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Seminal arginase activity in infertility.

Arginase (Arg) activity in seminal plasma and sperm cells from infertile men and healthy fertile donors was measured. There were no statistically meaningful differences in seminal plasma Arg activity between the two groups whereas sperm cells from oligospermic infertile men had a higher Arg activity compared with the controls. Some important correlations were established between sperm count and Arg activity (negative values) and sperm motility and Arg activity (positive values) in both sperm cells and plasma samples from infertile men. Results suggest that the arginine-nitric oxide pathway within sperm cells from oligospermic infertile men is disturbed by enhanced Arg activity. We think that this may play a part in sperm dysfunction and male infertility.

Adult↗

Localization and differential expression of arginase II in the kidney of male and female mice.

Arginase II (AII) has been almost exclusively studied in male mammalian kidneys. Our investigations were conducted to localize AII gene expression in the female mouse kidney, and to analyze the differential expression of AII gene at the transcriptional and translational levels in the kidneys of female and male mice. Total RNAs and soluble proteins extracted from renal zones and whole kidneys were analyzed by Northern and Western blots, respectively. Mitochondrial and cytosolic proteins were analyzed by Western blot. L-[guanidino-14C]arginine hydrolysis by AII was detected in microdissected tubules and the 14CO2 released from [14C]urea hydrolysis was quantified. The results of these experiments showed that: (1) both AII mRNA and protein were highly expressed in the deep cortex and the outer stripe of the outer medulla, (2) urea was produced mainly in the proximal straight tubules (PST), (3) the 38-kDa AII protein was more abundant in the mitochondria than the cytosol, and (4) the renal content of AII mRNA and protein was about three-fold higher in female than in male mice. In conclusion, in both genders, AII gene expression is restricted to the PST and localized into mitochondria. AII gene is differentially expressed in the kidney of female and male mice since higher levels of AII mRNA, protein and activity were observed in the kidneys of the former than those of the latter. Renal AII gene expression was gender-dependent in mice but not in rats. Finally, in the PST of females, L-arginine-derived ornithine may be a precursor for the renal production of L -glutamate and L-glutamine because high levels of AII, ornithine aminotransferase and glutamine synthetase are expressed in this nephron segment.

Animals↗

Integration of the multiple controls regulating the expression of the arginase gene CAR1 of Saccharomyces cerevisiae in response to differentnitrogen signals: role of Gln3p, ArgRp-Mcm1p, and Ume6p.

Expression of the catabolic gene encoding arginase in Saccharomyces cerevisiae, CAR1, is controlled by multiple nitrogen signals, such as the presence of the inducer, arginine, and the nature and amount of the nitrogen source. The present study has determined or confirmed the identity of the proteins involved in these different controls, as well as their targets in the CAR1 promoter. We show that Gln3p activates CAR1 expression through the GATAA sequences in the absence of an optimal nitrogen source, such as ammonia, glutamine or asparagine. Ume6p, which also controls the expression of early meiotic genes, represses CAR1 expression through a sequence called URS, as a function of nitrogen availability. Thus, the responses to the quality of the nitrogen source and to nitrogen starvation are achieved through different cis- and trans-regulatory elements. At least one of the multiple Rap1p and Abf1p binding sites is required for the basal transcription of the gene. The UAS(arg), containing the previously defined "arginine boxes" is the region that responds to the inducer through the action of the ArgRp-Mcm1p proteins, and its deletion alone significantly affects growth on arginine as sole nitrogen source. The functional UAS(arg) is about 60 nucleotides long, and contains two sequences homologous to the binding site for MADS-box proteins, to which ArgRIp and Mcm1p belong. No obvious palindromic sequence similar to the binding site of Gal4p, Ppr1p or Put3p is present in the UAS(arg), although ArgRIIp contains a Zn(II)2Cys6 motif. Interestingly, we have found that induction of CAR1 expression by arginine in the presence of an optimal nitrogen source is counteracted by Gln3p, independently of its action at the GATAA sequences.

Arginase↗

Physicochemical and kinetic properties of beef liver argininosuccinase. Studies in the presence and absence of arginase.

Physicochemical properties of beef liver argininosuccinase (EC 4.3.2.1) are reported, which show that the operational kinetic unit at pH 7.5 in the concentration range used for enzymic assays is of molecular weight 203 000. This information is utilized in the interpretation of initial velocity studies of the forward reaction (argininosuccinate as initial substrate) where, in an Eadie-Hofstee plot, deviation from linearity is observed. These results are examined with the aid of a rate equation, formulated as a ratio of two polynomials in initial substrate concentration, which provides a quantitative description of the system in terms of cooperative effects. The kinetics of the reverse reaction catalysed by argininosuccinase were also investigated by performing experiments of different design in which the rate of change of fumarate concentration was monitored as a function of time. Comparison of these results with numerical solutions obtained by integrating the differential rate equation reflecting the reversible reaction permitted estimation of the relevant kinetic parameters. One of the latter experiments involved a coupled assay with argininosuccinase and arginase as the consecutive catalysts and indicated that no chemical interaction occurred between the enzymes. This observation, which is relevant to consideration of fluxes in the urea cycle, was supported by both sedimentation velocity studies on mixtures of the enzymes and by other kinetic analysis.

