scholarly journals Activation of tyrosine hydroxylase by micromolar concentrations of Ca in leaky adrenal medullary cells and PC12 cells

1986 ◽  
Vol 40 ◽  
pp. 212
Author(s):  
Nobuyuki Yanagihara ◽  
Yasuhito Uezono ◽  
Yoshiro Koda ◽  
Akihiko Wada ◽  
Futoshi Izumi
Keyword(s):  
Tyrosine Hydroxylase ◽  
Pc12 Cells ◽  
Adrenal Medullary Cells ◽  
Medullary Cells

Expression and regulation of M-type K+ channel in PC12 cells and rat adrenal medullary cells

2018 ◽  
Vol 372 (3) ◽  
pp. 457-468 ◽  
Author(s):  
Keita Harada ◽  
Hidetada Matsuoka ◽  
Masumi Inoue
Keyword(s):  
Pc12 Cells ◽  
K Channel ◽  
Type K ◽  
Adrenal Medullary Cells ◽  
Medullary Cells

Vitamin D increases expression of the tyrosine hydroxylase gene in adrenal medullary cells

1996 ◽  
Vol 36 (1) ◽  
pp. 193-196 ◽  
Author(s):  
Elzbieta Puchacz ◽  
Walter E. Stumpf ◽  
Ewa K. Stachowiak ◽  
Michal K. Stachowiak
Keyword(s):  
Vitamin D ◽  
Tyrosine Hydroxylase ◽  
Tyrosine Hydroxylase Gene ◽  
Hydroxylase Gene ◽  
Adrenal Medullary Cells ◽  
Medullary Cells

scholarly journals Stimulation of Catecholamine Synthesis by Environmental Estrogenic Pollutants

Endocrinology ◽  
2005 ◽  
Vol 146 (1) ◽  
pp. 265-272 ◽  
Author(s):  
Nobuyuki Yanagihara ◽  
Yumiko Toyohira ◽  
Susumu Ueno ◽  
Masato Tsutsui ◽  
Kensuke Utsunomiya ◽  
...  
Keyword(s):  
Tyrosine Hydroxylase ◽  
The United States ◽  
Term Treatment ◽  
Short Term ◽  
Short Term Treatment ◽  
Catecholamine Synthesis ◽  
Adrenal Medullary Cells ◽  
Regulatory Standard ◽  
Long Term Treatment ◽  
Medullary Cells

Environmental estrogenic pollutants are compounds that have been shown to have estrogenic effects on fetal development and reproductive systems. Less attention, however, has been paid to their influence on neuronal functions. We report here the effects of estrogenic pollutants on catecholamine synthesis in bovine adrenal medullary cells used as a model system of noradrenergic neurons. Treatment of cultured bovine adrenal medullary cells with p-nonylphenol and bisphenol A at 10 nm for 3 d stimulated [14C]catecholamine synthesis from [14C]tyrosine and tyrosine hydroxylase activity, an effect that was not inhibited by ICI 182,780, an antagonist of estrogen receptors. Significant effects of p-nonylphenol on [14C]catecholamine synthesis were observed at 0.1 nm, which is 45 times lower than that of the international regulatory standard (4.5 nm), and the maximum effects were around 10–100 nm. The concentrations (0.1–10 nm) used in the present study are similar to the range observed in rivers in the United States or Europe. On the other hand, short-term treatment of cells with 10 nmp-nonylphenol for 10 min also activated tyrosine hydroxylase, which was suppressed by U0126, an inhibitor of MAPK kinase. Furthermore, treatment of cells with p-nonylphenol for 5 min increased the phospho-p44/42MAPK in a concentration-dependent (1–1000 nm) manner, whereas p-nonylphenol (100 nm, 2 d) enhanced both levels of non-phospho- and phospho-p44/42MAPK. These findings suggest that short-term and long-term treatment of cells with estrogenic pollutants at environmental concentrations stimulates catecholamine synthesis and MAPK through an estrogen receptor-independent pathway.

Activation of tyrosine hydroxylase by micromolar concentrations of calcium in digitonin-permeabilized adrenal medullary cells

1987 ◽  
Vol 146 (2) ◽  
pp. 530-536 ◽  
Author(s):  
Nobuyuki Yanagihara ◽  
Yasuhito Uezono ◽  
Yoshiro Koda ◽  
Akihiko Wada ◽  
Futoshi Izumi
Keyword(s):  
Tyrosine Hydroxylase ◽  
Adrenal Medullary Cells ◽  
Medullary Cells
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