title: Amino acid immunoreactivity in corticospinal terminals.
abstract: Anterogradely labeled corticospinal axons and their terminals were identified after injections of wheat germ-agglutinin conjugated to horseradish peroxidase in the sensorimotor cortex of rats. Thin myelinated axons were labeled in the corticospinal tract. Terminal labeling was densest in the internal basilar nucleus and laminae III-IV of the dorsal horn throughout the spinal cord; electron microscopical observations were mainly from the cervical enlargement. Labeled terminals were most often small and dome-shaped with densely packed, clear round vesicles and sparse mitochondria. These terminals established asymmetric synapses with small dendrites or spines and were never involved in axoaxonic contacts. Postembedding immunocytochemistry was used to study the subcellular distribution of glutamate, aspartate, and gamma-aminobutyric acid (GABA). Corticospinal terminals appeared enriched in glutamate, but not GABA. Some corticospinal terminals appeared enriched in aspartate, though the labeling was less selective than in the case of glutamate. GABA immunolabeling was very dense in about 20% of terminals. These were most often small, rich in mitochondria, and made symmetric synapses; they were not anterogradely labeled from the cortex. Quantitative analysis on double immunolabeled material allowed a direct comparison of particle density for different antigens in the same section. Terminals with a high density of particles coding for glutamate were not enriched with GABA, and terminals immunolabeled for GABA were not enriched with glutamate. There was no significant correlation between glutamate and aspartate immunolabeling in corticospinal terminals; a subpopulation of these terminals may be enriched in aspartate. Aspartate immunolabeling was consistently higher in dendrites postsynaptic (in the plane of section) to corticospinal terminals than in other dendrites.(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: Department of Cell Biology and Anatomy, University of North Carolina, Chapel Hill 27599.
authors.forename: J G
authors.initials: JG
authors.lastname: Valtschanoff
authors.forename: R J
authors.initials: RJ
authors.lastname: Weinberg
authors.forename: A
authors.initials: A
authors.lastname: Rustioni
mesh_terms: D000596:Amino Acids / Q000276:immunology / Q000378:metabolism*; D000818:Animals; D001224:Aspartic Acid / Q000276:immunology / Q000378:metabolism; D001369:Axons / Q000648:ultrastructure; D002540:Cerebral Cortex / Q000276:immunology / Q000378:metabolism* / Q000648:ultrastructure; D005971:Glutamates / Q000276:immunology / Q000378:metabolism; D018698:Glutamic Acid; D006735:Horseradish Peroxidase; D007150:Immunohistochemistry; D008297:Male; D008854:Microscopy, Electron; D008928:Mitochondria / Q000648:ultrastructure; D009411:Nerve Endings / Q000276:immunology / Q000378:metabolism* / Q000648:ultrastructure; D051381:Rats; D017207:Rats, Sprague-Dawley; D013116:Spinal Cord / Q000276:immunology / Q000378:metabolism* / Q000648:ultrastructure; D016610:Tissue Embedding; D018998:Wheat Germ Agglutinin-Horseradish Peroxidase Conjugate; D014909:Wheat Germ Agglutinins; D005680:gamma-Aminobutyric Acid / Q000378:metabolism
chemical_list: D000596:Amino Acids; D005971:Glutamates; D018998:Wheat Germ Agglutinin-Horseradish Peroxidase Conjugate; D014909:Wheat Germ Agglutinins; D001224:Aspartic Acid; D018698:Glutamic Acid; D005680:gamma-Aminobutyric Acid; D006735:Horseradish Peroxidase