A ureahydrolase that catalyzes the hydrolysis of arginine or canavanine to yield L-ornithine (ORNITHINE) and urea. Deficiency of this enzyme causes HYPERARGININEMIA. EC 3.5.3.1.
A rare autosomal recessive disorder of the urea cycle. It is caused by a deficiency of the hepatic enzyme ARGINASE. Arginine is elevated in the blood and cerebrospinal fluid, and periodic HYPERAMMONEMIA may occur. Disease onset is usually in infancy or early childhood. Clinical manifestations include seizures, microcephaly, progressive mental impairment, hypotonia, ataxia, spastic diplegia, and quadriparesis. (From Hum Genet 1993 Mar;91(1):1-5; Menkes, Textbook of Child Neurology, 5th ed, p51)
An essential amino acid that is physiologically active in the L-form.
An amino acid produced in the urea cycle by the splitting off of urea from arginine.
Amino derivatives of caproic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the amino caproic acid structure.
A free radical gas produced endogenously by a variety of mammalian cells, synthesized from ARGININE by NITRIC OXIDE SYNTHASE. Nitric oxide is one of the ENDOTHELIUM-DEPENDENT RELAXING FACTORS released by the vascular endothelium and mediates VASODILATION. It also inhibits platelet aggregation, induces disaggregation of aggregated platelets, and inhibits platelet adhesion to the vascular endothelium. Nitric oxide activates cytosolic GUANYLATE CYCLASE and thus elevates intracellular levels of CYCLIC GMP.
A CALCIUM-independent subtype of nitric oxide synthase that may play a role in immune function. It is an inducible enzyme whose expression is transcriptionally regulated by a variety of CYTOKINES.
A urea cycle enzyme that catalyzes the formation of orthophosphate and L-citrulline (CITRULLINE) from CARBAMOYL PHOSPHATE and L-ornithine (ORNITHINE). Deficiency of this enzyme may be transmitted as an X-linked trait. EC 2.1.3.3.
An NADPH-dependent enzyme that catalyzes the conversion of L-ARGININE and OXYGEN to produce CITRULLINE and NITRIC OXIDE.
A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.
Inorganic or organic compounds that contain the basic structure RB(OH)2.
A high-affinity, low capacity system y+ amino acid transporter with strong similarity to CATIONIC AMINO ACID TRANSPORTER 1. The two isoforms of the protein, CAT-2A and CAT-2B, exist due to alternative mRNA splicing. The transporter has specificity for the transport of ARGININE; LYSINE; and ORNITHINE.

Expression of arginase II and related enzymes in the rat small intestine and kidney. (1/943)

Arginase, which catalyzes the conversion of arginine to urea and ornithine, and consists of a liver-type (arginase I) and a non-hepatic type (arginase II). Arginine is also used for the synthesis of nitric oxide and creatine phosphate, while ornithine is used for the synthesis of polyamines and proline, and thus collagen. Arginase II mRNA and protein are abundant in the intestine (most abundant in the jejunum and less abundant in the ileum, duodenum, and colon) and kidney of the rat. In the kidney, the levels of arginase II mRNA do not change appreciably from 0 to 8 weeks of age. In contrast, arginase II mRNA and protein in the small intestine are not detectable at birth, appear at 3 weeks of age, the weaning period, and their levels increase up to 8 weeks. On the other hand, mRNAs for ornithine aminotransferase (OAT), ornithine decarboxylase, and ornithine carbamoyltransferase (OCT) are present at birth and their levels do not change much during development. Arginase II is elevated in response to a combination of bacterial lipopolysaccharide, dibutyryl cAMP, and dexamethasone in the kidney, but is not affected by these treatments in the small intestine. Immunohistochemical analysis of arginase II, OAT, and OCT in the jejunum revealed their co-localization in absorptive epithelial cells. These results show that the arginase II gene is regulated differentially in the small intestine and kidney, and suggest different roles of the enzyme in these two tissues. The co-localization of arginase II and the three ornithine-utilizing enzymes in the small intestine suggests that the enzyme is involved in the synthesis of proline, polyamines, and/or citrulline in this tissue.  (+info)

