Arginase catalyzes the hydrolysis of
arginine to
ornithine and
urea. At least two isoforms of mammalian arginase exists (
types I and II, this enzyme) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type II isoform encoded by this gene, is located in the mitochondria and expressed in extra-hepatic tissues, especially kidney. The physiologic role of this isoform is poorly understood; it is thought to play a role in
nitric oxide and
polyamine metabolism. Transcript variants of the type II gene resulting from the use of alternative
polyadenylation sites have been described.
Krause BJ, Prieto CP, Muñoz-Urrutia E, San Martín S, Sobrevia L, Casanello P (May 2012). "Role of arginase-2 and eNOS in the differential vascular reactivity and hypoxia-induced endothelial response in umbilical arteries and veins". Placenta. 33 (5): 360–6.
doi:
10.1016/j.placenta.2012.02.006.
hdl:10533/131155.
PMID22391327.
Warnken M, Haag S, Matthiesen S, Juergens UR, Racké K (April 2010). "Species differences in expression pattern of arginase isoenzymes and differential effects of arginase inhibition on collagen synthesis in human and rat pulmonary fibroblasts". Naunyn-Schmiedeberg's Archives of Pharmacology. 381 (4): 297–304.
doi:
10.1007/s00210-009-0489-6.
PMID20107769.
S2CID23774473.
Rodrigues Pereira N, Bandeira Moss M, Assumpção CR, Cardoso CB, Mann GE, Brunini TM, Mendes-Ribeiro AC (March 2010). "Oxidative stress, l-arginine-nitric oxide and arginase pathways in platelets from adolescents with anorexia nervosa". Blood Cells, Molecules & Diseases. 44 (3): 164–8.
doi:
10.1016/j.bcmd.2009.12.003.
PMID20071203.
Bron L, Jandus C, Andrejevic-Blant S, Speiser DE, Monnier P, Romero P, Rivals JP (February 2013). "Prognostic value of arginase-II expression and regulatory T-cell infiltration in head and neck squamous cell carcinoma". International Journal of Cancer. 132 (3): E85-93.
doi:
10.1002/ijc.27728.
PMID22815199.
S2CID40117905.
Arginase catalyzes the hydrolysis of
arginine to
ornithine and
urea. At least two isoforms of mammalian arginase exists (
types I and II, this enzyme) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type II isoform encoded by this gene, is located in the mitochondria and expressed in extra-hepatic tissues, especially kidney. The physiologic role of this isoform is poorly understood; it is thought to play a role in
nitric oxide and
polyamine metabolism. Transcript variants of the type II gene resulting from the use of alternative
polyadenylation sites have been described.
Krause BJ, Prieto CP, Muñoz-Urrutia E, San Martín S, Sobrevia L, Casanello P (May 2012). "Role of arginase-2 and eNOS in the differential vascular reactivity and hypoxia-induced endothelial response in umbilical arteries and veins". Placenta. 33 (5): 360–6.
doi:
10.1016/j.placenta.2012.02.006.
hdl:10533/131155.
PMID22391327.
Warnken M, Haag S, Matthiesen S, Juergens UR, Racké K (April 2010). "Species differences in expression pattern of arginase isoenzymes and differential effects of arginase inhibition on collagen synthesis in human and rat pulmonary fibroblasts". Naunyn-Schmiedeberg's Archives of Pharmacology. 381 (4): 297–304.
doi:
10.1007/s00210-009-0489-6.
PMID20107769.
S2CID23774473.
Rodrigues Pereira N, Bandeira Moss M, Assumpção CR, Cardoso CB, Mann GE, Brunini TM, Mendes-Ribeiro AC (March 2010). "Oxidative stress, l-arginine-nitric oxide and arginase pathways in platelets from adolescents with anorexia nervosa". Blood Cells, Molecules & Diseases. 44 (3): 164–8.
doi:
10.1016/j.bcmd.2009.12.003.
PMID20071203.
Bron L, Jandus C, Andrejevic-Blant S, Speiser DE, Monnier P, Romero P, Rivals JP (February 2013). "Prognostic value of arginase-II expression and regulatory T-cell infiltration in head and neck squamous cell carcinoma". International Journal of Cancer. 132 (3): E85-93.
doi:
10.1002/ijc.27728.
PMID22815199.
S2CID40117905.