| Gene References into Functions |
- Arg1 expression, which is abundant in polarized M2 cells, is associated with strain/genotype differences from different pathways. PMID: 25872571
- Arginase promotes endothelial dysfunction and hypertension in obesity by reducing arginine bioavailability. PMID: 25557182
- 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
- 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
- Report utility of arginase-1 for monitoring drug-induced liver injury in rat model. PMID: 22872058
- 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
- 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
- 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
- Arginase contributes significantly to L-proline supply for collagen synthesis in rat fibroblasts, in which arginase I is the predominant isoenzyme PMID: 20107769
- 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
- crystal structure: arginase-boronic acid complex highlights a physiological role in erectile function PMID: 10542097
- Regulates low-level NO production by neuronal NOS (nNOS), most likely by competing for L-arginine. PMID: 11829529
- Mechanisms involved in substrate binding and catalysis are elucidated via synthesis and evaluation of alternative substrate. PMID: 12020133
- The upregulation of the arginase expression in wound derived fibroblasts underlines the distinct regulation of l-arginine metabolism in WFBs. PMID: 12069499
- 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
- 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
- Arg I plays a critical role in the pathobiology of age-related endothelial dysfunction. PMID: 16380531
- 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
- 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
- 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
- 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
- Arginase promotes neointima formation in rat injured carotid arteries. PMID: 19164802
- 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
- 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
- Limits iNOS-mediated NO synthese in macrophages, probably by limiting L-arginine availability for iNOS (substrate competition) PMID: 9179379
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