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Cholinergic, opioid and glycine receptor binding sites localized in human spinal cord by in vitro autoradiography Changes in amyotrophic lateral sclerosis
Author(s) -
Gillberg PerGöran,
Aquilonius StenMagnus
Publication year - 1985
Publication title -
acta neurologica scandinavica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.967
H-Index - 95
eISSN - 1600-0404
pISSN - 0001-6314
DOI - 10.1111/j.1600-0404.1985.tb00874.x
Subject(s) - spinal cord , grey matter , amyotrophic lateral sclerosis , glycine receptor , muscarinic acetylcholine receptor , chemistry , substantia nigra , strychnine , motor neuron , receptor , endocrinology , neuroscience , medicine , glycine , anatomy , biology , biochemistry , white matter , parkinson's disease , disease , amino acid , magnetic resonance imaging , radiology
– Binding sites for the receptor ligands 3 H‐quinuclidinylbenzilate, 3 H‐alpha‐bungarotoxin ( 3 H‐alpha‐Btx), 3 H‐etorphine and 3 H‐strychnine were localized autoradiographically at cervical, thoracic and lumbar levels of spinal cords from postmortem human control subjects and subjects with amyotrophic lateral sclerosis (ALS). The highest densities of muscarinic binding sites were found in the motor neuron areas and in the substantia gelatinosa, while the grey matter binding was very low within Clarke's column. Both 3 H‐alpha‐Btx and opioid receptor binding sites were numerous within the substantia gelatinosa, while glycine receptor binding sites were more uniformly distributed within the spinal grey matter. In ALS cases, muscarinic receptor binding sites were markedly reduced in motor neuron areas and slightly reduced in the dorsal horn, while the other binding sites studied were relatively unchanged.