Arginase from human full-term placenta. (2/943)

Arginase was purified about 1800-fold from extracts of human full-term placenta; the enzyme appeared to be homogenous by disc electrophoresis and molecular-sieve chromatography. The mol. wt. determination by gel filtration and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis yielded a value of 70000 for the most pure and the partially purified enzyme. The human placenta arginase is a metalloenzyme with an optimum pH of 9.1. The Km for L-arginine is 27 mM. L-Ornithine and L-lysine show competitive inhibition with Ki values of 6.3 and 14 mM respectively.  (+info)

Glucocorticoids mediate the enhanced expression of intestinal type II arginase and argininosuccinate lyase in postweaning pigs. (3/943)

Arginine metabolism is enhanced in the small intestine of weanling pigs, but the molecular mechanism(s) involved is not known. The objectives of this study were to determine the following: 1) whether glucocorticoids play a role in induction of intestinal arginine metabolic enzymes during weaning; 2) whether the induction of enzyme activities was due to increases in corresponding mRNA levels; and 3) the identity of the arginase isoform(s) expressed in the small intestine. Jejunum was obtained from 29-d-old weaned pigs that were or were not treated with 17-beta-hydroxy-11beta-(4-dimethylaminophenyl)17alpha-(prop- 1-ynyl)es tra-4,9-dien-3-one (RU486, an antagonist of glucocorticoid receptors), or from age-matched suckling pigs. Activities and mRNA levels for type I and type II arginases, argininosuccinate synthase (ASS) and argininosuccinate lyase (ASL) were determined. Activities of arginase, ASL and ASS increased by 635, 56 and 106%, respectively, in weanling pigs, compared with suckling pigs. RU486 treatment attenuated the increase in arginase activity by 74% and completely prevented the ASL induction in weanling pigs, but had no effect on ASS activity. Pig intestine expresses both type I and type II arginases. On the basis of immunoblot analyses, there was no significant difference in levels of intestinal type I arginase among these three groups of pigs, indicating that changes in arginase activity were due only to type II arginase. The mRNA levels for type II arginase and ASL increased by 135 and 198%, respectively, in weanling pigs compared with suckling pigs, and this induction was completely prevented by RU486. In contrast, ASS mRNA levels did not differ between suckling and weanling pigs. These results suggest that intestinal type II arginase, ASS and ASL are regulated differentially at transcriptional and post-translational levels and that glucocorticoids play a major role in the induction of type II arginase and ASL mRNAs in the small intestine of weanling pigs.  (+info)

Metabolic capacity for L-citrulline synthesis from ammonia in rat isolated colonocytes. (4/943)

Ammonia is present at high concentration in the colon lumen and is considered a colon cancer suspect. Furthermore, ammonia usually eliminated by the liver in the ornithine cycle is considered highly toxic to cerebral function when present in excess in the blood plasma. Therefore, the metabolic pathways involved in ammonia metabolism in colonocytes were studied in the present study. Rat colonocytes were found equipped with low carbamoylphosphate synthase I activity, high ornithine carbamoyltransferase and arginase activities and low argininosuccinate synthase activity. High (10 and 50 mmol/l) NH4Cl concentrations but not low concentrations (1 and 5 mmol/l) were found able to increase respectively 3- and 10-fold the conversion of radioactive L-arginine to L-citrulline. In contrast, very low capacity for L-citrulline conversion to L-arginine is found in colonocytes. It is concluded that an incomplete ornithine cycle is operative in colonocytes which results in ammonia stimulated L-citrulline production. The contribution of this metabolic pathway in relation to ammonia detoxication by colonocytes is discussed.  (+info)

Regulation of the genes for arginase isoforms and related enzymes in mouse macrophages by lipopolysaccharide. (5/943)

