Immunohistochemical localization of catecholamine biosynthetic enzymes in the adrenal gland of the domestic fowl (Gallus domesticus).

The present study investigated the cellular localization of 3 catecholamine biosynthetic enzymes, tyrosine hydroxylase (TH), dopamine beta-hydroxylase (DBH), and phenylethanolamine N-methyltransferase (PNMT) to identify and analyze the localization of norepinephrine (NE) and epinephrine (E) cells in the adrenal gland in the chicken using peroxidase-antiperoxidase immunohistochemical techniques. Tyrosine hydroxylase immunoreactivity (IR) was observed in almost all adrenal medullary cells of the adult chicken. Dopamine beta-hydroxylase IR coincided with that of TH. Many medullary cells also exhibited PNMT IR, but PNMT-immunonegative cells were also observed. Tyrosine hydroxylase IR was localized in the E- and NE-containing cells, but PNMT IR was localized only in the E-containing cells. Approximately 69% of medullary cells were E-containing, and the remaining were NE-containing cells. The ratio of E- and NE-containing cells between the subcapsular and central zone was statistically significant (P < 0.01). Although cortical cells of the adrenal gland did not show TH-, DBH-, or PNMT-positive reactions, ganglia close to the adrenal gland showed TH, DBH, and PNMT immunoreactivities. These findings indicated the cellular localization of 3 catecholamine-biosynthesizing enzymes in chicken adrenal medulla and suggest that the majority of medullary cell are E-containing cells. The ratio of E cells to NE cells varies among the 3 zones in the adrenal glands of the chicken.