ArticleThe Biochemical journal1997
Structure, organization and expression of the mouse ornithine decarboxylase antizyme gene.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Biological Significance and Therapeutic Promise of Programmed Ribosomal Frameshifting.International journal of molecular sciences · 2025Review
- Article
- Role of Polyamine-Induced Dimerization of Antizyme in Its Cellular Functions.International journal of molecular sciences · 2022Article
- Systemic overexpression of antizyme 1 in mouse reduces ornithine decarboxylase activity without major changes in tissue polyamine homeostasis.Transgenic research · 2014Article
- OAZ-t/OAZ3 is essential for rigid connection of sperm tails to heads in mouse.PLoS genetics · 2009Article
- Antizyme mRNA distribution and regulation in rat small intestinal enterocytes.Digestive diseases and sciences · 2002Article
- Concurrent overexpression of ornithine decarboxylase and spermidine/spermine N(1)-acetyltransferase further accelerates the catabolism of hepatic polyamines in transgenic mice.The Biochemical journal · 2001Article
- Antizyme expression: a subversion of triplet decoding, which is remarkably conserved by evolution, is a sensor for an autoregulatory circuit.Nucleic acids research · 2000Review
- Two zebrafish (Danio rerio) antizymes with different expression and activities.The Biochemical journal · 2000Article
- Identification of putative programmed -1 ribosomal frameshift signals in large DNA databases.Genome research · 1999Article
- Anti-tumor activity of antizyme which targets the ornithine decarboxylase (ODC) required for cell growth and transformation.Oncogene · 1999Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ornithine decarboxylase antizyme is a protein that participates in the regulation of cellular polyamine levels. In this study we have isolated and sequenced the mouse gene encoding antizyme protein. Transfection of various cell lines with a 5.5 kb genomic fragment containing the antizyme locus resulted in the production of a 29 kDa antizyme protein, confirming that this locus contained a functional gene. Comparison of the mouse gene with the corresponding rat gene [Miyazaki, Matsufuji and Hayashi, (1992) Gene 113, 191-197] revealed an identical exon/intron organization and high level of nucleotide sequence conservation that was 89% for the entire transcription unit. Protein-coding regions of the two genes exhibited 97% nucleotide sequence identity and there were only four amino acid differences between the 227-residue antizyme protein sequences of the mouse and rat. The promoter of the antizyme gene was functional in mouse (N2A and NIH/3T3) and hamster (CHO) cell lines. The presence of 0.1 mM spermidine in culture medium increased the amount of immunoreactive antizyme protein in cells transfected with the antizyme gene or antizyme cDNA, possibly owing to facilitated frameshifting in the translation of antizyme mRNA. Recombinant antizyme protein was also produced in Escherichia coli and used to raise specific polyclonal antibodies in rabbits and to devise immunological methods for the measurement of antizyme concentration.
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