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Gene Review

Ass1  -  argininosuccinate synthetase 1

Mus musculus

Synonyms: AA408052, ASS, Argininosuccinate synthase, Ass, Ass-1, ...
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Disease relevance of Ass1

  • The absence of citrin leads to a liver-specific, quantitative decrease of argininosuccinate synthetase (ASS), causing hyperammonemia and citrullinemia [1].
  • We demonstrated that the neonatal crisis in Ass mice can be ameliorated by the injection of a recombinant adenovirus carrying human AS cDNA (Ad.CMVhAS) within hours after birth [2].
  • Renal cell carcinoma does not express argininosuccinate synthetase and is highly sensitive to arginine deprivation via arginine deiminase [3].
  • Recently, pegylated arginine deiminase (ADI; EC has been used to treat the patients with hepatocellular carcinoma or melanoma, in which the level of argininosuccinate synthetase (ASS) activity is low or undetectable [3].
  • Based on our results, we suggest that immunization of AD patients with Ass should be done with caution as the increase in Ass could trigger the brain inflammation in uncontrollable level [4].

Psychiatry related information on Ass1

  • LRP-1, although abundant in brain microvessels in young mice, was downregulated in older animals, and this downregulation correlated with regional Ass accumulation in brains of Alzheimer's disease (AD) patients [5].

High impact information on Ass1


Chemical compound and disease context of Ass1


Biological context of Ass1


Anatomical context of Ass1


Associations of Ass1 with chemical compounds


Other interactions of Ass1

  • The strain distribution pattern for this polymorphism indicated close linkage of Ass-1 to Hc (the fifth component of complement) on proximal mouse chromosome 2 with a recombination fraction of 0.016 and a 95% confidence interval of 0.003 to 0.054 [10].
  • In contrast, these agents consistently inhibit induction of argininosuccinate synthetase mRNA in both LPS- and IFN-gamma-stimulated cells [17].

