Open AccessCloning and sequencing of a rat CuZn superoxide dismutase cDNA
Author(s) -
DELABAR JeanMaurice,
NICOLE Annie,
JACOB Yves,
SINET PierreM.,
JÉRÔME Henri,
D'AURIOL Luc,
GALIBERT Francis,
MEUNIERROTIVAL Michèle
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb13500.x
Subject(s) - microbiology and biotechnology , superoxide dismutase , northern blot , messenger rna , complementary dna , biology , nucleic acid sequence , untranslated region , coding region , molecular cloning , western blot , clone (java method) , enzyme , gene , biochemistry
The molecular cloning and nucleotide sequence of a cDNA clone (pR SOD) for rat CuZn superoxide dismutase (CuZnSOD) is reported. Nucleotide sequence homology with human superoxide dismutase is 86% for the coding region and 71% for the 3′ untranslated region. The deduced amino acid sequence is given and the homologies with the sequences reported for other species are presented. Northern blot analysis of total RNA from various rat and mouse tissues and from two mouse cell lines show that pR SOD hybridizes with one mRNA species of about 0.7 kb. The amount of CuZnSOD mRNA in each tissue, measured by densitometry of the Northern blot autoradiograms, correlates with the enzymatic activity based on protein content. These results indicate that the control of CuZnSOD activity in mammalian tissues is largely dependent on the regulation of CuZnSOD mRNA levels. In human liver, fibroblasts and FG2 hepatoma cells, two CuZnSOD mRNAs (0.7 kb and 0.9 kb) are observed. The level of CuZnSOD mRNA in FG2 is 25% that of the liver and four times more abundant than in fibroblasts.