Animals↗

A simplified procedure for the estimation of arginine in plasma and urine using arginase.

To ensure reliable arginine estimation, other compounds giving positive results with Chinard's ninhydrin reaction were removed by simple ion-exchange chromatography. Eluted arginine was converted to ornithine by arginase and estimated using Chinard's ninhydrin reaction. Plasma arginine level in adults was in the range 56--98 mumol/l, and urine arginine in the range 0.58--1.77 mg/day.

Adult↗

L-arginine depletion by arginase reduces nitric oxide production in endotoxic shock: an electron paramagnetic resonance study.

Nitric oxide (NO) synthesis was measured in the liver, lung, spleen and kidney of lipopolysaccharide-treated male rats using the nitric oxide spin trap, iron (II)-diethyldithiocarbamate (FeDETC2). Nitric oxide formation in vivo was determined by the increase in intensity of the characteristic triplet hyperfine EPR spectrum of [NO-FeDETC2]. Intravenous bovine liver arginase, at a dose which completely depleted circulating arginine, significantly reduced the formation of nitric oxide in these tissues. The general decrease in NO levels was confirmed by the decrease in plasma nitrite levels. These results directly demonstrate that NO formation in endotoxic shock depends on extracellular arginine; depletion of plasma arginine may be a useful therapeutic strategy.

Animals↗

Differences in the arginase activity produced by resident and stimulated murine and rat peritoneal macrophages.

1. Murine macrophages showed a considerably higher in vitro arginase production in short time cultures than rat peritoneal cells. 2. The in vivo stimulation with casein or thioglycollate resulted in an enhanced in vitro enzyme production in mice. 3. The adherence is not the condition of the enzyme production. 4. The difference between the two species cannot be explained by the lack of bivalent ions, the absence of energy supply, proteolysis, the low number of macrophages or by the different cell types of the peritoneal exudate of mouse and rat. 5. The lysozyme production of murine and rat peritoneal macrophages was also investigated and no difference was observed between the two species.

Animals↗

Determination of arginase activity in macrophages: a micromethod.

We propose a modification of Schimke's method for urea determination as a valuable micromethod for measuring arginase in activated macrophages. The method exhibits the following advantages: (a) it uses small amounts of samples (approximately 25,000 macrophages per assay); (b) it does not interfere with other related metabolites that are also present in the activated macrophage such as citrulline or arginine; (c) saturating concentrations of the substrate arginine can be used; and (d) it is much more sensitive than Schimke's method and can detect small amounts of urea, in the order of 0.02 mumol.

Animals↗

A specific arginase-based assay for L-canavanine in leguminous plants.

A convenient method for the analysis of free L-canavanine in leguminous plants is described. Canavanine was specifically hydrolyzed to canaline and urea by the enzyme arginase (EC 3.5.3.1). The resulting amino-oxy functions of canaline were measured based on their ability to bleach the yellow colour of pyridoxal 5'-phosphate. Canavanine in the seeds of Canavalia ensiformis was determined with this method.

Arginase↗

T cell-macrophage interaction in arginase-mediated resistance to herpes simplex virus.

Peritoneal macrophages activated by-products derived from a herpes simplex virus-specific helper T cell clone were used to investigate intrinsic and extrinsic resistance mechanisms to herpes simplex virus type 1 infection in vitro. T cell-activated macrophages produced fewer infective centres, indicating enhanced intrinsic resistance, and markedly reduced the growth of virus in a permissive cell line. The reduction in virus growth correlated with the depletion of arginine in the support medium, presumably resulting from increased arginase production by activated macrophages. The significance of these findings for antiviral immunity in vivo is discussed.

Animals↗

Antitumor effect and toxicity of two new active-site-directed irreversible ornithine decarboxylase and extrahepatic arginase inhibitors.

The irreversible ornithine decarboxylase and extrahepatic arginase inhibitors (+)-S-2-amino-5-iodoacetamidopentanoic acid (2-AIPA) and (+)-S-2-amino-6-iodoacetamidohexanoic acid (2-AIHA) were evaluated. The LD50 tests were made in rats and mice using both compounds. Rats and mice were treated with either 2-AIPA or 2-AIHA i.p. for a period of 180 days. The treated animals showed a decrease of total serum proteins and increased ALT and AST levels. CK was also modified but inversely related to dose. Protection tests were carried out using L5178Y mouse lymphosarcoma. The mean survival time for each treated group was calculated and the percentage T/C was determined. For 2-AIPA it was 170 and for 2-AIHA it was 210 at 15 mg/kg.

Amino Acids↗

Alteration in IL-1 and arginase activity of tumor-associated macrophages: a role in the promotion of tumor growth.

