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PubMed2006

In vitro and in vivo complementation of the Helicobacter pylori arginase mutant using an intergenic chromosomal site.

BACKGROUND: Gene complementation strategies are important in validating the roles of genes in specific phenotypes. Complementation systems in Helicobacter pylori include shuttle vectors, which transform H. pylori at relatively low frequencies, and chromosomally based approaches. Chromosomal complementation strategies are susceptible to polar effects and disruption of other H. pylori genes, leading to unwanted pleiotropic effects. MATERIALS AND METHODS: A new complementation strategy was developed for H. pylori by utilizing a suicide plasmid vector that contains fragments of an H. pylori intergenic region (hp0203-hp0204), a chloramphenicol acetyltransferase cassette (cat), and a multiple-cloning site. Genes of interest could be cloned into the intergenic plasmid and the genes integrated into H. pylori by homologous recombination into the intergenic chromosomal region without disrupting any annotated H. pylori gene. The complementation system was validated using the gene encoding arginase (rocF). RESULTS: A rocF mutant unable to hydrolyze or consume l-arginine regained these functions by complementation with the wild-type rocF gene. Complemented strains also had restored arginase protein as determined by Western blot analysis. The complementation system could be successfully applied to multiple H. pylori strains. The intergenic region varied in length and sequence across 17 H. pylori strains, but the flanking-3' ends of the hp0203 and hp0204 coding regions were highly conserved. Inserting a cat cassette and wild-type rocF into the intergenic region did not alter the ability of strain SS1 to colonize mice. CONCLUSIONS: This complementation strategy should greatly facilitate genetic experiments in H. pylori.

Animals↗
PubMed2003

Disruption of the CAR1 gene encoding arginase enhances freeze tolerance of the commercial baker's yeast Saccharomyces cerevisiae.

The effect of intracellular charged amino acids on freeze tolerance in dough was determined by constructing homozygous diploid arginase-deficient mutants of commercial baker's yeast. An arginase mutant accumulated higher levels of arginine and/or glutamate and showed increased leavening ability during the frozen-dough baking process, suggesting that disruption of the CAR1 gene enhances freeze tolerance.

Arginase↗
PubMed1982

Inhibition of herpes simplex virus multiplication by activated macrophages: a role for arginase?

Proteose-peptone-activated mouse macrophages can prevent productive infection by herpes simplex virus in neighboring cells in vitro whether or not those cells belong to the same animal species. The effect does not require contact between the macrophages and the infected cells, may be prevented by adding extra arginine to the medium, and may be reversed when extra arginine is added 24 h after the macrophages. Arginase activity was found both intracellularly and released from the macrophages. The extracellular enzyme is quite stable; 64% activity was found after 48 h of incubation at 37 degrees C in tissue culture medium. No evidence was found that the inefficiency of virus replication in macrophages was due to self-starvation by arginase. As might be predicted macrophages can, by the same mechanism, limit productive infection by vaccinia virus.

Animals↗
PubMed1981

Arginase and kallikrein activities as biochemical indices of occupational exposure to lead.

In a group of 60 workers occupationally exposed to lead the blood and urine lead concentrations, haematocrit, ALA-D and arginase activities, and urinary 5-aminolaevulinic acid (ALA) and coproporphyrin concentrations, and kallikrein activity were determined. Correlation coefficients of -0.78 and 0.77 for Pb-B/ALA and Pb-B/arginase were found respectively for lead concentrations above 40 microgram/dl blood, and 0.83, 0.76, 0.74, and -0.64 for Pb-U/ALA, Pb-U/Cp-U, Pb-U/kallikrein, and Pb.U/kallikrein, respectively. It seems that the increase in serum arginase activity may be indicative of liver damage while the decrease in kallikrein activity may indicate kidney damage in workers exposed to lead.

Aminolevulinic Acid↗
PubMed2002

Role of glutamine and arginase in protection against ammonia-induced cell death in gastric epithelial cells.

Ammonia is a cytotoxic factor produced during Helicobacter pylori infection that may reduce the survival of surface epithelial cells. Here we examine whether ammonia kills cells and whether L-glutamine (L-Gln) protects against cell death by stimulating ammonia detoxification pathways. Cell viability and vacuolation were quantified in rat gastric epithelial (RGM1) cells incubated with ammonium chloride at pH 7.4 in the presence or absence of L-Gln. Incubation of RGM1 cells with ammonium chloride caused a dose-dependent increase in cell death and vacuolation, which were both inhibited by L-Gln. We show that RGM1 cells metabolize ammonia to urea via arginase, a process that is stimulated by L-Gln and results in reduced ammonia cytotoxicity. L-Gln also inhibits the uptake and facilitates the extrusion of ammonia from cells. Blockade of glutamine synthetase did not reduce the survival of RGM1 cells, demonstrating that the conversion of L-glutamate and ammonia to L-Gln is not involved in ammonia detoxification. Thus our data support a role for L-Gln and arginase in protection against ammonia-induced cell death in gastric epithelial cells.

