Entry - *601579 - ORNITHINE DECARBOXYLASE ANTIZYME 1; OAZ1 - OMIM
 
* 601579

ORNITHINE DECARBOXYLASE ANTIZYME 1; OAZ1


Alternative titles; symbols

OAZ
ANTIZYME 1


HGNC Approved Gene Symbol: OAZ1

Cytogenetic location: 19p13.3     Genomic coordinates (GRCh38): 19:2,269,486-2,273,488 (from NCBI)


TEXT

Description

Antizyme (ornithine decarboxylase antizyme) is the sole animal gene product known to be expressed with translational frameshifting (Rom and Kahana, 1994; Matsufuji et al., 1995). Elevation of cellular polyamine levels induces antizyme synthesis by raising frameshift efficiency. Matsufuji et al. (1996) noted that induced antizyme prevents further increase in polyamines by binding to ornithine decarboxylase (ODC; 165640), a key regulatory enzyme in polyamine biosynthesis, which accelerates degradation of ODC by the 26S proteasome. Antizyme also inhibits cellular uptake of polyamines.


Cloning and Expression

Tewari et al. (1994) reported the sequence of a human antizyme cDNA cloned from gingival fibroblasts. Matsufuji et al. (1996) obtained an antizyme cDNA from human liver based on the rat cDNA sequence. The 2 sequences are almost identical with each other. On Southern analysis, a single gene was detected.

Hayashi et al. (1997) reported the complete nucleotide sequence of the human antizyme gene.


Gene Structure

Hayashi et al. (1997) determined that the human antizyme gene consists of 5 exons.


Mapping

By fluorescence in situ hybridization, Matsufuji et al. (1996) assigned the antizyme gene to 19p13.3. Thus, the human antizyme gene is not linked with the ornithine decarboxylase gene, which is located on 2p.


Animal Model

Mackintosh et al. (2000) generated transgenic mice in which a very high level of constitutive antizyme-1 expression was directed specifically to the heart through the use of a cardiac-specific promoter. The high antizyme level did not abolish endogenous ODC activity and allowed apparently normal cardiac growth. However, a single acute dose of, or prolonged exposure to, isoproterenol caused substantially increased cardiac ODC activity and subsequent polyamine accumulation in nontransgenic but not in transgenic mice.


REFERENCES

  1. Hayashi, T., Matsufuji, S., Hayashi, S. Characterization of the human antizyme gene. Gene 203: 131-139, 1997. [PubMed: 9426243, related citations] [Full Text]

  2. Mackintosh, C. A., Feith, D. J., Shantz, L. M., Pegg, A. E. Overexpression of antizyme in the hearts of transgenic mice prevents the isoprenaline-induced increase in cardiac ornithine decarboxylase activity and polyamines, but does not prevent cardiac hypertrophy. Biochem. J. 350: 645-653, 2000. [PubMed: 10970775, related citations]

  3. Matsufuji, S., Inazawa, J., Hayashi, T., Miyazaki, Y., Ichiba, T., Furusaka, A., Matsufuji, T., Atkins, J. F., Gesteland, R. F., Murakami, Y., Hayashi, S. Assignment of the human antizyme gene (OAZ) to chromosome 19p13.3 by fluorescence in situ hybridization. Genomics 38: 102-104, 1996. [PubMed: 8954789, related citations] [Full Text]

  4. Matsufuji, S., Matsufuji, T., Miyazaki, Y., Murakami, Y., Atkins, J. F., Gesteland, R. F., Hayashi, S. Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme. Cell 80: 51-60, 1995. [PubMed: 7813017, related citations] [Full Text]

  5. Rom, E., Kahana, C. Polyamines regulate the expression of ornithine decarboxylase antizyme in vitro by inducing ribosomal frame-shifting. Proc. Nat. Acad. Sci. 91: 3959-3963, 1994. Note: Erratum: Proc. Nat. Acad. Sci. 91: 9195 only, 1994. [PubMed: 8171019, related citations] [Full Text]

  6. Tewari, D. S., Qian, Y., Thornton, R. D., Pieringer, J., Taub, R., Mochan, E., Tewari, M. Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme. Biochim. Biophys. Acta 1209: 293-295, 1994. [PubMed: 7811704, related citations] [Full Text]


Paul J. Converse - updated : 2/28/2001
Victor A. McKusick - updated : 6/15/2000
Victor A. McKusick - updated : 3/12/1999
Creation Date:
Victor A. McKusick : 12/13/1996
carol : 04/22/2013
alopez : 11/29/2010
carol : 3/1/2001
cwells : 2/28/2001
carol : 2/27/2001
cwells : 2/27/2001
terry : 6/15/2000
alopez : 9/8/1999
terry : 3/12/1999
terry : 7/9/1997
jenny : 1/14/1997
jenny : 12/20/1996
mark : 12/16/1996