The present investigations were undertaken to study whether the macrophages associated with Dalton's lymphoma (DLAM), a spontaneous T-cell lymphoma, are modulated for the secretion of tumor growth-promoting factors in ascites. The DL ascitic fluid (DLAF) and the culture supernatants of DLAM harvested from mid and late tumor-bearing stages, but not early tumor-bearing stage, enhanced the proliferation of DL cells in vitro. These observations indicate that DLAF contains certain DL growth-promoting substances and at least some of them are secreted by DLAM. The DLAM obtained from mid and late tumor-bearing stages showed enhanced IL-1 production and arginase activity, with a concomitant decline in the RNI production, which could be implicated in the DLAM-mediated promotion of tumor growth.

Animals↗

Hepatic arginase activity in intra- and extrauterine larvae of the ovoviviparous salamander. Salamandra salamandra (L.) (Amphibia, Urodela).

The hepatic arginase activity of Salamandra salamandra was determined at three different stages of intra- and extrauterine larval development and at fully metamorphosed juveniles. The highest enzymatic activity was found in intrauterine larvae in November, the lowest in intrauterine larvae in June of the following year. These data can be correlated with the ureotelism of intrauterine larvae previously described and are discussed with respect to the metabolism of larval and juvenile fire salamanders.

Animals↗

Subcellular localization and kinetic properties of arginase from the liver of Genypterus maculatus.

1. From the liver of the teleost fish Genypterus maculatus, a partially purified preparation of arginase was obtained and characterized. 2. The Km value for arginine was found to be 9.1 mM at pH 7.5 and 11.5 mM at the optimum pH of 9.5. At both pH values, competitive inhibition was caused by ornithine and lysine, whereas proline, leucine, valine and isoleucine caused a non-competitive inhibitory effect. Branched chain amino acids were more inhibitory than proline. 3. The enzyme was found localized in the mitochondrial matrix of the liver of Genypterus maculatus. It is suggested that this localization would be of importance in the use of arginine as an energy source.

Animals↗

Possible role of the control of arginase and methionine adenosyl transferase in the transport processes of endogenous formaldehyde and in hypermethylation.

The authors believe the normal formaldehyde equilibrium in the organism to be governed by a biological control mechanism, which is thought to be closely connected to L - arginine and - indirectly - to the arginase enzyme. Arginine reacts with formaldehyde in a spontaneous equilibrium reaction yielding methylol - derivatives thus mobilizing formaldehyde. The methylol - derivatives of L - arginine were found in serum and urine. The authors assume the methylol - derivatives of L - arginine to have an inhibiting effect on cell - proliferation.

Animals↗

Isolation and characterization of the arginase-encoding gene (arg) from Coccidioides immitis.

The arginase (ARG)-encoding gene (arg) of Coccidioides immitis, a human fungal pathogen, was cloned and sequenced. Both the genomic and cDNA sequences are provided. The transcription start point and poly(A) sites were confirmed. The arg gene, which was located on chromosome II of C. immitis by Southern hybridization, is a single-copy gene with two introns and a 966-bp ORF which translates a 322-aa protein of 35.1 kDa. The deduced ARG protein showed 44% identity and 68% similarity to the Saccharomyces cerevisiae ARG.

Amino Acid Sequence↗

Five forms of arginase in human tissues.

Five forms of arginase, A1, A2, A3, A4, and A5, were found to be present in human tissues. The molecular weight of all these forms is the same, 120,000, but they differ in the behavior on DEAE- and CM-cellulose, electrophoretic mobility, isoelectric point, and immunochemical properties. Forms A1 from kidney and A5 from liver show complete immunological incompatibility, whereas forms A2 from liver, A3 from salivary gland, and A4 from kidney exhibit partial incompatibility with respect to each other and to forms A1 and A5.

Adult↗

Advantage of serum type-I arginase and ornithine carbamoyltransferase in the evaluation of acute and chronic liver damage induced by thioacetamide in rats.

BACKGROUND: We evaluated the usefulness of serum type-I arginase (ARG) and ornithine carbamoyltransferase (OCT) in thioacetamide (TAA)-induced acute and chronic liver injury in rats. METHODS: In an acute injury model, we measured the time-courses of serum concentrations of ARG and OCT using ELISA, together with AST and ALT using biochemical enzymatic assays after a single administration of TAA (200 mg/kg, i.p.). In the chronic model, TAA was repeatedly administered (20 mg/kg/day, p.o.) for 16 weeks and serum concentrations of the enzymes were evaluated. RESULTS: In the acute model, the concentrations of the enzymes were increased in a similar manner, peaking 24 h after the administration, and ARG showed the earliest and greatest increase among the enzymes tested. In the chronic model, the serum concentration of OCT was significantly increased only 1 week after oral treatment, while concentrations of the other enzymes were increased at 8 to 12 weeks. In the histological analysis, TAA treatment damaged hepatocytes in both the acute and chronic model. CONCLUSIONS: These results clearly show the usefulness of ARG and OCT for the evaluation of acute and chronic liver injury, respectively.

Alanine Transaminase↗