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Human ARG1 Protein expressed in Escherichia coli (E. coli) - ABIN2666493
Babu, Kumaraswami, Nutman: Alternatively activated and immunoregulatory monocytes in human filarial infections. in The Journal of infectious diseases 2009
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Human ARG1 Protein expressed in HEK-293 Cells - ABIN2180550
Ikemoto, Tabata, Miyake, Kono, Mori, Totani, Murachi: Expression of human liver arginase in Escherichia coli. Purification and properties of the product. in The Biochemical journal 1990
Show all 4 references for 2180550
Human ARG1 Protein expressed in Escherichia coli (E. coli) - ABIN667001
Iyer, Yoo, Kern, Rozengurt, Tsoa, OBrien, Yu, Grody, Cederbaum: Mouse model for human arginase deficiency. in Molecular and cellular biology 2002
Show all 2 references for 667001
Human ARG1 Protein expressed in Human Cells - ABIN2004367
Haffner, Teupser, Holdt, Ernst, Burkhardt, Thiery: Regulation of arginase-1 expression in macrophages by a protein kinase A type I and histone deacetylase dependent pathway. in Journal of cellular biochemistry 2008
High arginase expression is associated with glioblastoma.
Report the value of Arg-1 in distinguishing HepPar-1-positive prostatic carcinoma from hepatocellular carcinoma at metastatic sites or cases of liver metastasis from prostate carcinoma.
AEG-1 (show MTDH Proteins) is positively activated in the tumorigenesis and deterioration of NSCLC.
Arginase-1 expression is common (62.5%) in hepatoid adenocarcinoma and hence it is not useful in distinguishing hepatocellular carcinoma from hepatoid adenocarcinoma.
Arginase 1 was highly expressed by tumor-associated Gr1+ microglia and macrophages.
The authors report here that Candida albicans blocks nitric oxide production in human-monocyte-derived macrophages by induction of host arginase activity.
Evidence for a negative association of arginase I with job strain and positive association with job control and social support in females.
Two argininemia patients were initially diagnosed by tandem mass spectrometry in newborn screening. Mutation analysis of the ARG1 gene was performed by direct sequencing.Two missense mutations, p.D100N and p.R71T, in Patient-1 were predicted to lower the stability of arginase Iota by analysis of 3D crystal structure, while two nonsense mutations, p.G12X and p.E42X, in Patient-2 were predicted to lead to truncated protein.
The results of this study suggested a novel relationship exists between ARG1, neutrophil-lymphocyte ratio , and stroke severity which may help guide future mechanistic studies of post-stroke immune suppression.
This study provides a molecular mechanism of the pathogenesis of systemic lupus erythematosus by demonstrating an Arg-1-dependent effect of myeloid-derived suppressor cells in the development of TH17 cell-associated autoimmunity.
Arginase has a role in preventing angiogenesis in endothelial cells exposed to hypoxia
Ang II (show AGT Proteins) increases endothelial arginase activity/expression through a p38 MAPK (show MAPK14 Proteins)/ATF-2 (show ATF2 Proteins) pathway leading to reduced endothelial NO production
results indicate that arginase induction depends in part on epidermal growth factor (EGF (show EGF Proteins)) receptor (show EGFR Proteins) activity, and that EGFR (show EGFR Proteins) inhibitors may attenuate vascular remodeling without affecting nitric oxide release
high glucose (HG)-treated bovine coronary endothelial cells (BCECs) showed increased arginase activity and diminished NO production
this study shows that Ron (show MST1R Proteins) is expressed in a subpopulation of macrophages during chronic inflammation induced by obesity that exhibit a repair phenotype as determined by the expression of arginase 1
This study uncovers synergistic activation of Arg1 by retinoic acid and IL-4 (show IL4 Proteins) in M2 macrophages.
this study shows that group 2 innate lymphoid cells selectively express arginase 1 and that this is critical for their bioenergetics, proliferation and function
this study shows that c-Jun (show JUN Proteins) regulates the activation state of macrophages and promotes arthritis via differentially regulating cyclooxygenase-2 (show PTGS2 Proteins) and arginase-1 levels
deletion or TNF-mediated restriction of Arg1 unleashes the production of nitric oxide by NOS2, which is critical for pathogen control.
Data indicate that transfected mouse arginase-1 (Arg-I) promotes endothelial senescence and inflammatory responses through eNOS (show NOS3 Proteins)-uncoupling in human umbilical vein endothelial cells (HUVEC cells).
Arg1 is down-regulated during osteoclast differentiation and may negatively regulate osteoclast differentiation by regulating nitric oxide production.
Results show that arginase 1 is abundantly present in the bone and bone marrow stromal cells and reveal the role of its deregulation in diabetes-induced bone complications. * HFHS diet induced Arginase activity and expression in bone and bone marrow.
T Lymphocyte Inhibition by Tumor-Infiltrating Dendritic Cells Involves Ectonucleotidase CD39 (show ENTPD1 Proteins) but Not Arginase-1.
The immunosuppressive effect of a purified substance (ISF (show ATP6V0A2 Proteins)) in the culture medium of neonatal pig liver fragments was due to arginase activity that decreased arginine concentration in culture medium, not to another function of ISF (show ATP6V0A2 Proteins).
Results show that ischemia markedly potentiated the expression of arginase-1, and also induced the SOD2 (show SOD2 Proteins) in the wound tissue.
Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exist (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type I isoform encoded by this gene, is a cytosolic enzyme and expressed predominantly in the liver as a component of the urea cycle. Inherited deficiency of this enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia. Two transcript variants encoding different isoforms have been found for this gene.
, liver-type arginase
, type I arginase
, arginase 1
, arginase I
, arginase 1, liver
, AI type I arginase
, arginase, hepatic