Ammonia↗
PubMed1975

Effects of testosterone and prolactin on rat prostatic weight, 5alpha-reductase, and arginase.

Prostatic weights, 5alpha-reductase, and arginase activities were utilized as indexes for the effects of prolactin in short-term experiments in intact, hypophysectomized or castrated rats. Experiments were performed in which a dose-related response in the above parameters was obtained with testosterone administration in castrated mature and immature rats in order to evaluate the effects of simultaneously administered prolactin. This approach was necessitated by the failure of prolactin alone to affect the parameters listed in intact, castrated or hypophysectomized rats. It was shown that ovine prolactin may have an enhancing effect on the prostatic weight, 5alpha-reductase, and arginase activities, but that this effect is neither consistent nor striking when compared to that of testosterone.. Nevertheless, it is still possible that the long-term effects of prolactin, even if they are only of an enhancing quality, may play an important role in normal prostatic physiology and in abnormal states.

3-Oxo-5-alpha-Steroid 4-Dehydrogenase↗
PubMed2004

Arginase inhibition increases nitric oxide production in bovine pulmonary arterial endothelial cells.

Nitric oxide (NO) is produced by NO synthase (NOS) from L-arginine (L-Arg). Alternatively, L-Arg can be metabolized by arginase to produce L-ornithine and urea. Arginase (AR) exists in two isoforms, ARI and ARII. We hypothesized that inhibiting AR with L-valine (L-Val) would increase NO production in bovine pulmonary arterial endothelial cells (bPAEC). bPAEC were grown to confluence in either regular medium (EGM; control) or EGM with lipopolysaccharide and tumor necrosis factor-alpha (L/T) added. Treatment of bPAEC with L/T resulted in greater ARI protein expression and ARII mRNA expression than in control bPAEC. Addition of L-Val to the medium led to a concentration-dependent decrease in urea production and a concentration-dependent increase in NO production in both control and L/T-treated bPAEC. In a second set of experiments, control and L/T bPAEC were grown in EGM, EGM with 30 mM L-Val, EGM with 10 mM L-Arg, or EGM with both 10 mM L-Arg and 30 mM L-Val. In both control and L/T bPAEC, treatment with L-Val decreased urea production and increased NO production. Treatment with L-Arg increased both urea and NO production. The addition of the combination L-Arg and L-Val decreased urea production compared with the addition of L-Arg alone and increased NO production compared with L-Val alone. These data suggest that competition for intracellular L-Arg by AR may be involved in the regulation of NOS activity in control bPAEC and in response to L/T treatment.

Animals↗
PubMedDate not supplied

The influence of L-arginine on the regulation of epidermal arginase.

Topical preparations containing urea are firmly established in dermatological therapy and nursing care therapy. In addition, urea is frequently used as an inactive ingredient with disinfecting, keratoplastic and penetration-promoting action in topical preparations. Despite good tolerance and ensured action, particularly the irritating effect on erosive, exudative or strongly inflammatory skin restricts its application. Endogenic urea is synthesised from L-arginine by an extra-hepatic arginase in keratinocytes. This enzymatic reaction is subject to regulation by manganese ions and the intracellular L-arginine concentration. L-Arginine is predominantly transported into the cell by a membrane transport system that is dependent on the membrane potential. By incubating keratinocyte cultures in different concentrations of L-arginine and manganese chloride, it could be shown that the keratinocytic urea synthesis can be increased. In relevant concentrations, L-arginine and manganese chloride do not exhibit any proliferation-inhibiting action, do not trigger any apoptosis or necrosis, and are stable. An increase in the expression of arginase cannot be detected using L-arginine. The application of L-arginine alone or in combination with manganese chloride increases the endogenous intrakeratinocytic urea synthesis and thus offers an option for topical therapeutic application in cases of dry skin conditions.

Apoptosis↗
PubMed2006

Serum nitrite/nitrate and arginase levels in patients with allergic rhinitis.

