylase (TyrOHase), and glutamic acid decarboxylase (GluDCase) in large motor neurons of the hypoglossal nucleus and the spinal cord and in nerve terminals of motor end plates in tongue and skeletal muscle of five mammalian species, including man. These enzymes, which are responsible for the synthesis of acetylcholine (AcCho), taurine, dopamine, and γ-aminobutyrate (GABA), respectively, were detected by immunocytochemical studies with monoclonal or polyclonal antibodies raised against the enzymes. Electron microscopy of the neuromuscular junctions showed that the immunoreactivity in each case was confined to the cytoplasmic matrix of presynaptic nerve terminals. Immunoreactivity obtained for each enzyme antibody varied with the species. It was highest in fresh, unfixed muscle and lowest in aldehyde-fixed specimens. Negative controls were obtained with preimmune sera and antisera preabsorbed with pure ChoAcTase, CSADCase, or GluDCase antigen. Double-labeling studies with ChoAcTase antibodies and acetylcholinesterase (AcChoEase) antibodies, AcChoEase enzyme activity, or α-bungarotoxin binding indicated that ChoAcTase, AcChoEase, and AcCho receptors were colocalized at the same end plates.

AB - Immunocytochemical evidence is presented for the existence of choline acetyltransferase (ChoAcTase), cysteine sulfinic acid decarboxylase (CSADCase), tyrosine hydroxylase (TyrOHase), and glutamic acid decarboxylase (GluDCase) in large motor neurons of the hypoglossal nucleus and the spinal cord and in nerve terminals of motor end plates in tongue and skeletal muscle of five mammalian species, including man. These enzymes, which are responsible for the synthesis of acetylcholine (AcCho), taurine, dopamine, and γ-aminobutyrate (GABA), respectively, were detected by immunocytochemical studies with monoclonal or polyclonal antibodies raised against the enzymes. Electron microscopy of the neuromuscular junctions showed that the immunoreactivity in each case was confined to the cytoplasmic matrix of presynaptic nerve terminals. Immunoreactivity obtained for each enzyme antibody varied with the species. It was highest in fresh, unfixed muscle and lowest in aldehyde-fixed specimens. Negative controls were obtained with preimmune sera and antisera preabsorbed with pure ChoAcTase, CSADCase, or GluDCase antigen. Double-labeling studies with ChoAcTase antibodies and acetylcholinesterase (AcChoEase) antibodies, AcChoEase enzyme activity, or α-bungarotoxin binding indicated that ChoAcTase, AcChoEase, and AcCho receptors were colocalized at the same end plates.

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