The phosphorylation of Ser40 of tyrosine hydroxylase has no effect on the stability of the enzyme in PC12 cells

Akira Nakashima, Yoko S. Kaneko, Keiji Mori, Toshiharu Nagatsu, Akira Ota

研究成果: Article

1 引用 (Scopus)

抄録

It is well established that the phosphorylation of tyrosine hydroxylase (TH) at Ser40 is critical in regulating the catalytic activity of the enzyme. However, the influence of the phosphorylation of Ser40 on the stability of TH protein has not been investigated. This study was performed to estimate such a possibility. Although the treatment of rat pheochromocytoma cell line PC12 cells with forskolin increased the amount of TH phosphorylated at Ser40 in the cells, it did not affect the total amount of TH in the cells. Next, human TH type 1 (hTH1) of wild-type and a mutant missing the first 52 amino acid residues were expressed as histidine-tagged forms in PC-12 cells, and then the cells were treated with forskolin. However, the phosphorylation of hTH1 at Ser40 did not affect the amount of the wild-type hTH1 protein present in PC12 cells. Finally, wild-type and a mutant in which Ser40 was replaced by Asp (S40D, a mimic of TH phosphorylated at Ser40) were expressed in PC-12 cells as histidine-tagged forms or untagged forms. Neither histidine-tagged nor untagged forms showed any difference in their amounts of wild-type hTH1 and S40D hTH1 present in the cells. Collectively, these results indicate the fact that the phosphorylation of Ser40 does not affect the stability of TH protein in PC12 cells.

元の言語English
ページ(範囲)279-288
ページ数10
ジャーナルBiogenic Amines
19
発行部数4-6
DOI
出版物ステータスPublished - 01-12-2005

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Enzyme Stability
PC12 Cells
Tyrosine 3-Monooxygenase
Phosphorylation
Histidine
Colforsin
Proteins
Viperidae
Amino Acids
Enzymes

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Pharmacology

これを引用

Nakashima, Akira ; Kaneko, Yoko S. ; Mori, Keiji ; Nagatsu, Toshiharu ; Ota, Akira. / The phosphorylation of Ser40 of tyrosine hydroxylase has no effect on the stability of the enzyme in PC12 cells. :: Biogenic Amines. 2005 ; 巻 19, 番号 4-6. pp. 279-288.
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abstract = "It is well established that the phosphorylation of tyrosine hydroxylase (TH) at Ser40 is critical in regulating the catalytic activity of the enzyme. However, the influence of the phosphorylation of Ser40 on the stability of TH protein has not been investigated. This study was performed to estimate such a possibility. Although the treatment of rat pheochromocytoma cell line PC12 cells with forskolin increased the amount of TH phosphorylated at Ser40 in the cells, it did not affect the total amount of TH in the cells. Next, human TH type 1 (hTH1) of wild-type and a mutant missing the first 52 amino acid residues were expressed as histidine-tagged forms in PC-12 cells, and then the cells were treated with forskolin. However, the phosphorylation of hTH1 at Ser40 did not affect the amount of the wild-type hTH1 protein present in PC12 cells. Finally, wild-type and a mutant in which Ser40 was replaced by Asp (S40D, a mimic of TH phosphorylated at Ser40) were expressed in PC-12 cells as histidine-tagged forms or untagged forms. Neither histidine-tagged nor untagged forms showed any difference in their amounts of wild-type hTH1 and S40D hTH1 present in the cells. Collectively, these results indicate the fact that the phosphorylation of Ser40 does not affect the stability of TH protein in PC12 cells.",
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The phosphorylation of Ser40 of tyrosine hydroxylase has no effect on the stability of the enzyme in PC12 cells. / Nakashima, Akira; Kaneko, Yoko S.; Mori, Keiji; Nagatsu, Toshiharu; Ota, Akira.

:: Biogenic Amines, 巻 19, 番号 4-6, 01.12.2005, p. 279-288.

研究成果: Article

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