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Abnormal expression of tyrosine hydroxylase not accompanied by phosphorylation at serine 40 in cerebellar Purkinje cells of ataxic mutant mice, rolling mouse Nagoya and dilute‐lethal
Author(s) -
Sawada Kazuhiko,
Ando Masahiro,
SakataHaga Hiromi,
Sun XueZhi,
Jeong YoungGil,
Hisano Setsuji,
Takeda Noriaki,
Fukui Yoshihiro
Publication year - 2004
Publication title -
congenital anomalies
Language(s) - English
Resource type - Journals
eISSN - 1741-4520
pISSN - 0914-3505
DOI - 10.1111/j.1741-4520.2003.00008.x
Subject(s) - tyrosine hydroxylase , cerebellum , immunostaining , mutant , phosphorylation , tyrosine , purkinje cell , immunohistochemistry , biology , medicine , endocrinology , chemistry , microbiology and biotechnology , biochemistry , dopamine , gene
This study examined immunohistochemically the expression of an enzymatically active form of tyrosine hydroxylase (TH), phosphorylated TH at Ser 40 (phospho‐TH), in the cerebellum of ataxic mutant mice, rolling mouse Nagoya (RMN) and dilute‐lethal (DL). TH immunostaining appeared in some Purkinje cells in RMN and DL, but in a few of the Purkinje cells of littermate controls for both mutants. In all groups of mice, there were no phospho‐TH immunoreactive Purkinje cells in the cerebellum, although the subsets of TH immunoreactive Purkinje cells were found in the adjacent sections. The results suggest that TH expression in the Purkinje cells of ataxic mutants abnormally increases without activation of this enzyme by phosphorylation. This may mean that TH in Purkinje cells is not related to catecholamine synthesis.