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The Absence of Phosphorylated Tyrosine Hydroxylase Expression in the Purkinje Cells of the Ataxic Mutant Pogo Mouse
Author(s) -
Lee N. S.,
Kim C. T.,
Han S. Y.,
Kawk J. H.,
Sawada K.,
Fukui Y.,
Jeong Y. G.
Publication year - 2006
Publication title -
anatomia, histologia, embryologia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.34
H-Index - 35
eISSN - 1439-0264
pISSN - 0340-2096
DOI - 10.1111/j.1439-0264.2005.00657.x
Subject(s) - tyrosine hydroxylase , cerebellum , mutant , immunostaining , immunohistochemistry , tyrosine , biology , phosphorylation , phenotype , microbiology and biotechnology , immunofluorescence , purkinje cell , medicine , endocrinology , biochemistry , antibody , immunology , gene
Summary The pogo mouse is a new ataxic autosomal recessive mutant that arose in Korean wild mice (KJR/Mskist). Its ataxic phenotype includes difficulty in maintaining a normal posture and the inability to walk in a straight line. Several studies have reported that tyrosine hydroxylase (TH) is persistently ectopically expressed in particular subsets of Purkinje cells in a parasagittal banding pattern in several ataxic mutant mice, e.g. tottering alleles and pogo mice. In this present study, we examined the expression of an enzymatically active form of TH and phosphorylated TH at Ser 40 (phospho‐TH) by using immunohistochemistry and double immunofluorescence in the cerebellum of pogo mice. TH immunostaining appeared in some Purkinje cells in pogo, but in only a few of Purkinje cells of their heterozygous littermate controls. In all groups of mice, no phospho‐TH immunoreactive Purkinje cells were observed in the cerebellum, although subsets of TH immunoreactive Purkinje cells were found in adjacent sections. This study suggests that TH expression in the Purkinje cells of pogo abnormally increases without activation of this enzyme by phosphorylation. This may mean that TH in the Purkinje cells of these mutants does not catalyse the conversion of tyrosine to l ‐DOPA, and is not related to catecholamine synthesis.