The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

ARG1  -  arginase, liver

Sus scrofa

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of ARG1

 

High impact information on ARG1

 

Chemical compound and disease context of ARG1

  • These results suggest that NO-mediated dilation of coronary arterioles is inhibited in hypertension by an increase in arginase activity in EC, which limits l-arginine availability to NOS for NO production [2].
 

Biological context of ARG1

  • The administration of arginase in healthy pigs did not influence cardiac output, mean arterial pressure, heart rate, or total peripheral resistance, but led to an increase of mean pulmonary arterial pressure from 19 +/- 3 to 48 +/- 5 mmHg and to a reduction of arterial hepatic blood flow from 229 +/- 65 ml/min to 154 +/- 41 ml/min [1].
  • RESULTS: Myometrial arginase activity in pregnant animals was more than double that of myometrium from nonpregnant animals by the time the first measurement was made at 0.14 gestation [7].
  • OBJECTIVES: Arginase has been suggested to play an important role in cellular growth and development, particularly important to the fetus, by supplying L-ornithine for the synthesis of polyamines [7].
  • The objective of this study was to quantify arginine catabolism via arginase and nitric oxide synthase pathways in the mammary tissue of sows on d 28 of lactation [8].
  • BACKGROUND: Therapeutic use of supplemental arginine has been proposed as a safe and efficacious method to produce NO from nitric oxide synthase (NOS) and to produce proline and polyamines from arginase to improve wound healing [9].
 

Anatomical context of ARG1

  • The objectives of this study were to determine the following: 1) whether glucocorticoids play a role in induction of intestinal arginine metabolic enzymes during weaning; 2) whether the induction of enzyme activities was due to increases in corresponding mRNA levels; and 3) the identity of the arginase isoform(s) expressed in the small intestine [10].
  • Proline oxidase and OAT, but not arginase, were present in allantoic and amniotic fluids for the production of ornithine (the immediate substrate for polyamine synthesis) [11].
  • In enterocytes isolated from pig jejunum, L-arginine is metabolized to L-citrulline either directly or indirectly through the sequence of reactions catalysed by arginase and ornithine transcarbamylase [12].
  • CONCLUSION: Although NO appears to be necessary for granulation tissue formation, early supplemental arginine may disturb the reciprocal regulation of NOS 2 and arginase, leading to the preferential metabolism of arginine to excess NO rather than ornithine, with consequent reductions in angiogenesis and granulation tissue formation [9].
  • Arginase activity was roughly 10, 40 and 100 times greater in hepatic tissue than in renal cortex, renal medulla or intestinal mucosa, respectively, while hepatic ornithine transcarbamoylase (OTC) activity was about 15 times greater than the activity present in mucosa tissue [13].
 

Associations of ARG1 with chemical compounds

  • Following liver revascularization in the pigs, plasma arginase concentrations increased from 48 +/- 19 IU/L to 2613 +/- 944 IU/L, resulting in a drop in plasma levels of L-arginine (-87%) and in a drop in nitrite (-82%) and nitrate (-53%) concentrations [1].
  • The induction of arginase appears to be sufficient to account for the formation of urea from ammonia, glutamine and arginine in post-weaning pig enterocytes [6].
  • A primed continuous infusion of arginase (25,000 IU) increased plasma arginase levels to a maximum of 3,690 +/- 962 IU and evoked a decrease of L-arginine, but did not alter plasma nitrite or nitrate levels [1].
  • RU486 treatment attenuated the increase in arginase activity by 74% and completely prevented the ASL induction in weanling pigs, but had no effect on ASS activity [10].
  • The activities of arginase, argininosuccinate synthase (ASS), argininosuccinate lyase (ASL) and pyrroline-5-carboxylate (P5C) synthase were measured [14].
 

Other interactions of ARG1

 

