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PubMed2004

[Effect of vasectomy on arginase's activity in accessory sexual glands of rats].

BACKGROUND: Although vasectomy is the most used contraceptive method, its effect over male biochemical and physiological parameters has not been evaluated. OBJECTIVE: To study the effect of vasectomy on arginase activity in accessory sex glands of the rat. MATERIAL AND METHODS: Twenty male healthy rats weighing 300-350 g were divided into four groups (n = 5). Groups I, II and III were vasectomized, and group IV was the control group. In order to measure the activity of arginase in the accessory sex glands, glucose, triglycerides and protein concentration, as well as arginase activity in serum, rats were killed at 4, 30 and 60 days post-surgery. RESULTS: The biochemical parameters of serum changed following vasectomy, but it is possible that these changes were at random. However, arginase activity in serum in accessory sex glands was not affected by vasectomy. CONCLUSION: Vasectomy does not affect arginase activity in accessory sex glands of male rats in spite of the high activity observed in short time in both coagulant and bulbourethral glands. Changes observed in serum biochemical parameters, which included glucose, triglycerides, proteins, arginase and alkaline phosphatase activities, were not relevant.

Animals↗

PubMed1987

[Intestinal arginase in the phylogenetic development of animals].

The activity of intestinal arginase was studied in 31 species belonging to the types Annelides, Arthropoda and Chordata. Large variations of the enzyme activity were tested. The differences were of 2 orders of magnitude--100 times. Four groups were selected: animals with very low arginase activity up to 0.20 microM of ornithine/mg of protein/15 min; this group comprises both phylogenetically lower and higher animals (cockroach, locust, frog, duck, domestic hen, broiler chicken, horse, hyppopotamus, ox, sheep, antelope); animals with rather low activity up to 0.22 to 0.60 microM of ornithine/mg of protein/15 min (crayfish, herring, salmon, bream, cod, pike-perch, mink, fox, dog. man); animals with moderate activity up to 0.63 to 1.15 microM of ornithine/mg of protein/15 min (pigeon, coypu, guinea-pig, hog); animals with high activity up 1.15 to 9.26 microM of ornithine/mg of protein/15 min (rabbit, rat, hamster, mouse). According to the profile the activity of the enzyme along the long axis of the intestine two groups of animals could be separated: one in which arginase activity is the same over the whole length of the intestine, in animals with very low and rather low arginase activity, and the second in which there is a distinct topographical differentiation of activity (the highest in the jejunum decreasing gradually with differing gradients) in animals with moderate and high arginase activity. Intestinal arginase activity in quails in ontogenic development from the birth up to 233 days, show 2 peaks--one at 9 and the second at 23 days.

Animals↗

PubMed1985

Comparison of arginase activity in red blood cells of lower mammals, primates, and man: evolution to high activity in primates.

Arginase activity in red blood cells (RBC) of various mammalian species including man was determined. In nonprimate species, the activity generally fell below the level of detectability of the assay: less than 1.0 mumol urea/g hemoglobin per hr. Activities in higher nonhuman primates were equal to or of the same order of magnitude as those in man (approximately 950 mumol/g hemoglobin per hr). RBC arginase deficiency with normal liver arginase activity has been shown to segregate as an autosomal codominant trait in Macaca fascicularis established and bred in captivity. This study confirms the presence of this polymorphism in wild populations trapped in several geographic areas and demonstrates the absence of immunologically cross-reactive material in the RBC of RBC arginase-deficient animals. These data when taken together suggest that the expression of arginase in RBC is the result of a regulatory alteration, has evolved under positive selective pressure, and is not an example of the vestigial persistence of an arcane function. The expression of arginase in the RBC results in a marked drop in the arginine content of these cells.

Animals↗

PubMed1993

Enzyme immunoassay of liver-type arginase and its potential clinical application.

We developed an efficient enzyme-linked immunosorbent assay (ELISA) system for measurement of human liver-type arginase in serum. A conjugate of the Fab' fragment of anti-human liver (recombinant) arginase IgG and horseradish peroxidase was used as the second antibody. This assay is highly specific, sensitive, and reproducible, enabling us to detect arginase at concentrations as low as several micrograms per liter without any prior processing of serum. The reaction is linear up to 200 micrograms/L. The arginase concentration in serum, as determined by this method, increased markedly and temporarily at the time of surgical operation or later injury to the liver. The increase was accompanied or followed by increases in serum concentrations of aspartate aminotransferase, alanine aminotransferase, and lactate dehydrogenase, suggesting that the arginase emerged from damaged hepatocytes. In view of a limited tissue distribution of liver-type arginase, our ELISA system may be useful in diagnosis of various hepatic disorders as well as follow-up of postoperative conditions of patients.

