Ganglion cells and topographically related nerves in the vallate papilla/von Ebner gland complex.
Ganglion cells and topographically related nerves in the vallate papilla/von Ebner gland complex were investigated in rat tongue by cytochemical, immunocytochemical, and ultrastructural methods to evaluate the possible presence of different neuronal subpopulations. Immunostaining for neurofilaments and protein gene product 9.5 revealed ganglionic cell bodies and nerve fibers. A large part of the neurons were positive at immunostaining for neuronal nitric oxide synthase (NOS), vesicular acetylcholine transporter (VAChT), or vasoactive intestinal peptide (VIP). A small subset of nerve fibers revealed immunoreactivity for cholecystokinin. Axons traveling under the lingual epithelium were evidenced by their content of calcitonin gene-related peptide (CGRP) or substance P (SP). Cell bodies positive for SP or CGRP were not detected. Using methods of co-localization, three different neuronal classes were detected. The main population was composed of AChE/NADPH-diaphorase (NADPHd)-positive cells. Small groups of acetylcholine esterase (AChE)-positive/NADPHd-negative cells were visible. Isolated neurons were AChE-negative/NADPHd-positive. The results of co-localization experiments for VAChT/NOS were consistent with those obtained by cytochemical co-localization of AChE and NADPHd. Experiments of co-localization for peptidergic and nitrergic structures revealed CGRP- and SP-immunoreactive fibers in the vallate papilla/von Ebner gland ganglion. In conclusion, the results demonstrated in the VP/VEG complex peptidergic, cholinergic, and nitrergic neurons. The presence of different neuronal subclasses suggests that a certain degree of functional specialization may exist.
Sbarbati
Andrea
A
Department of Morphological and Biomedical Sciences, Section of Anatomy and Histology, University of Verona, Italy. SBARBATI@borgoroma.univr.it
Merigo
Flavia
F
Bernardi
Paolo
P
Crescimanno
Caterina
C
Benati
Donatella
D
Osculati
Francesco
F
D000110:Acetylcholinesterase / Q000378:metabolism; D000818:Animals; D015740:Calcitonin Gene-Related Peptide / Q000378:metabolism; D002352:Carrier Proteins / Q000378:metabolism; D005088:Exocrine Glands / Q000378:metabolism*; D005724:Ganglia / Q000378:metabolism* / Q000648:ultrastructure; D007150:Immunohistochemistry; D026901:Membrane Transport Proteins; D009252:NADPH Dehydrogenase / Q000378:metabolism; D009474:Neurons / Q000378:metabolism / Q000648:ultrastructure; D019001:Nitric Oxide Synthase / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D013373:Substance P / Q000378:metabolism; D014059:Tongue / Q000294:innervation* / Q000378:metabolism* / Q000648:ultrastructure; D050494:Vesicular Acetylcholine Transport Proteins; D033921:Vesicular Transport Proteins
D002352:Carrier Proteins; D026901:Membrane Transport Proteins; C493461:Slc18a3 protein, rat; D050494:Vesicular Acetylcholine Transport Proteins; D033921:Vesicular Transport Proteins; D013373:Substance P; D019001:Nitric Oxide Synthase; D009252:NADPH Dehydrogenase; D000110:Acetylcholinesterase; D015740:Calcitonin Gene-Related Peptide