* 601579

ORNITHINE DECARBOXYLASE ANTIZYME 1; OAZ1


Alternative titles; symbols

OAZ
ANTIZYME 1


HGNC Approved Gene Symbol: OAZ1

Cytogenetic location: 19p13.3     Genomic coordinates (GRCh38): 19:2,269,486-2,273,488 (from NCBI)


TEXT

Description

Antizyme (ornithine decarboxylase antizyme) is the sole animal gene product known to be expressed with translational frameshifting (Rom and Kahana, 1994; Matsufuji et al., 1995). Elevation of cellular polyamine levels induces antizyme synthesis by raising frameshift efficiency. Matsufuji et al. (1996) noted that induced antizyme prevents further increase in polyamines by binding to ornithine decarboxylase (ODC; 165640), a key regulatory enzyme in polyamine biosynthesis, which accelerates degradation of ODC by the 26S proteasome. Antizyme also inhibits cellular uptake of polyamines.


Cloning and Expression

Tewari et al. (1994) reported the sequence of a human antizyme cDNA cloned from gingival fibroblasts. Matsufuji et al. (1996) obtained an antizyme cDNA from human liver based on the rat cDNA sequence. The 2 sequences are almost identical with each other. On Southern analysis, a single gene was detected.

Hayashi et al. (1997) reported the complete nucleotide sequence of the human antizyme gene.


Gene Structure

Hayashi et al. (1997) determined that the human antizyme gene consists of 5 exons.


Mapping

By fluorescence in situ hybridization, Matsufuji et al. (1996) assigned the antizyme gene to 19p13.3. Thus, the human antizyme gene is not linked with the ornithine decarboxylase gene, which is located on 2p.


Animal Model

Mackintosh et al. (2000) generated transgenic mice in which a very high level of constitutive antizyme-1 expression was directed specifically to the heart through the use of a cardiac-specific promoter. The high antizyme level did not abolish endogenous ODC activity and allowed apparently normal cardiac growth. However, a single acute dose of, or prolonged exposure to, isoproterenol caused substantially increased cardiac ODC activity and subsequent polyamine accumulation in nontransgenic but not in transgenic mice.


REFERENCES

  1. Hayashi, T., Matsufuji, S., Hayashi, S. Characterization of the human antizyme gene. Gene 203: 131-139, 1997. [PubMed: 9426243] [Full Text: https://doi.org/10.1016/s0378-1119(97)00504-0]

  2. Mackintosh, C. A., Feith, D. J., Shantz, L. M., Pegg, A. E. Overexpression of antizyme in the hearts of transgenic mice prevents the isoprenaline-induced increase in cardiac ornithine decarboxylase activity and polyamines, but does not prevent cardiac hypertrophy. Biochem. J. 350: 645-653, 2000. [PubMed: 10970775]

  3. Matsufuji, S., Inazawa, J., Hayashi, T., Miyazaki, Y., Ichiba, T., Furusaka, A., Matsufuji, T., Atkins, J. F., Gesteland, R. F., Murakami, Y., Hayashi, S. Assignment of the human antizyme gene (OAZ) to chromosome 19p13.3 by fluorescence in situ hybridization. Genomics 38: 102-104, 1996. [PubMed: 8954789] [Full Text: https://doi.org/10.1006/geno.1996.0601]

  4. Matsufuji, S., Matsufuji, T., Miyazaki, Y., Murakami, Y., Atkins, J. F., Gesteland, R. F., Hayashi, S. Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme. Cell 80: 51-60, 1995. [PubMed: 7813017] [Full Text: https://doi.org/10.1016/0092-8674(95)90450-6]

  5. Rom, E., Kahana, C. Polyamines regulate the expression of ornithine decarboxylase antizyme in vitro by inducing ribosomal frame-shifting. Proc. Nat. Acad. Sci. 91: 3959-3963, 1994. Note: Erratum: Proc. Nat. Acad. Sci. 91: 9195 only, 1994. [PubMed: 8171019] [Full Text: https://doi.org/10.1073/pnas.91.9.3959]

  6. Tewari, D. S., Qian, Y., Thornton, R. D., Pieringer, J., Taub, R., Mochan, E., Tewari, M. Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme. Biochim. Biophys. Acta 1209: 293-295, 1994. [PubMed: 7811704] [Full Text: https://doi.org/10.1016/0167-4838(94)90199-6]


Contributors:
Paul J. Converse - updated : 2/28/2001
Victor A. McKusick - updated : 6/15/2000
Victor A. McKusick - updated : 3/12/1999

Creation Date:
Victor A. McKusick : 12/13/1996

Edit History:
carol : 04/22/2013
alopez : 11/29/2010
carol : 3/1/2001
cwells : 2/28/2001
carol : 2/27/2001
cwells : 2/27/2001
terry : 6/15/2000
alopez : 9/8/1999
terry : 3/12/1999
terry : 7/9/1997
jenny : 1/14/1997
jenny : 12/20/1996
mark : 12/16/1996