Adolescent↗

PubMed1996

Developmental regulation of the urea-cycle enzyme arginase in the direct developing frog Eleutherodactylus coqui.

Direct developing organisms obviate the larval intermediary from their ontogeny, hatching as miniature adults. To investigate this phenomenon, we have examined the developmental expression of arginase in the direct developing frog Eleutherodactylus coqui. An enzyme in the ornithine-urea cycle, the activation of liver arginase is necessary for the switch from ammonotelism to ureotelism which occurs when many frogs metamorphose and assume a terrestrial existence. Arginase enzyme activity is detectable at low levels in late prehatching stages of E. coqui, and increases at hatching, at which point the protein becomes detectable on Western blots. The activity increases gradually during posthatching development, reaching maximal levels at approximately the same time as yolk resorption is completed. Thyroid hormone is responsible for upregulating arginase activity during metamorphosis in Rana, but the role of thyroid hormone in direct developing frogs is unknown. A high dose (250 nM) of the thyroid hormone analogue 3,3'5-triiodo-L-thyronine (T3) caused precocious induction of arginase protein and activity, showing that even in a direct developing frog, some level of responsiveness to the metamorphic trigger, thyroid hormone, has been retained.

Animals↗

PubMed1978

Arginase activity and other cellular events associated with epidermal hyperplasia.

The unknown biochemical role of arginase in epidermal metabolism was probed by examining the association of elevated arginase activity with epidermal hyperplasia and hyperkeratinization. Epidermal hyperplasia was induced experimentally by topical application of 1-decanol to the right side of male hairless mice while the contralateral side served as control. Arginase activity, incorporation of 3H-thymidine into DNA, DNA and protein content were measured in the separated control and experimental epidermis six hours and on days 1 through 5 and 7 after 1-decanol application. After six hours, the epidermis appears damaged histologically, and DNA synthesis is inhibited. By day 1, incorporation of 3H-thymidine into DNA is elevated and a new hyperplastic epidermis has formed beneath the original epidermis. Epidermal arginase is elevated two through seven days after 1-decanol application and always is associated with continuing epidermal hyperplasia. The stimulation of DNA synthesis, which parallels the induction of epidermal hyperplasia by 1-decanol, precedes the induction of epidermal arginase activity. An attempt to relate these results with polyamine synthesis and other metabolic events is made.

Animals↗

PubMed1996

Chemical modification and inactivation of rat liver arginase by N-bromosuccinimide: reaction with His141.

Treatment of rat liver arginase with N-bromosuccinimide results in modification of six tryptophan residues per enzyme molecule and is accompanied by loss of catalytic activity (E. Ber and G. Muzynska (1979) Acta Biochim. Pol. 26, 103-114). In order to probe the chemistry of N-bromosuccinimide inactivation and the role of tryptophan residues in catalysis, the two tryptophan residues of rat liver arginase, Trp122 and Trp164, have been separately mutated to phenylalanine using site-directed mutagenesis of the protein expressed in Escherichia coli. Both single Trp -> Phe mutant enzymes have kinetic parameters nearly identical to those for the wild-type enzyme. Treatment of native, wild-type, and each of the Trp -> Phe mutant enzymes with N-bromosuccinimide results in loss of absorbance at 280 nm and is accompanied by a loss of catalytic activity. However, treatment of the wild-type enzyme with N-bromosuccinimide in the presence of the arginase inhibitors NG-hydroxy-L-arginine or the combination of L-ornithine and borate protects against inactivation, even though tryptophan residues are modified. Treatment of the H101N and H126N mutant arginases with N-bromosuccinimide also results in loss of catalytic activity and modification of tryptophan residues. In contrast, the H141N mutant arginase is not inactivated by N-bromosuccinimide, indicating that His141 is the critical target for the N-bromosuccinimide inactivation of the enzyme.

Amino Acid Sequence↗

PubMed2002

Functional consequences of the G235R mutation in liver arginase leading to hyperargininemia.

Hyperargininemia is a rare autosomal disorder that results from a deficiency in hepatic type I arginase. This deficiency is the consequence of random point mutations that occur throughout the gene. The G235R patient mutation has been proposed to affect the catalytic activity and structural integrity of the protein [D. E. Ash, L. R. Scolnick, Z. F. Kanyo, J. G. Vockley, S. D. Cederbaum, and D. W. Christianson (1998) Mol. Genet. Metab. 64, 243-249]. The G235R (patient) and G235A (control) arginase mutants of rat liver arginase have been generated to probe the effects of these point mutations on the structure and function of hepatic type I arginase. Both mutant arginases were trimeric by gel filtration, but the control G235A mutant had 56% of wild-type activity and the G235R mutant had less than 0.03% activity compared to the wild-type enzyme. The G235R mutant contained undetectable levels of tightly bound manganese as determined by electron paramagnetic resonance, while the G235A mutant had a Mn(II) stoichiometry of 2 Mn/subunit. Molecular modeling indicates that the introduction of an arginine residue at position 235 results in a major rearrangement of the metal ligands that compromise Mn(II) binding.

