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PubMedDate not supplied

[Comparative study of the activity of arginase isoenzymes in brain tumors of humans and experimental animals].

Isoenzyme spectrum and total activity of arginase were studied in rat brain during growth of transplanted neurinoma and glioma as well as in malignant tissues of human brain. After transplantation of the tumors two peaks of arginase activation were observed within 2-4 days in rat brain tissues and within 16 days in tumoral tissue. Positively charged isoenzyme I of arginase was mainly activated but activity of neutral isoenzyme II was unaltered or slightly decreased. In human brain tumors activity of isoenzyme I was also prevailed, while activity of isoenzyme II was increased in some cases. Regulation of the arginase activity appears to occur by a complex mechanism and the enzyme plays a key role in development of nervous tissue neoplasms.

Animals↗

PubMed1977

Reactivation of the EDTA-treated arginase from rat and calf liver.

1. The anionic calf liver arginase, like the cationic rat liver enzyme, is inactivated by EDTA-treatment. The activity is fully restored by Mn2+. A smaller effect is observed with Cd2+, Ni2+ and Co2+. 2. The EDTA-inactivated calf liver arginase, unlike the rat liver enzyme, does not dissociate into subunits, and its mol.wt. (120 000) is unchanged. 3. The reactivation of rat liver arginase subunits (mol.wt. 30 000) by Ni2+ is accompanied, similarly as in the case of Mn2+, by reassociation to the form of mol.wt. 120 000, i.e. the same as for the native enzyme. 4. It is suggested that Mn2+ in arginase is bound at the active site and at the site responsible for maintenance of the oligomeric structure. In calf liver enzyme this binding site is inaccessible to the chelating agent.

Animals↗

PubMed1983

Arginase activity and polyamine biosynthesis in psoriasis.

Polyamine biosynthesis and arginase activity in psoriasis were studied using keratotome strips and suction blister roofs as specimens. In the uninvolved psoriatic skin a slight (1.3-fold; p less than 0.05) increase in the spermidine level was observed compared with control skin. There was also a 1.2-fold increase (p less than 0.05) in the spermidine/spermine molar ratio, which is considered to be an indicator of proliferation activity. No changes were noted in other polyamines or polyamine-synthesizing enzymes ornithine decarboxylase (ODC) and S-adenosyl-L-methionine decarboxylase (AMDC) in the uninvolved psoriatic skin vs. control skin. Neither was there any significant difference in the arginase activity. In psoriatic lesions the levels of all polyamines, as well as the activities of biosynthetic enzymes, were significantly (p less than 0.001) elevated. The putrescine level was elevated to 2.5-fold, spermidine to 2.7-fold and spermine to 1.4-fold. The enzyme activities expressed severalfold increases. The enhancement of arginase activity was less prominent than that of polyamine-synthesizing enzymes, but the increase from 271 +/- 88 to 354 +/- 126 mumol/g/h (1.3-fold) was statistically significant (p less than 0.001; paired t-test). The increase in arginase activity in suction blister roofs, which represents pure epidermis, was more pronounced than that in keratotome strips, i.e. about double. The results show thus that polyamine biosynthesis is significantly enhanced in psoriatic lesions, but there is only a slight difference between the uninvolved psoriatic skin and control skin.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗

PubMed1984

Immunological properties of rat arginases.

Five immunologically different forms of arginase were evidenced in rat tissues by the double diffusion test and immunoelectrophoresis. New symbols for these arginases are proposed (beginning with the most anionic forms): A1 (kidney), A2 (liver), A3 (salivary glands), A4 (kidney) and A5 (liver). Arginases A1 from kidney and A5 from liver are paternal forms built of one-type subunits. Subunits of form A1 exhibit a non-identity cross-reaction with subunits of form A5. Arginases A2, A3 and A4 are hybrids composed of both kinds of subunits.

Animals↗

PubMed1997

Differences of alkaline phosphatase and arginase activities in human colorectal carcinoma cell lines.

