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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
Authors:Sawada Kazuhiko  Ando Masahiro  Sakata-Haga Hiromi  Sun Xue-Zhi  Jeong Young-Gil  Hisano Setsuji  Takeda Noriaki  Fukui Yoshihiro
Affiliation:Department of Anatomy and Developmental Neurobiology, University of Tokushima School of Medicine,; Department of Otolaryngology, University of Tokushima School of Medicine, Tokushima,; Environmental and Toxicological Research Group, National Institute of Radiological Sciences, Chiba, Japan,; Department of Anatomy, College of Medicine, Konyang University, Nonsan, Chungnam, South Korea, and; Laboratory of Neuroendocrinology, Institute of Basic Medical Sciences, University of Tsukuba, Tsukuba, Japan
Abstract:This study examined immunohistochemically the expression of an enzymatically active form of tyrosine hydroxylase (TH), phosphorylated TH at Ser40 (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.
Keywords:ataxia    cerebellum    dilute-lethal    phosphorylation    Purkinje cells    rolling mouse Nagoya    tyrosine hydroxylase
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