ArticleThe Biochemical journal2005
Regulation of all members of the antizyme family by antizyme inhibitor.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 54 citations in OpenAlex.
- EPLIN-β is a novel substrate of ornithine decarboxylase antizyme 1 and mediates cellular migration.Journal of cell science · 2023Article
- A novel mechanism for A-to-I RNA-edited AZIN1 in promoting tumor angiogenesis in colorectal cancer.Cell death & disease · 2022Article
- Genome-wide RNAi screen identifies novel players in human 60S subunit biogenesis including key enzymes of polyamine metabolism.Nucleic acids research · 2022Article
- Role of Antizyme Inhibitor Proteins in Cancers and Beyond.OncoTargets and therapy · 2021Review
- Polyamines in mammalian pathophysiology.Cellular and molecular life sciences : CMLS · 2019Review
- Purification and Characterization of Ornithine Decarboxylase fromMolecules (Basel, Switzerland) · 2019Article
- Developing a novel FRET assay, targeting the binding between Antizyme-AZIN.Scientific reports · 2019Article
- Antizyme Inhibitors in Polyamine Metabolism and Beyond: Physiopathological Implications.Medical sciences (Basel, Switzerland) · 2018Review
- Article
- RefSeq curation and annotation of antizyme and antizyme inhibitor genes in vertebrates.Nucleic acids research · 2015Article
- Article
- Evidence of a role for antizyme and antizyme inhibitor as regulators of human cancer.Molecular cancer research : MCR · 2011Review
- Critical factors governing the difference in antizyme-binding affinities between human ornithine decarboxylase and antizyme inhibitor.PloS one · 2011Article
- Minimal antizyme peptide fully functioning in the binding and inhibition of ornithine decarboxylase and antizyme inhibitor.PloS one · 2011Article
- Regulation of the nitrogen transfer pathway in the arbuscular mycorrhizal symbiosis: gene characterization and the coordination of expression with nitrogen flux.Plant physiology · 2010Article
- Critical factors determining dimerization of human antizyme inhibitor.The Journal of biological chemistry · 2009Article
- Antizyme and antizyme inhibitor, a regulatory tango.Cellular and molecular life sciences : CMLS · 2009Review
- Antizyme inhibitor 2 (AZIN2/ODCp) stimulates polyamine uptake in mammalian cells.The Journal of biological chemistry · 2008Article
- Identification of polymorphisms and balancing selection in the male infertility candidate gene, ornithine decarboxylase antizyme 3.BMC medical genetics · 2006Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ODC (ornithine decarboxylase) is the rate-limiting enzyme in polyamine biosynthesis. Polyamines are essential for cellular growth and differentiation but enhanced ODC activity is associated with cell transformation. Post-translationally, ODC is negatively regulated through members of the antizyme family. Antizymes inhibit ODC activity, promote ODC degradation through the 26 S proteasome and regulate polyamine transport. Besides the ubiquitously expressed antizymes 1 and 2, there is the tissue-specific antizyme 3 and an yet uncharacterized antizyme 4. Antizyme 1 has been shown to be negatively regulated through the AZI (antizyme inhibitor) that binds antizyme 1 with higher affinity compared with ODC. In the present study, we show by yeast two- and three-hybrid protein-protein interaction studies that AZI interacts with all members of the antizyme family and is capable of disrupting the interaction between each antizyme and ODC. In a yeast-based ODC complementation assay, we show that human ODC is able to complement fully the function of the yeast homologue of ODC. Co-expression of antizymes resulted in ODC inhibition and cessation of yeast growth. The antizyme-induced growth inhibition could be reversed by addition of putrescine or by the co-expression of AZI. The protein interactions could be confirmed by immunoprecipitation of the human ODC-antizyme 2-AZI complexes. In summary, we conclude that human AZI is capable of acting as a general inhibitor for all members of the antizyme family and that the previously not yet characterized antizyme 4 is capable of binding ODC and inhibiting its enzymic activity similar to the other members of the antizyme family.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.