Remarkable differences in the levels of alkaline phosphatase and arginase were found in colorectal cell lines tested. In HT-29 cells, which are extremely sensitive to the induction of cell differentiation, very low levels of arginase were detected. On the other hand, high levels of arginase were present in cell lines derived from highly malignant tumours. Both findings support a prognostic significance of arginase activity in colorectal carcinomas.

Alkaline Phosphatase↗

PubMed1986

Cloning and expression in Escherichia coli of cDNA for arginase of rat liver.

A cDNA expression library constructed in a plasmid pUC8 from poly(A)+ RNA of rat liver was screened immunologically, using an antibody against arginase of rat liver. A cDNA clone was isolated and identified by hybrid-selected translation. The clone contained an insert approximately 1.35 kilobase pairs in length. In the bacterial clone, we detected a specific protein of Mr = about 43,000 that is slightly larger than the purified arginase (Mr = about 40,000) and a high activity of arginase was expressed. The arginase mRNA species of about 1600 bases long was detected in the liver, but not in the small intestine, kidney, spleen and heart of the rats.

Animals↗

PubMed1982

Polyamine dependence of Chinese hamster ovary cells in serum-free culture is due to deficient arginase activity.

We recently isolated a Chinese hamster ovary cell line which grows well without serum but requires the exogenous polyamines putrescine, spermidine or spermine for continuous replication. Here we show that these cells are defective in the arginase-catalyzed synthesis of ornithine, the precursor of polyamines, and that ornithine can replace polyamines in the medium for supporting growth of the cells. The activities of two other key enzymes of polyamine biosynthesis, ornithine decarboxylase and adenosylmethionine decarboxylase, are clearly detectable and show increase during polyamine starvation. In ornithine-and polyamine-free medium cellular putrescine and spermidine are rapidly depleted while the concentration of spermine decreases only moderately. We show further that the cells are able to grow in serum-containing medium without added ornithine or polyamines. This is explained by our finding that serum contains arginase which synthesizes ornithine from arginine in the medium. All the sera from different animal species tested contained arginase activity although in greatly varying amounts. Serum-free medium is therefore essential for expression of arginase deficiency in cells in tissue culture. The eventual importance of polyamines for serum-free cultures in general is discussed.

Adenosylmethionine Decarboxylase↗

PubMed1979

Comparative studies on serum arginase and transaminases in hepatic necrosis in various species of domestic animals.

Serum concentrations of arginase, glutamic pyruvic transaminase (SGPT) and glutamic oxaloacetic transaminase (SGOT) in dogs, cats, horses, cattle, sheep and pigs were determined before and after oral administration of CCl(4) at doses known to cause hepatic necrosis. Following CCl(4) administration, serum concentration of arginase and SGOT increased to a level of diagnostic significance in all animals. SGPT increased markedly in dogs and cats and marginally in 1 of 3 cattle and 2 of 3 pigs. In the surviving animals, the serum concentration of arginase returned to normal range much earlier than SGPT or SGOT. Based on the CCl(4) experimental toxicity results of this study, an elevated level of serum arginase would appear to be a reliable indicator of hepatic necrosis in both small and large animals whereas SGPT would be a reliable indicator of hepatic necrosis only in dogs and cats.

Journal Article↗

PubMed1995

Separation of arginase isoforms by capillary zone electrophoresis and isoelectric focusing in density gradient column.

Four major arginase isoforms, I, II, III and IV, have been detected in Evernia prunastri thallus. They differ in terms of both physical and biochemical properties. The isoelectric point (pI) of these proteins has been determined by both isoelectric focusing in density gradient column and high-performance capillary electrophoresis (HPCE). Isoelectric focusing revealed charge microheterogeneity for isoforms II and IV whereas arginases I and II had the same pI value of 5.8. HPCE separation confirmed this charge microheterogeneity for isoform IV but not for isoform III, and provided evidence of microheterogeneity for isoforms I and II. The effect of various electrolyte buffers and running conditions on the HPCE separation of arginase isoform were investigated. Addition of 0.5 mM spermidine (SPD) to the running buffer reduced the electroosmotic flow (EOF) and permitted discriminating between the native proteins and protein fragments.

