PNMT


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[9] Human genes: TH, tyrosine hydroxylase; DBH, dopamine beta-hydroxylase; PNMT, phenylethanolamine N-methyltransferase; SDH3, succinate dehydrogenase complex iron sulfur subunit B; SDHD, succinate dehydrogenase complex subunit D; VHL, von Hippel-Lindau tumor suppressor; RET, ret proto-oncogene.
Immunohistochemical studies of TH in the patient tumor contrasting with the expression of DBH and PNMT and genetic analysis of TH in blood and pheochromocytoma.
Phenylethanolamine N-methyl transferase (PNMT), an enzyme localized in adrenal chromaffin cells and pheochromocytes, leads to the methylation onto the amino group of norepinephrine to produce epinephrine.
Meanwhile, both epinephrine and metanephrine were within the normal range because of failure of formation of epinephrine and its metabolite, metanephrine due to the large size of the adrenal tumor and its impact on glucocoriticoid driven PNMT action on conversion of epinephrine to norepinephrine.
Immunohistochemistry for catecholamine-synthesizing enzymes was performed with anti-TH polyclonal antibodies (raised in rabbits with use of rat TH; Chemicon International) diluted 1:1000 in PBS containing 1 g/L BSA, anti-DBH polyclonal antibodies (raised in rabbits with use of bovine DBH; Eugene Tech International) diluted 1:100 in PBS containing 1 g/L BSA, and anti-PNMT polyclonal antibodies (raised in rabbits with use of bovine PNMT; Chemicon International) diluted 1:1000 in PBS containing 1 g/L BSA.
As controls we used four slides of healthy human adrenal medulla for each of the respective staining procedures for TH, DBH, and PNMT. Two of the four slides were used as positive controls and underwent the immunochemical staining protocol as described above.