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Asl  -  argininosuccinate lyase

Rattus norvegicus

Synonyms: ASAL, Argininosuccinate lyase, Arginosuccinase
 
 
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Disease relevance of Asl

 

High impact information on Asl

 

Chemical compound and disease context of Asl

 

Biological context of Asl

  • Molecular cloning and nucleotide sequence of rat brain argininosuccinate lyase cDNA with an extremely long 5'-untranslated sequence: evidence for the identity of the brain and liver enzymes [9].
  • Using as a probe rat liver argininosuccinate lyase cDNA, already isolated and sequenced (Amaya, Y., Matsubasa, T., Takiguchi, M., Kobayashi, K., Saheki, T., Kawamoto, S. and Mori, M., J. Biochem., 103 (1988) 177-181), we screened a rat brain cDNA library constructed in the lambda gt11 expression vector and obtained a single cDNA clone [9].
  • Multiple copies of partial and inverted (antisense) B1 repeats and multiple upstream ATG codons are present in the region, which suggests a possibility of translational control of the argininosuccinate lyase gene expression in rat brain [10].
  • Hypoxia did not affect ASL mRNA stability, indicating that this effect occurs at the transcriptional level [1].
  • The ASL mRNA was first detectable on day 15.5 of gestation and increased in amount concomitantly with the rise in the enzyme activity, suggesting that the appearance of enzyme activity reflects the turning on of specific gene transcription [11].
 

Anatomical context of Asl

 

Associations of Asl with chemical compounds

 

Regulatory relationships of Asl

 

Other interactions of Asl

 

Analytical, diagnostic and therapeutic context of Asl

  • Northern-blot analysis revealed that these agents only gave a transient induction of ASL mRNA amount, which reached a peak at 6 h and declined thereafter [20].
  • Expression of urea synthesis, as reflected by carbamoylphosphate synthetase mRNA, showed a gradual decline after 90% hepatectomy, in contrast to rising levels of argininosuccinate lyase and arginase mRNA, possibly serving polyamine rather than urea synthesis [24].
  • Using RNase protection assay and non-radioactive in situ hybridization on aggregate cryosections, we show that both AS and AL genes are induced in astrocytes but not in neurons of aggregates exposed to 5 mM NH4Cl [2].
  • Hyperammonemia: regulation of argininosuccinate synthetase and argininosuccinate lyase genes in aggregating cell cultures of fetal rat brain [2].
  • To this end, ASL was purified, an ELISA assay was established to quantify the enzyme protein and a cDNA clone was used to measure the amount of specific mRNA in the liver in various stages of development [25].