Analytical, diagnostic and therapeutic context of Ass1


  1. Slc25a13-knockout mice harbor metabolic deficits but fail to display hallmarks of adult-onset type II citrullinemia. Sinasac, D.S., Moriyama, M., Jalil, M.A., Begum, L., Li, M.X., Iijima, M., Horiuchi, M., Robinson, B.H., Kobayashi, K., Saheki, T., Tsui, L.C. Mol. Cell. Biol. (2004) [Pubmed]
  2. Correction of argininosuccinate synthetase (AS) deficiency in a murine model of citrullinemia with recombinant adenovirus carrying human AS cDNA. Ye, X., Whiteman, B., Jerebtsova, M., Batshaw, M.L. Gene Ther. (2000) [Pubmed]
  3. Renal cell carcinoma does not express argininosuccinate synthetase and is highly sensitive to arginine deprivation via arginine deiminase. Yoon, C.Y., Shim, Y.J., Kim, E.H., Lee, J.H., Won, N.H., Kim, J.H., Park, I.S., Yoon, D.K., Min, B.H. Int. J. Cancer (2007) [Pubmed]
  4. Role of fibrillar Abeta25-35 in the inflammation induced rat model with respect to oxidative vulnerability. Masilamoni, J.G., Jesudason, E.P., Jesudoss, K.S., Murali, J., Paul, S.F., Jayakumar, R. Free Radic. Res. (2005) [Pubmed]
  5. Clearance of Alzheimer's amyloid-ss(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier. Shibata, M., Yamada, S., Kumar, S.R., Calero, M., Bading, J., Frangione, B., Holtzman, D.M., Miller, C.A., Strickland, D.K., Ghiso, J., Zlokovic, B.V. J. Clin. Invest. (2000) [Pubmed]
  6. Pegylated Recombinant Human Arginase (rhArg-peg5,000mw) Inhibits the In vitro and In vivo Proliferation of Human Hepatocellular Carcinoma through Arginine Depletion. Cheng, P.N., Lam, T.L., Lam, W.M., Tsui, S.M., Cheng, A.W., Lo, W.H., Leung, Y.C. Cancer Res. (2007) [Pubmed]
  7. Coinduction of nitric oxide synthase and argininosuccinate synthetase in a murine macrophage cell line. Implications for regulation of nitric oxide production. Nussler, A.K., Billiar, T.R., Liu, Z.Z., Morris, S.M. J. Biol. Chem. (1994) [Pubmed]
  8. Presence of argininosuccinate synthetase in glial cells as revealed by peptide-specific antisera. Schmidlin, A., Kalbacher, H., Wiesinger, H. Biol. Chem. (1997) [Pubmed]
  9. Chromosomal locations of the mouse fatty acid oxidation genes Cpt1a, Cpt1b, Cpt2, Acadvl, and metabolically related Crat gene. Cox, K.B., Johnson, K.R., Wood, P.A. Mamm. Genome (1998) [Pubmed]
  10. Assignment of the structural gene for argininosuccinate synthetase to proximal mouse chromosome 2. Jackson, M.J., Surh, L.C., O'Brien, W.E., Beaudet, A.L. Genomics (1990) [Pubmed]
  11. Expression of inducible nitric oxide synthase and enzymes of arginine metabolism in Fusarium kyushuense-exposed mouse lung. Mahmoud, Y.A., Harada, K., Nagasaki, A., Gotoh, T., Takeya, M., Salimuddin, n.u.l.l., Ueda, A., Mori, M. Nitric Oxide (1999) [Pubmed]
  12. Liver argininosuccinate synthase binds to bacterial lipopolysaccharides and lipid A and inactivates their biological activities. Satoh, M., Iwahori, T., Sugawara, N., Yamazaki, M. J. Endotoxin Res. (2006) [Pubmed]
  13. Generation of a mouse model for citrullinemia by targeted disruption of the argininosuccinate synthetase gene. Patejunas, G., Bradley, A., Beaudet, A.L., O'Brien, W.E. Somat. Cell Mol. Genet. (1994) [Pubmed]
  14. Carnitine administration to juvenile visceral steatosis mice corrects the suppressed expression of urea cycle enzymes by normalizing their transcription. Horiuchi, M., Kobayashi, K., Tomomura, M., Kuwajima, M., Imamura, Y., Koizumi, T., Nikaido, H., Hayakawa, J., Saheki, T. J. Biol. Chem. (1992) [Pubmed]
  15. Development of ornithine metabolism in the mouse intestine. Riby, J.E., Hurwitz, R.E., Kretchmer, N. Pediatr. Res. (1990) [Pubmed]
  16. Localization of arginine biosynthetic enzymes in renal proximal tubules and abundance of mRNA during development. Morris, S.M., Sweeney, W.E., Kepka, D.M., O'Brien, W.E., Avner, E.D. Pediatr. Res. (1991) [Pubmed]
  17. Novel actions of aspirin and sodium salicylate: discordant effects on nitric oxide synthesis and induction of nitric oxide synthase mRNA in a murine macrophage cell line. Kepka-Lenhart, D., Chen, L.C., Morris, S.M. J. Leukoc. Biol. (1996) [Pubmed]
  18. Functional gamma-secretase inhibitors reduce beta-amyloid peptide levels in brain. Dovey, H.F., John, V., Anderson, J.P., Chen, L.Z., de Saint Andrieu, P., Fang, L.Y., Freedman, S.B., Folmer, B., Goldbach, E., Holsztynska, E.J., Hu, K.L., Johnson-Wood, K.L., Kennedy, S.L., Kholodenko, D., Knops, J.E., Latimer, L.H., Lee, M., Liao, Z., Lieberburg, I.M., Motter, R.N., Mutter, L.C., Nietz, J., Quinn, K.P., Sacchi, K.L., Seubert, P.A., Shopp, G.M., Thorsett, E.D., Tung, J.S., Wu, J., Yang, S., Yin, C.T., Schenk, D.B., May, P.C., Altstiel, L.D., Bender, M.H., Boggs, L.N., Britton, T.C., Clemens, J.C., Czilli, D.L., Dieckman-McGinty, D.K., Droste, J.J., Fuson, K.S., Gitter, B.D., Hyslop, P.A., Johnstone, E.M., Li, W.Y., Little, S.P., Mabry, T.E., Miller, F.D., Audia, J.E. J. Neurochem. (2001) [Pubmed]
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