Animals↗

PubMed1985

Differential expression of multiple forms of arginase in cultured cells.

Arginase (EC 3.5.3.1), the final enzyme in the urea cycle, catalyzes the cleavage of arginine to orthinine and urea. At least two forms of this enzyme, AI and AII, have been described and are probably encoded by discrete genetic loci. The expression of these separate genes has been studied in mammalian cells grown in culture. The permanent rat-hepatoma line H4-II-E-C3 contained exclusively the AI enzyme; the form in mammals comprising about 98% of the arginase activity in liver and erythrocytes but catalyzing only about one half of that reaction in kidney, gastrointestinal tract, and brain. By contrast, human-embryonic-kidney and -brain cells, after transformation with the human papovavirus BK, contained only the AII species of arginase, which form contributes the remaining half of that catalysis in those mammalian tissues in vivo. We report here the results of an extensive study on the properties of these two forms of arginase in the three cell lines, including Km values for arginine, behavior on polyacrylamide gels under non-denaturing conditions, and cross-reactivity with lapine antibodies against the arginases from either rat or human liver.

Animals↗

PubMed2001

Arginase expression in peritoneal macrophages and increase in circulating polyamine levels in mice infected with Schistosoma mansoni.

We investigated the nitric oxide (NO) synthase and arginase pathways in resident peritoneal macrophages of mice infected with the tropical parasite Schistosoma mansoni. The two enzymes may have opposite effects, insofar as NO may be involved in the killing of the parasite whereas arginase may stimulate parasite growth via polyamine synthesis. We determined the effects of the infection on the expression and activity of the two enzymes in macrophages, before and after cytokine activation. Cells from infected mice expressed the hepatic type I arginase, whereas in control cells, the enzyme was expressed only after cytokine activation, as were NO synthase II and type II arginase in both groups of cells. Moreover, we found that in infected mice, arginase expression in macrophages was associated with a ten fold increase in the concentration of circulating ornithine-derived polyamines. This may be of pathological importance, since parasitic helminths are though to be dependent on their hosts for the uptake and interconversion of polyamines.

Animals↗

PubMed2000

A potential role for arginase in recurrent infections and hypertrophy of tonsillar and adenoidal tissue.

Since arginase has been found to be an arginine-depleting and nitric oxide synthase-regulating enzyme, the present study was devised to examine hypertrophied and infected tonsil and adenoid arginase activity in relation to a metabolic arginase-nitric oxide pathway and its association with disease processes. Tissues were taken from 32 children undergoing adenotonsillectomy. There was a statistically significant difference between the two tissue enzyme activities, with tonsillar arginase activity being higher than the corresponding adenoidal tissue (P < 0.005). This suggests a potential role for tissue arginase activity as an outcome module and a contributing factor in chronic recurrent infection and hypertrophy of tonsillar and adenoidal tissues.

Adenoids↗

PubMed2002

Diagnostic performance of arginase activity in colorectal cancer.

Arginase activity was measured in serum and biopsy from healthy individuals and colorectal cancer patients. Arginase activity in tumor samples (87 +/- 7.7 U/g tissue) was significantly higher than in controls (40.7 +/- 3.3 U/g tissue). However, serum arginase activity did not show any significant change in both groups. Finally, the micromethod used to quantify arginase activity in this study is superior to other methods because it has increased sensitivity, requires less sample, and is less time-consuming. Arginase differences are significant, according to the t-test (P<0.05)

Arginase↗

PubMed1988

Multiple molecular forms of mouse liver arginase.

Hepatic arginase (L-arginine amidinohydrolase, EC 3.5.3.1) is an oligomer composed of three or four subunits. The present studies indicate heterogeneity in the size and charge of arginase subunits in mouse liver. Two types of arginase subunits with molecular weights of approximately 35,000 and 38,000 have been found. These two subunits are detected in liver cytosol or in purified preparations of arginase after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. Two dimensional SDS-PAGE revealed multiple ionic forms of arginase for both the 35,000 and 38,000 subunits; the subunits contain basic proteins (pI range 7.8-9.1) and acidic proteins (pI range 5.8-6.4). Limited proteolysis by trypsin eliminated the molecular weight differences between the subunits without substantially affecting either their isoelectric points or activity. Comparative peptide maps and amino acid analyses of the 35,000- and 38,000-Da subunits showed that they were very similar. The data indicate that a neutral peptide (approx 3000 Da) is responsible for the differences in subunit molecular weight and that the multiple sized and charged forms are variants of the same protein.