Arginase exists in two isoforms, the hepatic (arginase I) and extrahepatic types (arginase II). Arginase I is markedly induced in rat peritoneal macrophages and rat tissues in vivo by bacterial lipopolysaccharide (LPS). In contrast, both arginase I and arginase II are induced in LPS-activated mouse peritoneal macrophages. In the present study, expression of arginase isoforms and related enzymes was studied in mouse tissues in vivo and in peritoneal macrophages with RNA blot and immunoblot analyses and enzyme assay. When mice were injected intraperitoneally with LPS, inducible nitric oxide synthase (iNOS) and arginase II were induced early in the lung and spleen. mRNAs for argininosuccinate synthase (AS) and ornithine decarboxylase (ODC) were also induced early. In comparison, arginase I was induced later in the lung. Early induction of iNOS, arginase II, AS, ODC, and cationic amino acid transporter 2 and late induction of arginase I were observed in LPS-activated peritoneal macrophages. These results indicate that the genes for the two arginase isoforms are regulated differentially. Possible roles of the arginase isoforms in the regulation of nitric oxide production and in polyamine synthesis are discussed.  (+info)

Biochemical and functional profile of a newly developed potent and isozyme-selective arginase inhibitor. (6/943)

An increase in arginase activity has been associated with the pathophysiology of a number of conditions, including an impairment in nonadrenergic and noncholinergic (NANC) nerve-mediated relaxation of the gastrointestinal smooth muscle. An arginase inhibitor may rectify this condition. We compared the effects of a newly designed arginase inhibitor, 2(S)-amino-6-boronohexanoic acid (ABH), with the currently available N(omega)-hydroxy-L-arginine (L-HO-Arg), on the NANC nerve-mediated internal anal sphincter (IAS) smooth-muscle relaxation and the arginase activity in the IAS and other tissues. Arginase caused an attenuation of the IAS smooth-muscle relaxations by NANC nerve stimulation that was restored by the arginase inhibitors. L-HO-Arg but not ABH caused dose-dependent and complete reversal of N(omega)-nitro-L-arginine-suppressed IAS relaxation that was similar to that seen with L-arginine. Both ABH and L-HO-Arg caused an augmentation of NANC nerve-mediated relaxation of the IAS. In the IAS, ABH was found to be approximately 250 times more potent than L-HO-Arg in inhibiting the arginase activity. L-HO-Arg was found to be 10 to 18 times more potent in inhibiting the arginase activity in the liver than in nonhepatic tissues. We conclude that arginase plays a significant role in the regulation of nitric oxide synthase-mediated NANC relaxation in the IAS. The advent of new and selective arginase inhibitors may play a significant role in the discrimination of arginase isozymes and have important pathophysiological and therapeutic implications in gastrointestinal motility disorders.  (+info)

Th1/Th2-regulated expression of arginase isoforms in murine macrophages and dendritic cells. (7/943)

Activated murine macrophages metabolize arginine by two alternative pathways involving the enzymes inducible NO synthase (iNOS) or arginase. The balance between the two enzymes is competitively regulated by Th1 and Th2 T helper cells via their secreted cytokines: Th1 cells induce iNOS, whereas Th2 cells induce arginase. Whereas the role of macrophages expressing iNOS as inflammatory cells is well established, the functional competence of macrophages expressing arginase remains a matter of speculation. Two isoforms of mammalian arginases exist, hepatic arginase I and extrahepatic arginase II. We investigated the regulation of arginase isoforms in murine bone marrow-derived macrophages (BMMPhi) in the context of Th1 and Th2 stimulation. Surprisingly, in the presence of either Th2 cytokines or Th2 cells, we observe a specific induction of the hepatic isoform arginase I in BMMPhi. Induction of arginase I was shown on the mRNA and protein levels and obeyed the recently demonstrated synergism among the Th2 cytokines IL-4 and IL-10. Arginase II was detectable in unstimulated BMMPhi and was not significantly modulated by Th1 or Th2 stimulation. Similar to murine BMMPhi, murine bone marrow-derived dendritic cells, as well as a dendritic cell line, up-regulated arginase I expression and arginase activity upon Th2 stimulation, whereas arginase II was never detected. In addition to revealing the unexpected expression of arginase I in the macrophage/monocyte lineage, these results uncover a further intriguing parallelism between iNOS and arginase: both have a constitutive and an inducible isoform, the latter regulated by the Th1/Th2 balance.  (+info)