Nitric oxide (NO) plays an important role in the regulation of upper respiratory function. Patients with untreated allergic rhinitis (AR) have an increased level of NO in the nasal cavity compared to normal individuals. We aimed to investigate serum levels of arginase and NO metabolites nitrite/nitrate in patients with AR during the symptomatic period. The patient and control groups consisted of 14 males and 12 females (mean age: 29, range: 20-40 years), and 10 males and 10 females (mean age: 27, range: 22-38 years), respectively. Nitrite/nitrate levels were 0.98 +/- 0.33 ng/ml in the patients with AR, and 0.78 +/- 0.26 ng/ml in the control group (p = 0.03). Arginase levels were 28.8 +/- 14.1 ng/ml in the patients with AR, and 20.8 +/- 13.5 ng/ml in the control group. The difference between the groups was statistically insignificant (p = 0.24). Our results support the view that NO plays an important role in the pathogenesis of AR, and NO metabolites may be used as a marker for monitoring the disease activity and therapy.

Adult↗
PubMed1989

Differential expression of the two human arginase genes in hyperargininemia. Enzymatic, pathologic, and molecular analysis.

Previous studies in our laboratory and others have demonstrated in humans and other mammals two isozymes of arginase (AI and AII) that differ both electrophoretically and antigenically. AI, a cytosolic protein found predominantly in liver and red blood cells, is believed to be chiefly responsible for ureagenesis and is the one missing in hyperargininemic patients. Much less is known about AII because it is present in far smaller amounts and localized in less accessible deep tissues, primarily kidney. We now report the application of enzymatic and immunologic methods to assess the independent expression and regulation of these two gene products in normal tissue extracts, two cultured cell lines, and multiple organ samples from a hyperargininemic patient who came to autopsy after an unusually severe clinical course characterized by rapidly progressive hepatic cirrhosis. AI was totally absent (less than 0.1%) in the patient's tissues, whereas marked enhancement of AII activity (four times normal) was seen in the kidney by immunoprecipitation and biochemical inhibition studies. Immunoprecipitation-competition and Western blot analysis failed to reveal presence of even an enzymatically inactive cross-reacting AI protein, whereas Southern blot analysis showed no evidence of a substantial deletion in the AI gene. Induction studies in cell lines that similarly express only the AII isozyme indicated that its activity could be enhanced severalfold by exposure to elevated arginine levels. Our findings suggest that the same induction mechanism may well be operative in hyperargininemic patients, and that the heightened AII activity may be responsible for the persistent ureagenesis seen in this disorder. These data lend further support to the existence of two separate arginase gene loci in humans, and raise possibilities for novel therapeutic approaches based on their independent manipulation.

Arginase↗
PubMed2003

Arginase: marker, effector, or candidate gene for asthma?

Microarray analysis of the expression profiles of lung tissue in two murine models of asthma revealed high levels of arginase I and arginase II activity, in association with IL-4 and IL-13 overexpression, suggesting that arginine pathways are critical in the pathogenesis of asthma.

Animals↗
PubMed1976

Glutamate dehydrogenase, alanine aminotransferase, thymidine kinase, and arginase in fetal and adult human and rat liver.

In fetal livers of both man and rat thymidine kinase activity was 12 times higher than in the adult, glutamate dehydrogenase and arginase were present at 20-50% of their adult values, whereas alanine aminotransferase activity was only an insignificant fraction of that in the adult. Although the developmental changes for the four enzymes were quantitatively similar in both species, qualitatively there were some significant differences. In adult human liver, glutamate dehydrogenase activity was distributed almost equally between the cytosol and particles; the concentration of only the soluble enzyme increased after birth. In rat liver, glutamate dehydrogenase remained exclusively a particulate enzyme. The soluble hepatic alanine aminotransferase activity rose in both species after birth (from less than 2 U/g to 41-57 U/g, respectively). Thymidine kinase was wholly soluble in the fetal livers; only in adult human liver was additional activity (at least 50% of the total) found in the particles. Arginase isozymes, identical and apparently the same single isozyme in fetal and adult rat liver, show an ontogenetic change in man. A shift from a single form, common to human fetal liver and fetal kidney, to at least two variants in adult human liver, indicates another complexity of the fully differentiated liver in man.

Adult↗
PubMed1980

Arginase and sucrase potential in the fission yeast Schizosaccharomyces pombe.