Arginase↗

PubMed1983

Activities of arginase, transamidinase, and ornithine aminotransferase in glia, neurons, and synaptosomes.

The regional, cellular, and subcellular distribution of some enzymes of the urea cycle in brain is not clearly known. Glia, neurons, and synaptosomes have been prepared from rat cerebral cortex and arginase (EC 3.5.3.1), transamidinase (EC 2.1.4.1), and ornithine aminotransferase (EC 2.6.1.13) have been estimated in order to understand the metabolic and functional role of these enzymes. It has been observed that arginase is predominantly localized in synaptosomes and neurons. The ornithine aminotransferase was found to be high in glial cells and very high in synaptosomes (higher than arginase). Transamidinase was mostly localized in glial cells. The implication of these results has been discussed in relation to a possible role of ornithine acting as a precursor of glutamate in glutametargic nerve endings and its possible participation in the glutamate-glutamine cycle.

Acyltransferases↗

PubMed1994

Comparison of substrate and inhibitor specificity of arginase and nitric oxide (NO) synthase for arginine analogues and related compounds in murine and rat macrophages.

Arginine utilizing enzymes in macrophages showed different specificities for various arginine analogues and derivatives as substrates and inhibitors. Isolated arginase was strongly inhibited by L-canavanine(Can) and L-ornithine(Orn) but only slightly by L-homoarginine(Hom) and L-argininamide(ArgNH2). These effects were not or only weakly observed when released urea was measured in long term cell cultures. On the other hand, both L-canavanine and L-argininamide were substrates for arginase in long-term cultures. The known inhibitors of NO synthase were ineffective. The mechanisms of inhibition were different for L-canavanine and L-ornithine, but clear mechanisms could not be identified). NO synthase was studied only in long term cell cultures without purification. Certain N-guanidino (NG)-substituted arginine derivatives caused a marked inhibition while inhibitors of arginase had only slight or no effect. L-homoarginine was also found to be the substrate of NO synthase. The comparison of these effects of arginine analogues and derivatives made possible a computer-aided approximation for the fitting of active centers of these enzymes to their substrates.

Amino Acid Oxidoreductases↗

PubMed1994

N omega-hydroxyl-L-arginine, an intermediate in the L-arginine to nitric oxide pathway, is a strong inhibitor of liver and macrophage arginase.

N omega-Hydroxy-L-arginine (L-NOHA) is a potent inhibitor of the hydrolysis of L-arginine (L-Arg) to L-ornithine (L-Orn) catalyzed by purified bovine liver arginase (BLA). It appears as one of the most powerful arginase inhibitors reported so far (Ki = 150 microM). The other products of NO synthase are either without effect (NO2-, NO3-) or much weaker inhibitors (L-citrulline (L-Cit) and NO) of BLA. Products derived from a possible hydrolysis of L-Arg (L-Orn and urea) or of L-NOHA (L-Cit, hydroxyurea and hydroxylamine) are also inactive toward BLA at concentrations up to 2 mM. The configuration of L-NOHA is important as D-NOHA is much less active, and its free -COOH and alpha-NH2 functions are required for recognition of BLA. L-NOHA is also a potent inhibitor of the arginase activity of rat liver homogenates and of murine macrophages (IC50 of 150 and 450 microM, respectively). These remarkable properties of L-NOHA could play a role in the modulation of the biosynthesis of the biological mediator NO by increasing local L-Arg concentrations.

Animals↗

PubMed1995

Arginase induction by suppressors of nitric oxide synthesis (IL-4, IL-10 and PGE2) in murine bone-marrow-derived macrophages.

The present study addresses the regulatory mechanisms involved in the arginine metabolism of macrophages by arginase and nitric oxide synthase. Induction of both enzymes with LPS or by mixed lymphocyte reaction has been reported. Here, we demonstrate that these enzymes can be independently induced in murine bone-marrow-derived macrophages with the appropriate agonists. Arginase expression is specifically triggered by IL-4, IL-10, PGE2 as well as non-toxic or detoxified LPS. Conversely, IFN gamma induces only NO synthesis in these cells. The results demonstrate that the metabolism of arginine in macrophages is controlled by TH1/TH2-dependent cytokines and suggest a regulatory role of arginase on the NO synthesis by intracellular substrate depletion.