Carbon and nitrogen repression of arginine catabolic enzymes in Bacillus subtilis. (8/943)

Specific activities of arginase and ornithine aminotransferase, inducible enzymes of arginine catabolism in Bacillus subtilis 168, were examined in cells grown with various carbon and nitrogen sources. Levels of these enzymes were similar in arginine-induced cultures whether glucose or citrate was the carbon source (in contrast to histidase), suggesting that carbon source catabolite repression has only limited effect. In media with combinations of nitrogen sources, glutamine strongly repressed induction of these enzymes by proline or arginine. Ammonium, however, only repressed induction by proline and had no effect on induction by arginine. These effects correlate with generation times in media containing these substances as sole nitrogen sources: growth rates decreased in the order glutamine-arginine-ammonium-proline. Similar phenomena were observed when glutamine or ammonium were added to arginine- or proline-grown cultures, or when arginine or proline were added to glutamine- or ammonium-grown cultures. In the latter cases, an additional feature was apparent, namely a surprisingly long transition between steady-state enzyme levels. The results are compared with those for other bacteria and for eucaryotic microorganisms.  (+info)

The symptoms of hyperargininemia typically become apparent within the first few months of life and may include:

1. Developmental delays
2. Seizures
3. Hypotonia (low muscle tone)
4. Cognitive impairment
5. Vision loss or blindness
6. Hearing loss
7. Kidney damage or failure
8. Increased risk of infections

Hyperargininemia is usually diagnosed through a combination of clinical evaluation, laboratory testing, and genetic analysis. Treatment for the disorder typically involves managing the symptoms and preventing complications. This may include:

1. Avoiding arginine-rich foods in the diet
2. Providing supplemental nutrition to support growth and development
3. Managing seizures with anticonvulsant medications
4. Physical therapy to improve muscle tone and mobility
5. Supportive care to address cognitive and vision impairments
6. Dialysis or kidney transplantation in cases of advanced kidney disease

The prognosis for individuals with hyperargininemia varies depending on the severity of the disorder and the presence of any additional medical conditions. With appropriate management, many individuals with hyperargininemia are able to lead active and fulfilling lives. However, the disorder can be life-threatening in some cases, particularly if left untreated or if complications arise.

