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A Novel Rat Tyrosine Hydroxylase mRNA Species Generated by Alternative Splicing
Author(s) -
Lanièce Philippe,
Le Hir Hervé,
BodeauPéan Sylvie,
Charon Yves,
Valentin Luc,
Thermes Claude,
Mallet Jacques,
Dumas Sylvie
Publication year - 1996
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1996.66051819.x
Subject(s) - tyrosine hydroxylase , messenger rna , biology , exon , alternative splicing , rna splicing , precursor mrna , tyrosine , adrenal medulla , amino acid , microbiology and biotechnology , rna , in situ hybridization , biochemistry , translation (biology) , protein biosynthesis , enzyme , gene , catecholamine , endocrinology
Tyrosine hydroxylase (TH) catalyzes the first and rate‐limiting step in the biosynthesis of catecholamines. Among the various mechanisms implicated in the regulation of TH activity, alternative splicing of TH primary transcript has been described as a characteristic of higher primates and Drosophila . We investigated whether there is such a regulatory mechanism in the rat. Reverse transcriptase‐PCR experiments were performed with RNA from PC12 cells. A new TH mRNA species was evidenced, resulting from the use of an alternative donor site in exon 2. RNase protection assays and in situ hybridization experiments detected this mRNA species in the adrenal medulla but not in the main catecholaminergic nuclei of the CNS. The corresponding putative protein lacks 33 amino acids in the N‐terminal regulatory domain. A recombinant protein was produced in E. coli . Its in vitro specific activity was similar to that of the previously identified TH protein.