References

  1. Identification of argininosuccinate lyase as a hypoxia-responsive gene in rat hepatocytes. Latasa, M.U., Carretero, M.V., García-Trevijano, E.R., Torres, L., Mato, J.M., Avila, M.A. J. Hepatol. (2000) [Pubmed]
  2. Hyperammonemia: regulation of argininosuccinate synthetase and argininosuccinate lyase genes in aggregating cell cultures of fetal rat brain. Braissant, O., Honegger, P., Loup, M., Iwase, K., Takiguchi, M., Bachmann, C. Neurosci. Lett. (1999) [Pubmed]
  3. Citrulline-argininosuccinate-arginine cycle coupled to Ca2+-signaling in rat pancreatic beta-cells. Nakata, M., Yada, T., Nakagawa, S., Kobayashi, K., Maruyama, I. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  4. Effects of acute ammonia toxicity on nitric oxide (NO), citrulline-NO cycle enzymes, arginase and related metabolites in different regions of rat brain. Swamy, M., Zakaria, A.Z., Govindasamy, C., Sirajudeen, K.N., Nadiger, H.A. Neurosci. Res. (2005) [Pubmed]
  5. Preparation of recombinant argininosuccinate synthetase and argininosuccinate lyase: expression of the enzymes in rat tissues. Yu, Y., Terada, K., Nagasaki, A., Takiguchi, M., Mori, M. J. Biochem. (1995) [Pubmed]
  6. Structure of the rat argininosuccinate lyase gene: close similarity to chicken delta-crystallin genes. Matsubasa, T., Takiguchi, M., Amaya, Y., Matsuda, I., Mori, M. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  7. Coinduction of nitric oxide synthase, argininosuccinate synthetase, and argininosuccinate lyase in lipopolysaccharide-treated rats. RNA blot, immunoblot, and immunohistochemical analyses. Nagasaki, A., Gotoh, T., Takeya, M., Yu, Y., Takiguchi, M., Matsuzaki, H., Takatsuki, K., Mori, M. J. Biol. Chem. (1996) [Pubmed]
  8. Argininosuccinate synthetase mRNA and activity are induced by immunostimulants in vascular smooth muscle. Role in the regeneration or arginine for nitric oxide synthesis. Hattori, Y., Campbell, E.B., Gross, S.S. J. Biol. Chem. (1994) [Pubmed]
  9. Molecular cloning and nucleotide sequence of rat brain argininosuccinate lyase cDNA with an extremely long 5'-untranslated sequence: evidence for the identity of the brain and liver enzymes. Kawamoto, S., Kaneko, T., Mizuki, N., Ohsuga, A., Fukushima, J., Amaya, Y., Mori, M., Okuda, K. Brain Res. Mol. Brain Res. (1989) [Pubmed]
  10. Structural analysis of an extremely long 5'-noncoding region of rat brain argininosuccinate lyase mRNA: presence of multiple B1 repeats and multiple upstream AUG codons, and a possibility of translational control. Kawamoto, S., Amaya, Y., Hattori, S., Miyagi, Y., Onishi, H., Okuda, K. Biochim. Biophys. Acta (1993) [Pubmed]
  11. Expression of argininosuccinate lyase mRNA in foetal hepatocytes. Regulation by glucocorticoids and insulin. Husson, A., Renouf, S., Fairand, A., Buquet, C., Benamar, M., Vaillant, R. Eur. J. Biochem. (1990) [Pubmed]
  12. NADPH-diaphorase and cytosolic urea cycle enzymes in the rat spinal cord. Nakamura, H. J. Comp. Neurol. (1997) [Pubmed]
  13. Regulation of diaphragmatic nitric oxide synthase expression during hypobaric hypoxia. Javeshghani, D., Sakkal, D., Mori, M., Hussain, S.N. Am. J. Physiol. Lung Cell Mol. Physiol. (2000) [Pubmed]
  14. Argininosuccinate synthetase and argininosuccinate lyase are localized around mitochondria: an immunocytochemical study. Cohen, N.S., Kuda, A. J. Cell. Biochem. (1996) [Pubmed]
  15. Amino acid sequence of rat argininosuccinate lyase deduced from cDNA. Amaya, Y., Matsubasa, T., Takiguchi, M., Kobayashi, K., Saheki, T., Kawamoto, S., Mori, M. J. Biochem. (1988) [Pubmed]
  16. Regulation of messenger ribonucleic acid levels for five urea cycle enzymes in cultured rat hepatocytes. Requirements for cyclic adenosine monophosphate, glucocorticoids, and ongoing protein synthesis. Nebes, V.L., Morris, S.M. Mol. Endocrinol. (1988) [Pubmed]
  17. Insulin antagonism of dexamethasone-induced increase or argininosuccinate synthetase and argininosuccinate lyase activities in cultured fetal rat liver. Räihä, N.C., Edkins, E. Biol. Neonate (1977) [Pubmed]
  18. Dexamethasone and glucagon cause synergistic increases of urea cycle enzyme activities in livers of normal but not adrenalectomized rats. Snodgrass, P.J. Enzyme (1991) [Pubmed]
  19. Expression and localization of enzymes of arginine metabolism in the rat eye. Koshiyama, Y., Gotoh, T., Miyanaka, K., Kobayashi, T., Negi, A., Mori, M. Curr. Eye Res. (2000) [Pubmed]
  20. Changes in levels of argininosuccinate lyase mRNA during induction by glucagon and cyclic AMP in cultured foetal-rat hepatocytes. Renouf, S., Buquet, C., Fairand, A., Benamar, M., Husson, A. Biochem. J. (1993) [Pubmed]
  21. Effect of cyclic AMP and prostaglandin E2 on the induction of nitric oxide- and prostanoid-forming pathways in cultured rat mesangial cells. Nüsing, R.M., Klein, T., Pfeilschifter, J., Ullrich, V. Biochem. J. (1996) [Pubmed]
  22. Regulation of cerebellar nitric oxide production in response to prolonged in vivo hypoxia. Guo, Y., Ward, M.E., Beasjours, S., Mori, M., Hussain, S.N. J. Neurosci. Res. (1997) [Pubmed]
  23. Protein damage and lipid peroxidation: effects of diethyl maleate, bromotrichloromethane and vitamin E on ammonia, urea and enzymes involved in ammonia metabolism. Park, J.R., Tappel, A.L. Toxicol. Lett. (1991) [Pubmed]
  24. Expression of messenger RNA for liver functions following 70% and 90% hepatectomy. Tygstrup, N., Jensen, S.A., Krog, B., Pietrangelo, A., Shafritz, D.A. J. Hepatol. (1996) [Pubmed]
  25. Changes in argininosuccinate lyase gene expression in the rat liver during development. Benamar, M., Gautier, C., Renouf, S., Fairand, A., Husson, A. Biol. Neonate (1992) [Pubmed]
 
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