Amino Acid Oxidoreductases↗

PubMed1995

Co-induction of arginase and nitric oxide synthase in murine macrophages activated by lipopolysaccharide.

In view of studies showing that not only nitric oxide synthase (NOS) activity but arginase activity is induced in rodent macrophages by lipopolysaccharide (LPS), the objective of this study was to investigate the co-induction of these two enzymes and to ascertain whether common mechanisms are involved. RAW 264.7 cells were activated by 2 micrograms LPS/ml and incubated for up to 48 hr. Inducible NOS (iNOS) and inducible arginase II (AII) activities were monitored, respectively, by measuring NO2-/NO3- accumulation in cell culture media and formation of urea (as CO2) from L-arginine by cell lysates. AII activity increased linearly up to at least 48 hr, whereas NO2-/NO3- formation reached a plateau well before 48 hr. Immunoprecipitation experiments revealed that AII accounted for 90-100% of arginase activity in LPS-activated macrophages. The inhibitor of NF-kappa B activation, pyrrolidine dithiocarbamate, inhibited the induction of iNOS but not AII. Moreover, whereas IFN-gamma caused iNOS induction, AII induction was nearly abolished by IFN-gamma, perhaps by inhibiting transcription of the AII gene. These observations indicate that co-induction of iNOS and AII occurs by distinct transcriptional mechanisms, AII induction could diminish NO production by decreasing L-arginine availability, and IFN-gamma can prevent AII induction.

Amino Acid Oxidoreductases↗

PubMed2002

Effects of arginase isoforms on NO Production by nNOS.

Both arginase isoforms (AI and AII) regulate high-level NO production by the inducible NOS, but whether the arginase isoforms also regulate low-level NO production by neuronal NOS (nNOS) is not known. In this study, 293 cells that stably overexpress nNOS gene (293nNOS cells) were transfected with rat AI (pEGFP-AI) or AII (pcDNA-AII) plasmids, and nitrite production was measured with or without supplemental L-arginine. Transfection with pEGFP-AI increased AI expression and activity 10-fold and decreased intracellular l-arginine by 50%. Nitrite production was inhibited by >80% when no l-arginine was supplemented but not when 1 mM L-arginine was present. The inhibition was reversed by an arginase inhibitor, N(omega)-hydroxy-L-arginine. Transfection with pcDNA-AII increased AII expression and activity but had little effect on nitrite production even if no l-arginine was added. These results suggest that, in 293nNOS cells, AI was more effective in regulating NO production by nNOS, most likely by competing for L-arginine.

Animals↗

PubMed1979

The significance of the arginine and arginase of tears in experimentally-induced herpes simplex corneae.

Experimental corneal herpes is always accompanied by the accumulation of arginine, the substrate of arginase, in tears, ensuring the multiplication of the herpes hominis virus. The main source of the large amount of arginine is the desquamating corneal epithelium, since after the epithelium of the cornea is abraded the arginine content of the tears again equals that of healthy tears. The low arginase content of rabbit tears can be supplemented by arginase applied as eyedrops, and this results in the cure of the herpetic process.

Animals↗

PubMed1977

[Biochemistry of free amino acids in the stratum corneum of human epidermis. I. The reaction of arginase (author's transl)].

The human horny layer contains insoluble arginase, which is tied to keratinic cells, with an activity of about 1 mU/cm2 skinsurface. About 50 p.c. of arginase is inhibited by water soluble substances of horny layer or by using soaps and syndets. By washing the skinsurface with water the activity increases. Presumable the horny layer arginase has a function in the urea production of sweat.

Arginase↗

PubMed1981

Inhibition of arginase in sheep brain homogenates by some L-amino acids.

The effect of 16 L-amino acids on the activity levels of arginase in sheep brain homogenates was studied. The amino acids leucine, valine, lysine, and ornithine inhibited arginase activity significantly. The other amino acids tested did not show a significant influence on arginase activity. The inhibition was related to the carbon chain length of the amino acids.

Amino Acids↗