Analytical, diagnostic and therapeutic context of ARG1

References

  1. Arginase release following liver reperfusion. Evidence of hemodynamic action of arginase infusions. Längle, F., Roth, E., Steininger, R., Winkler, S., Mühlbacher, F. Transplantation (1995) [Pubmed]
  2. Upregulation of vascular arginase in hypertension decreases nitric oxide-mediated dilation of coronary arterioles. Zhang, C., Hein, T.W., Wang, W., Miller, M.W., Fossum, T.W., McDonald, M.M., Humphrey, J.D., Kuo, L. Hypertension (2004) [Pubmed]
  3. Constitutive expression of arginase in microvascular endothelial cells counteracts nitric oxide-mediated vasodilatory function. Zhang, C., Hein, T.W., Wang, W., Chang, C.I., Kuo, L. FASEB J. (2001) [Pubmed]
  4. Arginine stimulates intestinal cell migration through a focal adhesion kinase dependent mechanism. Rhoads, J.M., Chen, W., Gookin, J., Wu, G.Y., Fu, Q., Blikslager, A.T., Rippe, R.A., Argenzio, R.A., Cance, W.G., Weaver, E.M., Romer, L.H. Gut (2004) [Pubmed]
  5. Improvement of cardiac output and liver blood flow and reduction of pulmonary vascular resistance by intravenous infusion of L-arginine during the early reperfusion period in pig liver transplantation. Längle, F., Steininger, R., Waldmann, E., Grünberger, T., Benditte, H., Mittlböck, M., Soliman, T., Schindl, M., Windberger, U., Mühlbacher, F., Roth, E. Transplantation (1997) [Pubmed]
  6. Urea synthesis in enterocytes of developing pigs. Wu, G. Biochem. J. (1995) [Pubmed]
  7. Myometrial arginase activity increases with advancing pregnancy in the guinea pig. Weiner, C.P., Knowles, R.G., Stegink, L.D., Dawson, J., Moncada, S. Am. J. Obstet. Gynecol. (1996) [Pubmed]
  8. Arginine catabolism in lactating porcine mammary tissue. O'Quinn, P.R., Knabe, D.A., Wu, G. J. Anim. Sci. (2002) [Pubmed]
  9. Local arginine supplementation results in sustained wound nitric oxide production and reductions in vascular endothelial growth factor expression and granulation tissue formation. Heffernan, D., Dudley, B., McNeil, P.L., Howdieshell, T.R. J. Surg. Res. (2006) [Pubmed]
  10. Glucocorticoids mediate the enhanced expression of intestinal type II arginase and argininosuccinate lyase in postweaning pigs. Flynn, N.E., Meininger, C.J., Kelly, K., Ing, N.H., Morris, S.M., Wu, G. J. Nutr. (1999) [Pubmed]
  11. Polyamine synthesis from proline in the developing porcine placenta. Wu, G., Bazer, F.W., Hu, J., Johnson, G.A., Spencer, T.E. Biol. Reprod. (2005) [Pubmed]
  12. Stimulation by D-glucose of the direct conversion of arginine to citrulline in enterocytes isolated from pig jejunum. Blachier, F., M'Rabet-Touil, H., Darcy-Vrillon, B., Posho, L., Duee, P.H. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  13. Urea cycle metabolism: effects of supplemental ornithine or citrulline on performance, tissue amino acid concentrations and enzymatic activity in young pigs fed arginine-deficient diets. Edmonds, M.S., Lowry, K.R., Baker, D.H. J. Anim. Sci. (1987) [Pubmed]
  14. Glucocorticoids play an important role in mediating the enhanced metabolism of arginine and glutamine in enterocytes of postweaning pigs. Flynn, N.E., Wu, G. J. Nutr. (1997) [Pubmed]
  15. Somatotropin-induced amino acid conservation in pigs involves differential regulation of liver and gut urea cycle enzyme activity. Bush, J.A., Wu, G., Suryawan, A., Nguyen, H.V., Davis, T.A. J. Nutr. (2002) [Pubmed]
  16. Porcine somatotropin, dietary protein and energy effects on arginase and transaminase activities in pigs. Rosebrough, R.W., Caperna, T.J., Campbell, R.G., Steele, N.C. International journal for vitamin and nutrition research. Internationale Zeitschrift für Vitamin- und Ernährungsforschung. Journal international de vitaminologie et de nutrition. (1998) [Pubmed]
  17. Effect of protein level and supplemental lysine on growth and urea cycle enzyme activity in the pig. Rosebrough, R.W., Steele, N.C., McMurtry, J.P. Growth. (1983) [Pubmed]
  18. Proteomic and transcriptomic analyses of differential stress/inflammatory responses in mandibular lymph nodes and oropharyngeal tonsils of European wild boars naturally infected with Mycobacterium bovis. Naranjo, V., Villar, M., Mart??n-Hernando, M.P., Vidal, D., H??fle, U., Gortazar, C., Kocan, K.M., V??zquez, J., de la Fuente, J. Proteomics (2007) [Pubmed]
  19. Direct colorimetric determination of serum arginase in various domestic animals. Mia, A.S., Koger, H.D. Am. J. Vet. Res. (1978) [Pubmed]
  20. A liver-derived immunosuppressive factor is an arginase: identification and mechanism of immunosuppression. Ohtani, Y., Hiyoshi, M., Ohkubo, T., Tsuji, K., Hagihara, M., Nakasaki, H., Makuuchi, H., Nagata, N., Mine, T., Takada, S., Yamamura, M., Tsuda, M. Biomed. Res. (2007) [Pubmed]
 
WikiGenes - Universities