PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “ARGINASE”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 559 records · Page 31Linked to original sources
PubMed2001

Expression of arginase isozymes in mouse brain.

The two forms of arginase (AI and AII) in man, identical in enzymatic function, are encoded in separate genes and are expressed differentially in various tissues. AI is expressed predominantly in the liver cytosol and is thought to function primarily to detoxify ammonia as part of the urea cycle. AII, in contrast, is predominantly mitochondrial, is more widely expressed, and is thought to function primarily to produce ornithine. Ornithine is a precursor in the synthesis of proline, glutamate, and polyamines. This study was undertaken to explore the cellular and regional distribution of AI and AII expression in brain using in situ hybridization and immunohistochemistry. AI and AII were detected only in neurons and not in glial cells. AI presented stronger expression than AII, but AII was generally coexpressed with AI in most cells studied. Expression was particularly high in the cerebral cortex, cerebellum, pons, medulla, and spinal cord neurons. Glutamic acid decarboxylase 65 and glutamic acid decarboxylase 67, postulated to be related to the risk of glutamate excitotoxic and/or gamma-aminobutyric acid inhibitoxic injury, were similarly ubiquitous in their expression and generally paralleled arginase expression patterns, especially in cerebral cortex, hippocampus, cerebellum, pons, medulla, and spinal cord. This study showed that AI is expressed in the mouse brain, and more strongly than AII, and sheds light on the anatomic basis for the arginine-->ornithine-->glutamate-->GABA pathway.

Animals↗
PubMed2002

Synthesis and evaluation of alternative substrates for arginase.

Two novel carboxyl-containing arginase substrates, 4-guanidino-3-nitrobenzoic acid and 4-guanidino-2-nitrophenylacetic acid, have been synthesized and found to give enhanced catalysis and dramatically lower K(m) values relative to 1-nitro-3-guanidinobenzene, a substrate designed for use in a chromophoric arginase assay. To more efficiently mimic the natural substrate, a series of sulfur analogs of L-arginine were synthesized and kinetically characterized. The parent compound, L-thioarginine, with the bridging guanidinium nitrogen of L-arginine replaced with sulfur, functions as efficiently as the natural substrate. The desamino analog shows extremely low turnover, while the k(cat) of the descarboxy analog is only 75-fold lower than that of arginine. These results suggest that the bridging nitrogen of L-arginine is not important for either substrate binding or catalysis, while the alpha-carboxyl group facilitates substrate binding, and the alpha-amino group is necessary for efficient catalysis. Isothiourea homologs previously reported to be nitric oxide synthase inhibitors have been found to undergo a rapid non-enzymatic rearrangement to a species that is probably the true inhibitor.

Animals↗
PubMed1986

Increased manganese content and reduced arginase activity in erythrocytes of a patient with prolidase deficiency (iminodipeptiduria).

Manganese was measured in blood of a patient with prolidase deficiency by neutron activation analysis. The manganese content of packed blood cells was 48.9 ng/g wet weight (controls 18.4 +/- 4.3 ng/g wet weight). It was proportionately increased in whole blood, whereas the serum manganese concentration was unchanged. The erythrocyte arginase activity was reduced to 46% of the mean control value. The reduced activities of two manganese-dependent enzymes, prolidase and arginase in erythrocytes in combination with an increased manganese content cannot be explained at the moment and leads to the speculation that manganese is inaccessible for enzyme activation.

Adult↗
PubMed1975

[Control activities and regulation by the glucocorticoids of three urea-cycle enzymes in rat foetal liver: argininosuccinate synthetase, argininosuccinase and arginase (author's transl)].

The activity of three urea-cycle enzymes, argininosuccinate synthetase, argininosuccinase and arginase have been studied in the foetal and new-born liver of rats. The activity increases with regularity between 17.5 days of pregnancy and birth in control foetuses. The lack of corticosteroid from 18.5 days of pregnancy decreases the activity of argininosuccinate synthetase. After administration of cortisol (hydrocortisone), to these 18.5 day-old foetuses lacking of corticosteroids, both activities of argininosuccinate synthetase and arginase are enhanced.

