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The arginase-polyamine signaling axis in immune cells: Implications for immune modulation and host-pathogen interactions. [PDF]
iScienceAziz S +3 more
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Enhancing Immunotherapy in Diffuse Large B-Cell Lymphoma: The Synergistic Potential of Metabolic Checkpoint Inhibitors and Immunomodulation. [PDF]
Onco Targets TherRajendraprasad MK, Riches JC.
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Intrahepatic Cholangiocarcinoma in Small-Duct Primary Sclerosing Cholangitis Associated With Crohn Disease: First Reported Case and Surveillance Implications. [PDF]
ACG Case Rep JAgrawal D, Kamath S, Reddy GN, Kodali S.
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Downregulation of arginase II and renal apoptosis by inorganic mercury: overexpression of arginase II reduces its apoptosisopenaire
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Structure of the murine arginase II gene
Mammalian Genome, 1998Mammals contain two genes encoding distinct isoforms of arginase (arginases I and II), both of which catalyze the conversion of arginine to ornithine and urea. However, their subcellular localization and tissue-specific patterns of expression are very different, indicating that they perform distinct physiologic roles.
O, Shi +3 more
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Archives of Toxicology, 2007
Inorganic mercury is a toxic metal that accumulates in the proximal tubules of the kidney, causing apoptosis. Arginase II is known to inhibit apoptosis, but its role in the renal apoptosis caused by inorganic mercury is poorly understood. In the present study, we examined the involvement of arginase II in inorganic mercury-dependent apoptosis. A single
Hironori, Kanda +8 more
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Inorganic mercury is a toxic metal that accumulates in the proximal tubules of the kidney, causing apoptosis. Arginase II is known to inhibit apoptosis, but its role in the renal apoptosis caused by inorganic mercury is poorly understood. In the present study, we examined the involvement of arginase II in inorganic mercury-dependent apoptosis. A single
Hironori, Kanda +8 more
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Expression, Purification, and Characterization of Human Type II Arginase
Archives of Biochemistry and Biophysics, 2001Human type II arginase, which is extrahepatic and mitochondrial in location, catalyzes the hydrolysis of arginine to form ornithine and urea. While type I arginases function in the net production of urea for excretion of excess nitrogen, type II arginases are believed to function primarily in the net production of ornithine, a precursor of polyamines ...
D M, Colleluori, S M, Morris, D E, Ash
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Adaptations of amphibian arginase—II. Response to temperature
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1973Abstract 1. 1. The effect of temperature on the kinetic properties (Michaelis constant and maximum velocity) and specific activity of Rana pipiens liver and kidney arginase and purified bovine arginase was studied. 2. 2. Winter R. pipiens were found to have lower kidney and liver arginase Michaelis constants than summer R.
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Arginases I and II: do their functions overlap?
Molecular Genetics and Metabolism, 2004Arginase, often perceived solely as the last of the now six enzymes of the urea cycle, exists in two forms and has a broad tissue distribution. A cytosolic form, AI, is highly expressed in the liver and is thought to be primarily involved in ureagenesis.
Stephen D, Cederbaum +5 more
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Classical and Slow-Binding Inhibitors of Human Type II Arginase
Biochemistry, 2001Arginases catalyze the hydrolysis of L-arginine to yield L-ornithine and urea. Recent studies indicate that arginases, both the type I and type II isozymes, participate in the regulation of nitric oxide production by modulating the availability of arginine for nitric oxide synthase.
D M, Colleluori, D E, Ash
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