Catecholamines and catecholamine-synthesizing enzymes in guinea-pig sensory ganglia.
Cranial and spinal sensory ganglia of the guinea-pig were investigated by means of histochemistry and biochemistry for the presence of catecholamines and catecholamine-synthesizing enzymes. Sensory neurons exhibiting immunoreactivity to the rate-limiting enzyme of catecholamine synthesis, tyrosine hydroxylase (TH), were detected by immunohistochemistry in lumbo-sacral dorsal root ganglia, the nodose ganglion and the petrosal/jugular ganglion complex. The carotid body was identified as a target of TH-like-immunoreactive (TH-LI) neurons by the use of combined retrograde tracing and immunohistochemistry. Double-labelling immunofluorescence revealed that most TH-LI neurons also contained somatostatin-LI, but TH-LI did not coexist with either calcitonin gene-related peptide- or substance P-LI. TH-LI neurons did not react with antibodies to other enzymes involved in catecholamine synthesis, i.e., aromatic amino acid decarboxylase (AADC), dopamine-beta-hydroxylase (D beta H), and phenylethanolamine-N-methyl-transferase (PNMT). Petrosal neurons as well as their endings in the carotid body lacked dopamine- and L-DOPA-LI. Sensory neurons did not display glyoxylic acid-induced catecholamine fluorescence. Ganglia containing TH-LI neurons were kept in short-term organ culture after crushing their roots and the exiting nerve in order to enrich intra-axonal transmitter content at the ganglionic side of the crush. However, even under these conditions, catecholamine fluorescence was not detected in axons projecting peripherally or centrally from the ganglia. Sympathetic noradrenergic nerves entered the ganglia and terminated within them. Accordingly, biochemical analyses of guinea-pig sensory ganglia revealed noradrenaline but no dopamine. In conclusion, catecholamines within guinea-pig sensory ganglia are confined to sympathetic nerves, which fulfill presently unknown functions. The TH-LI neurons themselves, however, lack any additional sign of catecholamine synthesis, and the presence of enzymatically active TH within these neurons is questionable.
Kummer
W
W
Institute for Anatomy and Cell Biology, University of Heidelberg, FRG.
Gibbins
I L
IL
Stefan
P
P
Kapoor
V
V
D000818:Animals; D002344:Carotid Body / Q000737:chemistry; D002395:Catecholamines / Q000032:analysis* / Q000096:biosynthesis; D004298:Dopamine / Q000032:analysis; D005557:Formaldehyde; D005727:Ganglia, Spinal / Q000737:chemistry* / Q000166:cytology / Q000201:enzymology*; D005976:Glutaral; D006038:Glyoxylates; D006168:Guinea Pigs; D007150:Immunohistochemistry; D007980:Levodopa / Q000032:analysis; D009412:Nerve Fibers / Q000737:chemistry / Q000648:ultrastructure; D009479:Neuropeptides / Q000032:analysis; D009924:Organ Culture Techniques; D014446:Tyrosine 3-Monooxygenase / Q000032:analysis
D002395:Catecholamines; D006038:Glyoxylates; D009479:Neuropeptides; D005557:Formaldehyde; D007980:Levodopa; D014446:Tyrosine 3-Monooxygenase; C031150:glyoxylic acid; D005976:Glutaral; D004298:Dopamine