arginase inhibition increases hepatic nitric oxide in HepG2 cells, and reverses the elevated mRNA expression of hepatic genes in lipid metabolism. The expression of phosphorylated 5' adenosine monophosphate-activated protein kinase alpha is increased by arginase inhibition in HepG2 cells
arginase inhibition increases hepatic nitric oxide in high fat diet-fed mice and reverses the elevated mRNA expression of hepatic genes in lipid metabolism. The expression of phosphorylated 5' adenosine monophosphate-activated protein kinase alpha is increased by arginase inhibition in the mouse liver. Arginase inhibition prevents diet-induced obesity and reduces liver weight
the disulfide bond is important for the overall stability and folding of the protein. Mutant proteins lacking the disulfide bond start to unfold at lower temperature than the wild-type. In the mutant proteins, the Tm of the holoenzyme is 4°C higher than that of the apoenzyme indicating that in the absence of the disulfide bond the metal ions have relatively larger role in the stability of the mutant proteins compared to the wild-type
initiates de novo polyamine biosynthesis by catalyzing the hydrolysis of L-arginine to generate L-ornithine and urea. The product L-ornithine subsequently undergoes decarboxylation to yield putrescine, which in turn is utilized for spermidine biosynthesis
the enzyme catalyses the catabolism of l-arginine to l-ornithine and urea. First committed step in polyamine biosynthesis. In pathogenic organisms, arginase plays a crucial role in depleting host L-arginine, a substrate for nitric oxide synthase that participates in protective immunity, thereby evading host immune response
the enzyme produces urea and ornithine as part of polyamine biosynthetic pathway, essential for the parasite replication and establishment of the infection
ARG1 and ARG2 are enzymatically active in hormone-sensitive and hormone-refractory prostate cancer cell lines and their decreased expression by siRNA results in reduced overall arginase activity and L-arginine metabolism. The decreased ARG1 and ARG2 expression also translates with diminished LNCaP cells cell growth and increased peripheral blood mononuclear cell activation following exposure to LNCaP cells conditioned media. Interleukin-8 is also upregulated following androgen stimulation and it directly increases the expression of ARG1 and ARG2 in the absence of androgens
coinhibitory and costimulatory molecules PD-1 and CTLA-4 on the Gr-1+CD11b+ myeloid-derived suppression cells regulate the activity and expression of arginase I. The blockage and silencing of PD-1, CTLA-4 or both PD-1 and CTLA4 molecules can significantly reduce arginase I activity and expression induced with tumor-associated factor. Similar results are also observed while their ligands B7-H1 and/or CD80 are blocked or silenced. CD80 deficiency also decreases the arginase I expression and activity. Antibody blockade or silencing of PD-1, CTLA-4 or both reduces the suppressive potential of PD-1+CTLA-4+ myeloid-derived suppression cells. Blockade of PD-1, CTLA-4 or both also slows tumor growth and improves the survival rate of tumor-bearing mice
comparison of the infectivity of arg- and wild-type Plasmodium berghei by inoculation of mice using sporozoites dissected from mosquito salivary glands shows a significant reduction in infectivity in the arg- strain 40 h postinfection
in arginase I-deficient bone marrow chimeric mice, following transfer of arginase I-deficient bone marrow into irradiated recipient mice, arginase I expression is not required for hematopoietic reconstitution and baseline immunity. Arginase I deficiency in bone marrow-derived cells decreases allergen-induced lung arginase by 85.8%. Arginase II-deficient mice have increased lung arginase activity following allergen challenge to a similar level to wild type mice. Bone-marrow-derived arginase I is not required for allergen-elicited sensitization, recruitment of inflammatory cells in the lung, and proliferation of cells. Allergen-induced airway hyperresponsiveness and collagen deposition are similar in arginase-deficient and wild type mice. Arginase II-deficient mice respond similarly to their control wild type mice with allergen-induced inflammation, airway hyperresponsiveness, proliferation and collagen deposition