NADPH-diaphorase activity and its colocalization with transmitters and neuropeptides in the postganglionic neurons of the rat superior cervical ganglion.
NADPH-diaphorase activity (NADPH-DA), a marker of neural nitric oxide synthase, was found in many postganglionic nerve cell bodies in the adult rat superior cervical ganglion (SCG) after colchicine treatment, postganglionic nerve trunk ligation or ganglion culture. NADPH-DA colocalized with immunoreactivity to tyrosine hydroxylase (TH), serotonin, vasoactive intestinal peptide (VIP), neuropeptide Y (NPY), methionine-enkephalin and somatostatin. Almost all cells showing NADPH-DA were TH-immunoreactive, although several TH-immunoreactive cells lacked NADPH-DA. While suggesting that nitric oxide has an important role in the neuronal modulation in the synaptic transmission in the rat SCG, our results point out that nitric oxide synthesis is confined to a subpopulation of ganglion neurons. Our findings confirm the idea that the superior cervical ganglion consists of several subpopulations in which noradrenaline is colocalized with other transmitter or neuropeptide. Only about one-fourth of serotonin-immunoreactive neurons contained NADPH-DA. Similarly, the neuropeptides studied showed only partial colocalization with NADPH-DA. Our results thus suggest that nitric oxide is not associated with any particular transmitter or peptide.
Department of Anatomy, University of Helsinki, Finland.
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Vanhatalo
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Soinila
D000818:Animals; D007150:Immunohistochemistry; D009252:NADPH Dehydrogenase / Q000378:metabolism*; D009479:Neuropeptides / Q000378:metabolism*; D018377:Neurotransmitter Agents / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D017783:Superior Cervical Ganglion / Q000166:cytology* / Q000201:enzymology* / Q000378:metabolism; D017779:Sympathetic Fibers, Postganglionic / Q000201:enzymology* / Q000378:metabolism; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism
D009479:Neuropeptides; D018377:Neurotransmitter Agents; D014446:Tyrosine 3-Monooxygenase; D009252:NADPH Dehydrogenase