酪氨酸羟化酶抗体

Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of the neurotransmitter dopamine and other catecholamines. TH functions as a tetramer, with each subunit composed of a regulatory and catalytic domain, and exists in several different isoforms (1,2). This enzyme is required for embryonic development since TH knockout mice die before or at birth (3). Levels of transcription, translation and post-translational modification regulate TH activity. The amino-terminal regulatory domain contains three serine residues: Ser9, Ser31, and Ser40. Phosphorylation at Ser40 by PKA positively regulates the catalytic activity of TH (4-6). Phosphorylation at Ser31 by CDK5 also increases the catalytic activity of TH through stabilization of TH protein levels (7-9). 1.Kumer, S.C. and Vrana, K.E. (1996) J Neurochem 67, 443-62. 2.Bodeau-Péan, S. et al. (1999) J Biol Chem 274, 3469-75. 3.Kobayashi, K. et al. (1995) J Biol Chem 270, 27235-43. 4.Lew, J.Y. et al. (1999) Mol Pharmacol 55, 202-9. 5.Vié, A. et al. (1999) J Biol Chem 274, 16788-95. 6.Lindgren, N. et al. (2000) J Neurochem 74, 2470-7. 7.Moy, L.Y. and Tsai, L.H. (2004) J Biol Chem 279, 54487-93. 8.Lehmann, I.T. et al. (2006) J Biol Chem 281, 17644-51. 9.Saraf, A. et al. (2007) J Biol Chem 282, 573-80.