title: Ultrastructural study of CCK and tyrosine hydroxylase immunoreactivity in the rat nucleus accumbens.
abstract: The cholecystokinin (CCK)- and tyrosine hydroxylase (TH)-like immunoreactive (LI) axons and boutons were studied in the caudal and medial parts of the rat nucleus accumbens (NAC), using the indirect immunoperoxidase technique, at the electron microscopic level. Both CCK- and TH-LI boutons contained clear synaptic vesicles and large granular vesicles of similar size, but the CCK-LI boutons contained more large granular vesicles than TH-LI boutons. The CCK-LI and TH-LI boutons were heterogeneous. This finding might be related to the various immunoreactive neuronal types innervating the caudomedial NAC. However, the CCK-LI boutons (containing mostly small, round, clear synaptic vesicles) formed mainly asymmetrical synaptic contacts with dendritic spines whereas the TH-LI boutons (containing medium-sized as well as small, round, clear synaptic vesicles) formed mostly symmetrical synaptic contacts with dendritic shafts.
authors.affiliation: Laboratoire de Cytologie, Université Pierre et Marie Curie, France.
authors.forename: H
authors.initials: H
authors.lastname: Baali-Cherif
authors.forename: B P
authors.initials: BP
authors.lastname: Roques
authors.forename: G
authors.initials: G
authors.lastname: Tramu
authors.forename: J
authors.initials: J
authors.lastname: Thibault
mesh_terms: D000818:Animals; D001369:Axons / Q000737:chemistry / Q000201:enzymology / Q000276:immunology / Q000648:ultrastructure; D002766:Cholecystokinin / Q000276:immunology / Q000302:isolation & purification*; D005260:Female; D007124:Immunoenzyme Techniques; D008297:Male; D009714:Nucleus Accumbens / Q000737:chemistry* / Q000201:enzymology / Q000276:immunology; D051381:Rats; D013569:Synapses / Q000737:chemistry / Q000201:enzymology / Q000276:immunology / Q000648:ultrastructure; D014446:Tyrosine 3-Monooxygenase / Q000276:immunology / Q000302:isolation & purification*
chemical_list: D002766:Cholecystokinin; D014446:Tyrosine 3-Monooxygenase