Adrenal Glands↗
PubMed1999

Nitric oxide biosynthesis, nitric oxide synthase inhibitors and arginase competition for L-arginine utilization.

Nitric oxide (NO) is a recently discovered mediator produced by mammalian cells. It plays a key role in neurotransmission, control of blood pressure, and cellular defense mechanisms. Nitric oxide synthases (NOSs) catalyze the oxidation of L-arginine to NO and L-citrulline. NOSs are unique enzymes in that they possess on the same polypeptidic chain a reductase domain and an oxygenase domain closely related to cytochrome P450s. NO and superoxide formation as well as NOS stability are finely regulated by Ca2+/calmodulin interactions, by the cofactor tetrahydrobiopterin, and by substrate availability. Strong interactions between the L-arginine-metabolizing enzymes are clearly demonstrated by competition between NOSs and arginases for L-arginine utilization, and by potent inhibition of arginase activity by N(omega)-hydroxy-L-arginine, an intermediate in the L-arginine to NO pathway.

Animals↗
PubMed2006

The role of L-arginine in toxic liver failure: interrelation of arginase, polyamine catabolic enzymes and nitric oxide synthase.

The existing interrelation in metabolic pathways of L-arginine to polyamines, nitric oxide (NO) and urea synthesis could be affected in sepsis, inflammation, intoxication and other conditions. The role of polyamines and NO in the toxic effect of mercury chloride on rat liver function was studied. Administration of mercury chloride for 24 h led to significantly elevated plasma activities of Alanine transaminase (ALT) and Aspartate transaminase (AST). Malondyaldehyde (MDA) levels were unaffected (p > 0.05) and arginase activity was significantly decreased (p < 0.05) while nitrate/nitrite production was significantly elevated (p < 0.001) in liver tissue. Polyamine oxidase (PAO) and diamine oxidase (DAO) activities, enzymes involved in catabolism of polyamines, were decreased. L-arginine supplementation to intoxicated rats potentiated the effect of mercury chloride on NO production and it was ineffective on arginase activity. Results obtained in this study show that mercury chloride-induced toxicity leads to abnormally high levels of ALT and AST that may indicate liver damage with the involvement of polyamine catabolic enzymes and NO.

Amine Oxidase (Copper-Containing)↗
PubMed1975

Purine and pyrimidine inhibitors of arginase.

1. Adenosine, inosine, adenine and uric acid are competitive inhibitors and cytidine and cytosine noncompetitive inhibitors of bovine liver arginase (L-arginine amidinohydrolase, EC 3.5.3.1). 2. The affinity of the enzyme for these inhibitors was 10--100 times as great as for substrate in terms of Ki versus Km. 3. These nucleic acid metabolites may thus function in vivo to regulate the urea cycle. 4. Several naturally occuring competitive and noncompetitive inhibitors of arginase of unknown structure have been isolated from plant and animal tissue. From their properties and methods of isolation, they may be the purines and pyrimidines herein described. 5. These purines and pyrimidines have no effect on tryptic hydrolysis.

Animals↗
PubMed1977

Immobilised monomers of human liver arginase.

Human liver arginase (L-arginine amidinohydrolase, EC 3.5.3.1) was immobilised by attachment to nylon with glutaraldehyde as a crosslinking agent. Incubation of the immobilised tetrameric enzyme with EDTA followed by dialysis resulted in the dissociation of the enzyme into inactive matrix-bound and solubilised subunits. Both species recovered enzymatic activity after incubation with Mn2+, and the activity of the reactivated matrix-bound subunits was nearly 25% of that shown by the enzyme initially attached to the support in the tetrameric form. When the reactivated bound subunits were incubated with soluble subunits in the presence of Mn2+, they 'picked-up' from the solution an amount of protein and enzymatic activity almost identical to that initially lost by the immobilised tetramer after the dissociating treatment with EDTA. This occurred only in the presence of Mn2+. It is suggested that the reactivation of the subunits of arginase involves the initial formation of an active monomer, which then acquires a conformation that favours a reassociation to the tetrameric state.

