Neuronal subpopulations in autonomic ganglia associated with the chicken ureter: an immunohistochemical study.
The neurochemical coding of neurones located in ganglia of the nerve trunk accompanying the chicken ureter was analysed and quantified using NADPH-diaphorase reactivity and immunohistochemistry against tyrosine hydroxylase (TH), nitric oxide synthase (NOS), calbindin (CAL), vasoactive intestinal polypeptide (VIP), neuropeptide Y (NPY), somatostatin (SOM), substance P (SP) and calcitonin gene-related peptide (CGRP) in untreated or colchicine-treated preparation. Almost all neurones were either positive for TH (38%) or for SOM (60%). Only 4% of the neurones were both TH- and SOM-positive and 3% of the neurones exhibited neither TH nor SOM immunoreactivity. The relative numbers of NPY-, NOS-, CAL- and VIP-positive neurones were 57%, 28%, 14% and 7%, respectively. No SP- or CGRP-positive neurones were observed. All NADPH-diaphorase-positive neurones expressed NOS immunoreactivity. Only in some TH-positive neurones was NPY and/or NOS found. Four major subpopulations were found in the ureteric ganglia. The SOM-positive neurones were subdivided into SOM/NPY/NOS- (28% of all neurones), SOM/NPY- (18%) and SOM/CAL/NPY-positive neurones (14%). A subpopulation of these peptid- ergic neurones also contained VIP. About 35% of the neurones contained TH only. Neurones of all subpopulations (72% of the neurones), except most of the CAL-positive neurones, were encircled by dense plexus of varicose SP/CGRP-positive, presumably sensory nerve fibres. Dense plexus of VIP-positive fibres were observed around 89% of the neurones. The chemical coding of the neuronal subpopulations identified in the ganglia accompanying the chicken ureter resembled that observed in the ganglia of Remak's nerve but was remarkably different from that of the autonomic neurones described in mammalian species.
Sann
H
H
Physiologisches Institut, Tierärztliche Hochschule, Bischofsholer Damm 15/102, D-30173 Hannover, Germany. hsann@physiology.tiho-hannover.de
D000818:Animals; D064026:Calbindins; D002645:Chickens; D005725:Ganglia, Autonomic / Q000737:chemistry / Q000166:cytology* / Q000201:enzymology; D007150:Immunohistochemistry; D009252:NADPH Dehydrogenase / Q000032:analysis; D009419:Nerve Tissue Proteins / Q000032:analysis; D009474:Neurons / Q000737:chemistry* / Q000201:enzymology; D009478:Neuropeptide Y / Q000032:analysis; D019001:Nitric Oxide Synthase / Q000032:analysis; D010320:Parvalbumins / Q000032:analysis; D064030:S100 Calcium Binding Protein G / Q000032:analysis; D013004:Somatostatin / Q000032:analysis; D013373:Substance P / Q000032:analysis; D014446:Tyrosine 3-Monooxygenase / Q000032:analysis; D014513:Ureter / Q000294:innervation*; D014660:Vasoactive Intestinal Peptide / Q000032:analysis
D064026:Calbindins; D009419:Nerve Tissue Proteins; D009478:Neuropeptide Y; D010320:Parvalbumins; D064030:S100 Calcium Binding Protein G; D013373:Substance P; D014660:Vasoactive Intestinal Peptide; D013004:Somatostatin; D019001:Nitric Oxide Synthase; D014446:Tyrosine 3-Monooxygenase; D009252:NADPH Dehydrogenase