Amino Acids↗

PubMed1991

pH-sensitive control of arginase by Mn(II) ions at submicromolar concentrations.

The manganese dependence of arginase was reinvestigated with extracts of mouse liver to see whether more physiological properties were displayed than have been reported for the purified enzyme. In a preincubation with Mn(II) ions at 37 degrees C the enzyme underwent a slow and reversible activation. At least 90-95% of the activation achieved was dependent on Mn2+. However, no Mn2+ was required for catalytic activity in the assay. The activation showed little dependence upon pH over the range 6.5-9.5, whereas the catalytic activity increased 12-fold in apparent accord with the titration curve of an ionizable group of pKa 7.9. The Mn2+ dependence of arginase activation obeyed Michaelis-Menten kinetics, with Kd varying from 0.3 microM at pH 6.8 to 0.08 microns at pH 7.7. Free Mn2+ concentrations were established in these assays with a trimethylenediaminetetraacetate-Mn buffer. Vmax increased about three-fold over this range. The calculated arginase activity at 0.05 microM Mn2+ increases about nine-fold over this physiological pH range. An enzyme model is proposed to explain these findings. The activity of arginase at "physiological" [Mn2+] and the pronounced pH dependence conferred upon it are consistent with a recently revised role for the urea cycle in the control of bicarbonate and pH in the body. It appears possible that arginase loses Mn2+ sensitivity during the usual purification.

Animals↗

PubMed1986

Uterine arginase inhibition affect the rat embryonic development.

The presence of polyamines (putrescine, spermidine and spermine) and the enzymatic activity of extrahepatic arginase (E.C. 3.5.3.1) which catalizes the hydrolysis of L-arginine into L-ornithine and urea have been related with cellular growth and development in several tissues. The enzymatic activity of arginase in rat implantation sites and its participation in reproductive process is demonstrated. Long-Evans adult rats during the 4th or 5th days of pregnancy were utilized. Arginase activity is higher in non-decidualized tissue (86.1 +/- 33 nmoles of urea/mg protein/min-1) when was compared with implantation sites (61.7 +/- 17). Intrauterine administration of several concentrations of a new synthetic L-ornithine analogue, AIAVA (2-amine-5-iodoacetamide valeric acid), produced embryonic growth arrest concomitant with arginase inhibition but not ornithine decarboxylase. From our results it is possible to stress the metabolic importance of uterine arginase in reproductive process.

Animals↗

PubMed1992

Regulation of arginase production by glucocorticoid in three human gastric cancer cell lines.

Gastric cancer tissues have high levels of glucocorticoid receptors (GR) and arginase. To investigate the interrelation of glucocorticoid, GR and arginase, three human gastric cancer cell lines (AZ-521, NUGC-3, KATO-III) were treated with hydrocortisone in the presence or absence of a glucocorticoid antagonist RU38486. GR were found to be present in all three lines, and hydrocortisone significantly increased the production of total arginase in all 3 lines. The induction of arginase production by hydrocortisone was inhibited by RU38486. These findings suggest that the regulation of arginase production by hydrocortisone in gastric cancer cells is mediated through GR.

Arginase↗

PubMedDate not supplied

The mechanisms of the inhibitory effects of liver extract on lymphocyte proliferation. III. The effects of arginase on DNA polymerase activities.

The incorporation of labeled precursors into DNA, RNA and protein in phytohaemagglutinin (PHA)-prestimulated human lymphocytes was maximally inhibited by liver extract (LEx) or arginase at 24 h. The activities of DNA polymerase alpha, beta and gamma were less inhibitable by these agents than was [3H]thymidine incorporation. The inhibition of DNA, RNA and protein syntheses by either LEx or arginase is probably due to arginine depletion by arginase activity, since their syntheses were similarly inhibited when cultured in an arginine-free medium in the absence of arginase. These results indicate that arginase nonspecifically inhibits the activities of DNA polymerase. The inhibition is probably due to arginine depletion.

Animals↗

PubMed1984

Effect of steroid hormones on age dependent changes in rat arginase isoenzymes.

Age dependent changes in rat liver and kidney arginase isoenzymes from day 1 to 73 weeks have been studied. It has been observed that total liver arginase activity (activity/liver) increases with age, but there is no appreciable change in the proportions of isoenzymes, their pH optima, electrophoretic mobilities and inhibition characteristics, although Km increases with age. Corticosterone induces liver arginase activity and the degree of induction decreases with age. The hormone has no effect on kidney arginase. Testosterone treatment, on the other hand, induces kidney arginase without any effect on liver enzyme.

Age Factors↗