Arginase↗
PubMed1985

A new enzyme-coupled spectrophotometric method for the determination of arginase activity.

A spectrophotometric method for the determination of arginase (EC 3.5.3.1) is presented. Arginase is coupled to urease and glutamate dehydrogenase and the decrease in absorbance at 340 nm due to the oxidation of NADPH is followed. The method is rapid, is sensitive, is economical and permits continuous monitoring. The initial velocities were directly proportional to the enzyme concentrations between 0.06 and 0.30 units per 0.5 ml. The Lineweaver-Burk plot yielded positive allosteric behavior for the tetrameric enzyme. The K' and the Hill coefficient, n, calculated from Hill plot were found to be 4.7 mM and 1.26 (r = 1.00), respectively. These values are in good agreement with the literature.

Arginase↗
PubMed1982

Measurement of arginine transport in human erythrocytes using their intrinsic arginase activity: implications for the treatment of familial hyperargininemia.

A procedure making use of the intracellular arginase activity has been developed for measuring the transport of arginine across the human erythrocyte membrane. (1) The arginine translocation is carrier mediated with simple Michaelis-Menten kinetics, showing one high affinity, low capacity transport system characterized by a half saturation constant KT of 0.177 +/- 0.036 mmol/1, and a maximum velocity VT of 0.332 +/- 0.068 mumol X h-1 X ml-1 cells. (2) Competition experiments with lysine, ornithine and leucine indicated that the arginine transport system in specific for dibasic amino acids. (3) The value calculated for the intracellular arginine concentration agreed well with the values obtained by independent methods. (4) The low arginine transport rate of human erythrocytes can explain the failure to lower the hyperargininemia in familial hyperargininemia by blood transfusion with normal arginase-containing erythrocytes.

Arginase↗
PubMed1992

A novel colorimetric method for assaying arginase activity.

Arginase catalyzes the conversion of arginine to urea and ornithine in the liver of ureotelic animals. Higher activity of this enzyme is found in tumors as well as in the sera of patients with hepatic diseases. We have developed a simple colorimetric method for its determination. This is based on the determination of residual arginine, after its conversion with p-nitrophenyl glyoxal (PNPG) at pH 9.0 in the presence of sodium ascorbate. The reaction product obeys Beer's law in the range of 0.01-0.20 mmol/L arginine with an arginine-equivalent molar extinction coefficient of 0.65 x 10(4) M-1 cm-1. The decrease in absorbance in the presence of arginase correlates with the enzyme activity. Color development as well as termination of enzyme activity is achieved by addition of a single reagent, thereby obviating the use of many chemicals necessary in other methods. The sensitivity of this method is equivalent to those of currently available procedures but has the added advantages of greater convenience.

Arginase↗
PubMed1982

The differential contribution of arginase and transamidinase to ornithine biosynthesis in two achromic human melanoma cell lines.

Cellular ornithine biosynthesis could be expected to play a significant role in putrescine formation and hence in growth. Two enzymes are involved in ornithine biosynthesis: arginase and transamidinase. These enzyme activities were studied in two human melanoma cell lines differing in their Km of diamine oxidase for putrescine and in their tumorigenicity in nude mice. Arginase activity accounts for the majority of ornithine formed in the highly tumorigenic cell line, while the majority of ornithine is derived from transamidinase action in the poorly tumorigenic cell line, with concomitant formation of methyl guanidine, a potent inhibitor of diamine oxidase.

Amidinotransferases↗
PubMed1983

Arginase, ornithine decarboxylase and S-adenosylmethionine decarboxylase in chicken brain and retina.

