Phosphorylation of tyrosine hydroxylase in isolated mice adrenal glands.
The site-specific phosphorylation of tyrosine hydroxylase (TH) was studied in mouse adrenal tissue. On addition of arsenite, a rapid increase in Ser19 phosphorylation occurred, concomitant with phosphorylation of p38 protein kinase. This is consistent with studies in other mammals, indicating a role of stress-activated protein kinases in TH regulation.
Toska
Karen
K
Department of Biochemistry and Molecular Biology, University of Bergen, Norway. karen.toska@ibmb.uib.no
Kleppe
Rune
R
Cohen
Philip
P
Haavik
Jan
J
D000311:Adrenal Glands / Q000201:enzymology*; D000818:Animals; D018053:Arsenites / Q000494:pharmacology; D002352:Carrier Proteins / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005260:Female; D015971:Gene Expression Regulation, Enzymologic; D007093:Imidazoles / Q000494:pharmacology; D051379:Mice; D008810:Mice, Inbred C57BL; D010766:Phosphorylation; D011485:Protein Binding; D011725:Pyridines / Q000494:pharmacology; D012694:Serine / Q000378:metabolism; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism*; D048051:p38 Mitogen-Activated Protein Kinases
D018053:Arsenites; D002352:Carrier Proteins; D004791:Enzyme Inhibitors; D007093:Imidazoles; D011725:Pyridines; D012694:Serine; D014446:Tyrosine 3-Monooxygenase; D048051:p38 Mitogen-Activated Protein Kinases; C015001:arsenite; C093642:SB 203580