title: Immunohistochemical evidence for species-specific coexistence of catecholamines, serotonin, acetylcholine and nitric oxide in glomus cells of rat and guinea pig aortic bodies.
abstract: The aortic bodies are small paraganglia distributed along the vagus nerve and its branches in the vicinity of the aortic arch which, like the carotid bodies, act as arterial chemoreceptors. In the rat carotid body, corelease of ATP and acetylcholine (ACh) from glomus cells is considered to be the main mechanism mediating fast hypoxic chemotransmission while dopamine, serotonin, and nitric oxide (NO) exert modulating effects. The present study was aimed at determination of the endogenous sources of serotonin, ACh and NO within rat and guinea pig aortic bodies by immunohistochemical double- and triple-labeling approaches, utilizing antibodies to serotonin, the NO and ACh synthesizing enzymes neuronal NO synthase (nNOS) and choline acetyltransferase (ChAT), respectively, as well as to the vesicular acetylcholine transporter (VAChT). Additional marker antibodies were directed against the rate-limiting enzyme of catecholamine synthesis, i.e. tyrosine hydroxylase (TH), and the vesicular protein, synaptophysin (SYN). In both species, all aortic body glomus cells were immunoreactive to serotonin and cholinergic markers. In the rat, all glomus cells were additionally catecholaminergic, as indicated by TH-immunoreactivity, whereas this applied only to a subgroup of guinea pig glomus cells. On the other hand, all guinea pig glomus cells were nNOS-immunoreactive, whereas only nerve fibers but not glomus cells exhibited nNOS-immunoreactivity in the rat. These data support the concept that the chemoexcitatory transmitters ACh and serotonin are involved in hypoxic excitation of aortic chemoreceptor terminals in both species. The production of the inhibitory modulators, dopamine and NO, however, appears to be species-specifically regulated.
authors.affiliation: Department of Physiology, Medical Faculty in Plzen, Charles University, Lidická 1, 305 66 Pizen, Czech Republic. magdalena.dvorakova@lfp.cuni.cz
authors.forename: Magdalena Chottova
authors.initials: MC
authors.lastname: Dvorakova
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Kummer
mesh_terms: D000109:Acetylcholine / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001016:Aortic Bodies / Q000166:cytology* / Q000378:metabolism; D002344:Carotid Body / Q000378:metabolism; D002395:Catecholamines / Q000378:metabolism*; D002795:Choline O-Acetyltransferase / Q000378:metabolism; D006168:Guinea Pigs; D007150:Immunohistochemistry; D026901:Membrane Transport Proteins / Q000378:metabolism; D019001:Nitric Oxide Synthase / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D012701:Serotonin / Q000378:metabolism*; D016708:Synaptophysin / Q000378:metabolism; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism; D050494:Vesicular Acetylcholine Transport Proteins
chemical_list: D002395:Catecholamines; D026901:Membrane Transport Proteins; C493461:Slc18a3 protein, rat; D016708:Synaptophysin; D050494:Vesicular Acetylcholine Transport Proteins; D012701:Serotonin; D000255:Adenosine Triphosphate; D019001:Nitric Oxide Synthase; D014446:Tyrosine 3-Monooxygenase; D002795:Choline O-Acetyltransferase; D000109:Acetylcholine