Arginase, ornithine decarboxylase and S-adenosylmethionine decarboxylase are active in both retina and brain. Activity is higher in cerebellum than in the cerebral hemispheres and optical lobes. Arginase and ornithine decarboxylase are very active in the retina of very young chicks, while S-adenosylmethionine decarboxylase is poorly active. By contrast, S-adenosylmethionine decarboxylase is much more active in brain. The pattern of activity during development is different; only ornithine decarboxylase is very active during embryonal life; S-adenosylmethionine decarboxylase, at all events in brain, is more active in adult life. Ornithine decarboxylase is inhibited in vitro by alpha-difluoromethylornithine, but not in vivo. Diaminopropane inhibits brain ornithine decarboxylase, but does not induce an ornithine decarboxylase-antizyme. Methylglyoxal bis(guanylhydrazone) promotes an increase of S-adenosylmethionine decarboxylase activity in both the brain and the retina in vivo.

Adenosylmethionine Decarboxylase↗
PubMed1992

Possible involvement of manganese in the catalytic mechanism of bovine liver arginase.

1. Bovine liver arginase followed Michaelis-Menten kinetics in the pH range of 4.5-9.0. The variation of vi with pH implied that a basic group (pKa 8.7) functions at the catalytic site. 2. Treatment of the enzyme with N-ethylmaleimide showed that there are no critical sulfhydryl groups on the enzyme. 3. The less selective reagent, 3-bromopyruvate, caused biphasic inactivation which was unaffected by the presence of ornithine. 4. The data pointed against critical involvement of active site amino acid side chains in the catalytic sequence in arginase. 5. The observed pH-rate profile may reflect ionization of metal-bound water.

Animals↗
PubMed1994

Kinetics of manganese reconstitution and thiol group exposition in dialyzed rat mammary gland arginase.

1. Rat mammary gland arginase is a metallo-enzyme dependent on Mn2+, which can be only partially substituted by Cd2+. 2. Reconstitution of the activity of dialyzed arginase by manganese is a two-phase process; the second phase is independent of the cation concentration, with a half-time recovery (t1/2) of 10.77 min. 3. The apparent Km for Mn2+ is 280 microM and 10.5 microM for enzyme dialyzed for 24 and 72 hr, respectively. 4. Treatment with 5 mM EDTA at pH 6 totally inhibits enzyme activity, which is reconstituted by Mn2+. 5. Results obtained with iodoacetamide treatment suggest the existence of sulphydryl groups accessible only when the enzyme is dialyzed.

Animals↗
PubMed1992

Crystallization and oligomeric structure of rat liver arginase.

Rat liver arginase, a manganese-metalloenzyme, has been crystallized from polyethylene glycol 8000 in N,N-bis(2-hydroxyethyl)glycine (Bicine) buffer at pH 8.5. Crystals form as either cubes or pyramids and belong to space group P3(1) (or P3(2)) with hexagonal unit cell dimensions a = b = 88.9 A, c = 114.8 A, or a = b = 88.5 A, c = 104.5 A; the variation along the c axis does not correlate with the external crystal morphology of cube or pyramid-shaped. X-ray diffraction data are measured to a limiting resolution of 2.4 A. Given the volume constraints of the unit cell it is likely that rat liver arginase is a trimer, with three 35,000 Da monomers in the asymmetric unit. This resolves a persistent ambiguity regarding the oligomeric structure of this enzyme.

Animals↗
PubMed1990

Liver arginase activity and urinary nitrogen products profile in adult Bufo arenarum under different protein intake.

The effect of different levels of diet protein on adult Bufo arenarum liver arginase activity and protein content, plasma urea and urinary profile of nitrogen waste products was estimated. Animals kept under environmental constant conditions were submitted to a nutritional standardization period being fed beef meat daily during four days. Then animals were distributed in three groups: Group 0 (control), that was sampled at the end of the standardization period; Group 1, that was starved for 18 days and Group 2, that was fed daily for 18 days and then sampled. With respect to controls, liver arginase specific activity was significantly lower in starving toads (Group 1); liver protein content was elevated in fasted animals (Group 1) and plasma urea concentration increased in the intensive feeding group (Group 2). Urinary nitrogen end products in animals from both control and experimental groups showed no changes either in their absolute values or in their partition percentage rates.

Animals↗