The induction potentials of 2 enzymes, sucrase and arginase, have been measured in asynchronous and synchronous cultures of the fission yeast Schizosaccharomyces pombe. The effect on potential of inhibiting DNA synthesis is asynchronous cultures has been studied using 2 temperature-sensitive dcd mutants, one blocked in DNA replication and the other blocked in mitosis. The results show that despite inhibition of DNA synthesis, sucrase and arginase potential both continue to increase exponentially for at least a generation of growth after shifting the cdc mutants from the permissive to the restrictive temperature. A second method of inhibiting DNA synthesis, using deoxyadenosine, has also been tested. Cells treated with deoxyadenosine stop the increase in potential for a short period. However, experiments carried out using a cdc mutant together with deoxyadenosine show that the block to the increase in potential is due to a side effect of the inhibitor. It appears that increase in potential is not dependent upon continued DNA replication, and that gene dosage does not control potential in the normal cell cycle. This conclusion is supported by measurements on mutants of different cell sizes. potential is proportional to size (protein content per cell is asynchronous culture) and not to DNA content. Although potential is not gene limited in normal cells, it does appear to be so in the abnormally large cells produced by a cdc block. If cdc mutants of different sizes are grown asynchronously, and DNA synthesis is inhibited by a shift to the restrictive temperature, there is no increase in potential. This critical ratio is different for the 2 enzymes, but for each enzyme it is similar in all the mutants tested. When large cells (produced by a mutant block for 4.5 h) are shifted down in temperature, there are synchronous rounds of DNA synthesis and division and also step doublings in potential. In synchronous cultures of wild type cells, both enzymes show a stepwise doubling of potential at 0.2 of a cycle after DNA replication. In synchronous cultures of cdc mutants blocked either in replication or in mitosis, the potential steps continue with the normal timing observed in wild type cells. This shows that the steps are not dependent on the events of the DNA-division cycle but are controlled by another mechanism. Attainment of a critical size might be part of this mechanism, but tests with size mutants argue against this.

Arginase↗
PubMed1975

Effect of estrogen administration on activities of testosterone 5alpha-reductase, alkaline phosphatase and arginase in the ventral and the dorsolateral prostates of rats.

Daily treatment with 5 or 500 mug of estradiol benzoate of male adult rats for 7 days did not change the activity of testosterone 5alpha-reductase in the ventral prostate, while the activity decreased slightly in the dorsolateral prostate. The activity of alkaline phosphatase was increased by 60% over the respective control in the ventral prostate from rats treated with the larger dose of estrogen, but the estrogen treatment did not affect the alkaline phosphatase activity in the dorsolateral prostate. On the contrary, the estrogen treatment evoked three-fold elevation in the arginase activity of the dorsolateral prostate in contrast to the decreased arginase activity in the ventral prostate following estrogen administration. From these results, it was concluded that the alterations in some enzyme activity of the ventral and the dorsolateral prostates evoked by estrogen treatment were different from those observed in the respective lobes from castrated animals, although both estrogen administration and castration induced atrophy of the tissue. Furthermore, it might be also worth-while to mention that the ventral and the dorsolateral prostates of rats responded in a different manner to estrogen administered.

3-Oxo-5-alpha-Steroid 4-Dehydrogenase↗
PubMed1990

Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.).

Liver arginase of Clarias batrachus has been purified to 56.3-fold employing ammonium sulphate fraction, DEAE-cellulose and CM-cellulose chromatography. Bidirectional polyacrylamide gel electrophoresis shows the presence of two isoenzymes of arginase. The enzyme has a molecular weight of about 87,000 and Km 15.38 mM for L-arginine, optimum pH 9.5 and temperature 37 degrees C. Ornithine and leucine as competitive whereas valine and isoleucine act as non-competitive inhibitors with respect to L-arginine as substrate.

Animals↗
PubMed1998

Secreted, glycosylated arginase from Xanthoria parietina thallus induces loss of cytoplasmic material from Xanthoria photobionts.

A secreted, glycosylated arginase (lectin) from Xanthoria parietina thallus binds to the cell wall of Xanthoria photobiont when cell wall urease has previously been induced. The uptake of this secreted arginase by the algal cell without cell wall ligand for the lectin increases the concentration of algal putrescine and it is followed by an apparent loss of chlorophyll. However, neither chlorophyllase activity has been detected nor chlorophyllide concentration increases after loading the cells with putrescine. The loss of chlorophyll can be explained by the loss of algal protoplast resulting from the action of a putrescine-activated glucanase and the split of their membrane in an hypoosmotic medium. The loss and split of protoplasts have been shown by light and transmission electron microscopy.

Arginase↗