Rat Arginase 1(ARG1) ELISA Kit

Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.; Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion. In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival. Plays a role in the immune response of alternatively activated or M2 macrophages in processes such as wound healing and tissue regeneration, immune defense against multicellular pathogens and parasites, and immune suppression and allergic inflammation; the regulatory outcome seems to be organ specific. In tumor-infiltrating dendritic cells (DCs) and myeloid-derived suppressor cells (MDSCs) plays a role in suppression of T cell-mediated antitumor immunity.

1. Arg1 expression, which is abundant in polarized M2 cells, is associated with strain/genotype differences from different pathways. PMID: 25872571
2. Arginase promotes endothelial dysfunction and hypertension in obesity by reducing arginine bioavailability. PMID: 25557182
3. Lower activity and expression levels of iNOS and higher activity and expression levels of arginase-1 in rat alveolar macrophages were found to be linked to the susceptibility of T. gondii infection in these cells PMID: 23691079
4. Diabetes-induced increases in arginase I were involved in the diabetes-induced impairment of retinal blood flow by a mechanism involving vascular endothelial cell dysfunction. PMID: 23232640
5. Report utility of arginase-1 for monitoring drug-induced liver injury in rat model. PMID: 22872058
6. Arginase and methylated arginine derivatives appear to be essential modulators of the inflammatory response in the acute phase of a multiple sclerosis model. PMID: 22507752
7. This study suggested that the increased level of arginase-1 in SCI is associated with an increase in macrophages and reactive astrocytes, possibly contributing to the modulation of inflammation during the course of SCI. PMID: 22325098
8. we postulate that the increased level of arginase-1, which is partly from M2 macrophages, contributes to the modulation of neuroinflammation in experimental autoimmune encephalomyelitis lesions PMID: 22483960
9. Arginase contributes significantly to L-proline supply for collagen synthesis in rat fibroblasts, in which arginase I is the predominant isoenzyme PMID: 20107769
10. These findings reveal the basis for thrombin induction of endothelial arginase I and indicate that arginase inhibition may be an attractive therapeutic alternative in the setting of arterial thrombosis and its associated endothelial dysfunction. PMID: 20032511
11. crystal structure: arginase-boronic acid complex highlights a physiological role in erectile function PMID: 10542097
12. Regulates low-level NO production by neuronal NOS (nNOS), most likely by competing for L-arginine. PMID: 11829529
13. Mechanisms involved in substrate binding and catalysis are elucidated via synthesis and evaluation of alternative substrate. PMID: 12020133
14. The upregulation of the arginase expression in wound derived fibroblasts underlines the distinct regulation of l-arginine metabolism in WFBs. PMID: 12069499
15. Total arginase activity and arginase I and II protein expression did not differ between the young and aged groups in the prefrontal cortex. PMID: 15013576
16. The highest affinity inhibitorsof Arg1 displace the metal-bridging hydroxide ion (and sometimes occupy a Mn(2+)(A) site found vacant in the native enzyme) and maintain a conserved array of hydrogen bonds with their alpha-amino and -carboxylate groups. PMID: 15248756
17. Arg I plays a critical role in the pathobiology of age-related endothelial dysfunction. PMID: 16380531
18. Arginase I protein was undetectable in the non-pregnant myometrium and up-regulated at term gestation, contributing to enhanced overall arginase activity at term gestation. PMID: 16735458
19. Arginase acts as central regulator of trophic factor-deprived motor neuron survival by suppressing nitric oxide production and consequent peroxynitrite toxicity. Resistance of motor neurons to trophic factor deprivation may result from increased arginase. PMID: 16914676
20. Thus, in addition to enhancing the expression of Arg I and spermine in repaired spinal cords, our treatment may recruit activated macrophages and create a more favorable environment for axonal regrowth. PMID: 17418108
21. diabetes-induced impairment of vasorelaxation to acetylcholine was correlated with increases in reactive oxygen species and arginase activity and arginase I expression in aorta and liver. PMID: 17967788
22. Arginase promotes neointima formation in rat injured carotid arteries. PMID: 19164802
23. upregulation of Arg I and increased synthesis of polyamines play an important role in the conditioning lesion effect, and spermidine is sufficient to promote optic nerve regeneration in vivo PMID: 19641117
24. Data indicate that iNOS-dependent S-nitrosylation of arginase 1 and the increase in arginase activity lead to eNOS uncoupling, contributing to the nitroso-redox imbalance, endothelial dysfunction, and vascular stiffness observed in vascular aging. PMID: 19661445
25. Limits iNOS-mediated NO synthese in macrophages, probably by limiting L-arginine availability for iNOS (substrate competition) PMID: 9179379

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Cytoplasm. Cytoplasmic granule.

Arginase family

Detected in liver (at protein level).

KEGG: rno:29221

STRING: 10116.ENSRNOP00000017911

UniGene: Rn.9857