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Phosphorylation of Tyrosine Hydroxylase in Isolated Mice Adrenal Glands
Author(s) -
TOSKA KAREN,
KLEPPE RUNE,
COHEN PHILIP,
HAAVIK JAN
Publication year - 2002
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2002.tb04435.x
Subject(s) - tyrosine hydroxylase , phosphorylation , tyrosine 3 monooxygenase , adrenal gland , 21 hydroxylase , endocrinology , tyrosine , medicine , chemistry , biology , enzyme , biochemistry , congenital adrenal hyperplasia
A bstract : 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.
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