Phosphorylation of tyrosine hydroxylase in isolated mice adrenal glands

Karen Toska; Rune Kleppe; Philip Cohen; J. A.N. Haavik

doi:10.1111/j.1749-6632.2002.tb04435.x

Phosphorylation of tyrosine hydroxylase in isolated mice adrenal glands

Karen Toska (Lead / Corresponding author), Rune Kleppe, Philip Cohen, J. A.N. Haavik

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13 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	66-68
Number of pages	3
Journal	Annals of the New York Academy of Sciences
Volume	971
DOIs	https://doi.org/10.1111/j.1749-6632.2002.tb04435.x
Publication status	Published - Oct 2002

Keywords

Mice adrenal glands
Tyrosine hydroxylase

ASJC Scopus subject areas

General Biochemistry,Genetics and Molecular Biology
History and Philosophy of Science

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title = "Phosphorylation of tyrosine hydroxylase in isolated mice adrenal glands",

abstract = "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.",

keywords = "Mice adrenal glands, Tyrosine hydroxylase",

author = "Karen Toska and Rune Kleppe and Philip Cohen and Haavik, \{J. A.N.\}",

year = "2002",

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journal = "Annals of the New York Academy of Sciences",

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T1 - Phosphorylation of tyrosine hydroxylase in isolated mice adrenal glands

AU - Toska, Karen

AU - Kleppe, Rune

AU - Cohen, Philip

AU - Haavik, J. A.N.

PY - 2002/10

Y1 - 2002/10

N2 - 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.

AB - 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.

KW - Mice adrenal glands

KW - Tyrosine hydroxylase

UR - https://www.scopus.com/pages/publications/0037024647

U2 - 10.1111/j.1749-6632.2002.tb04435.x

DO - 10.1111/j.1749-6632.2002.tb04435.x

M3 - Article

C2 - 12438091

AN - SCOPUS:0037024647

SN - 0077-8923

VL - 971

SP - 66

EP - 68

JO - Annals of the New York Academy of Sciences

JF - Annals of the New York Academy of Sciences

ER -

Phosphorylation of tyrosine hydroxylase in isolated mice adrenal glands

Abstract

Keywords

ASJC Scopus subject areas

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