Adrenergic innervation of the substantia innominata: co-localization of phenylethanolamine N-methyltransferase and tyrosine hydroxylase immunoreactivities within the same axons.
Adrenergic input to the rat substantia innominata (SI) was studied by immunocytochemical localization of phenylethanolamine N-methyltransferase (PNMT), the synthetic enzyme for adrenaline. Using primary antibodies derived from different species, we demonstrated in double-immunofluorescence labeling experiments that all PNMT-immunoreactive fibers in SI are also immunoreactive for tyrosine hydroxylase, the synthetic enzyme for dopamine. This result indicates that the PNMT immunoreactive axons in SI are indeed adrenergic fibers.
Chang
H T
HT
Department of Anatomy and Neurobiology, University of Tennessee, Memphis 38163.
Kuo
H
H
D000320:Adrenergic Fibers / Q000378:metabolism*; D000818:Animals; D001369:Axons / Q000201:enzymology; D001479:Basal Ganglia / Q000378:metabolism*; D007150:Immunohistochemistry; D008297:Male; D010625:Phenylethanolamine N-Methyltransferase / Q000378:metabolism*; D051381:Rats; D013377:Substantia Innominata / Q000166:cytology / Q000378:metabolism*; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism*
D014446:Tyrosine 3-Monooxygenase; D010625:Phenylethanolamine N-Methyltransferase