... deficiency typically refers to decreased function of arginase I, the liver isoform of arginase. This deficiency is ... Arginase belong to the ureohydrolase family of enzymes. Arginase catalyzes the fifth and final step in the urea cycle, a series ... Specifically, arginase converts L-arginine into L-ornithine and urea. Mammalian arginase is active as a trimer, but some ... Arginase at the US National Library of Medicine Medical Subject Headings (MeSH) GeneReviews/NIH/NCBI/UW entry on Arginase ...
... urea Arginase Nadai Y (1958). "Arginase. II. Distribution and properties of D-arginase". J. Biochem. 45: 1011-1020. D-arginase ... D-arginase (EC 3.5.3.10) is an enzyme with systematic name D-arginine amidinohydrolase. This enzyme catalyses the following ...
... arginase; several phosphatases and phosphoesterases-that includes two bridging carboxylate ligands and a bridging water or ...
In people with arginase deficiency, arginase is missing, and arginine is not broken down properly. consequently, urea cannot be ... "Arginase Deficiency". GeneReviews. PMID 20301338. Retrieved 20 November 2016.update 2014 "Arginase Deficiency: Background, ... The ARG1 gene provides instructions for making an enzyme called arginase, this enzyme controls the last steps of the urea cycle ... "arginase deficiency". Genetics Home Reference. Retrieved 20 November 2016. Hames, David; Hooper, Nigel (2005). Instant Notes in ...
Waddington SN (2002). "Arginase in glomerulonephritis". Kidney Int. 61 (3): 876-81. doi:10.1046/j.1523-1755.2002.00236.x. PMID ...
Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exist (types I ... Jiang M, Ding Y, Su Y, Hu X, Li J, Zhang Z (December 2006). "Arginase-flotillin interaction brings arginase to red blood cell ... "Androgen-regulated expression of arginase 1, arginase 2 and interleukin-8 in human prostate cancer". PLOS ONE. 5 (8): e12107. ... "Entrez Gene: Arginase, liver". [provided by RefSeq, Sep 2011] Human ARG1 genome location and ARG1 gene details page in the UCSC ...
Arginase and urea synthesis". The Journal of Biological Chemistry. 184 (2): 479-484. doi:10.1016/S0021-9258(19)50977-2. PMID ...
"Arginase formulations and methods". Wipo (PCT). WO (8495A2). 2011. Ryan, Sinéad M; Mantovani, Giuseppe; Wang, Xuexuan; ...
Arginase, type II is an arginase protein that in humans is encoded by the ARG2 gene. Arginase catalyzes the hydrolysis of ... "Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide ... "Species differences in expression pattern of arginase isoenzymes and differential effects of arginase inhibition on collagen ... "Entrez Gene: Arginase, type II". Human ARG2 genome location and ARG2 gene details page in the UCSC Genome Browser. ...
Genetic disruption of arginase-2 in mouse attenuates the onset of senescence and extends lifespan. Arginase inhibitors have ... Arginase-II deficiency extends lifespan in mice. Frontiers in physiology, 8, 682. PMID 28943853 PMC 5596098 doi:10.3389/fphys. ...
It can also inhibit arginase, an enzyme that competes with NO synthase for arginine. The resulting increase in the ... Huynh, Ngan Ngoc; Chin-Dusting, Jaye (2006). "Amino Acids, Arginase and Nitric Oxide in Vascular Health". Clinical and ...
Cleavage by arginase also produces canaline, a potent insecticide. The toxicity of canavanine may be enhanced under conditions ...
"Enhancer-mediated control of macrophage-specific arginase I expression". Journal of Immunology. 172 (12): 7565-73. doi:10.4049/ ...
Evidence of boronic acid mimics as transition state analogue inhibitors of human arginase I was elucidated by x-ray crystal ... Among the synthesized analogues, R = L-Leu possesses the most potent inhibitory activity (Ki = 9.1 nM). Arginase is a binuclear ... Maarsingh H, Zaagsma J, Meurs H (October 2009). "Arginase: a key enzyme in the pathophysiology of allergic asthma opening novel ... "Design of amino acid sulfonamides as transition-state analogue inhibitors of arginase". Journal of the American Chemical ...
Arginine is cleaved by arginase to form urea and ornithine. The ornithine is then transported back to the mitochondria to begin ... Deficiency of arginase) Hyperornithinemia, hyperammonemia, homocitrullinuria (HHH) syndrome (Deficiency of the mitochondrial ... synthetase I OTC Ornithine transcarbamoylase ASS argininosuccinate synthetase ASL argininosuccinate lyase ARG1 arginase 1 ...
"Pirfenidone inhibits lung allograft fibrosis through L-arginine-arginase pathway". Am. J. Transplant. 5 (6): 1256-63. doi: ...
2007). "Arginase-flotillin interaction brings arginase to red blood cell membrane". FEBS Lett. 580 (28-29): 6561-4. doi:10.1016 ...
Arginase, which catalyses the conversion of arginine to urea and ornithine, is one of the five members of the urea cycle ... There are several arginase isozymes that differ in catalytic, molecular and immunological properties. Deficiency in the liver ... Baker BS, Tata JR, Xu Q (1993). "Developmental and hormonal regulation of the Xenopus liver-type arginase gene". Eur. J. ... The ureohydrolase superfamily includes arginase (EC 3.5.3.1), agmatinase (EC 3.5.3.11), formiminoglutamase (EC 3.5.3.8) and ...
They also promote extracellular matrix synthesis via production of ornithine, via arginase; this is used as a precursor for ...
EDTA also acts as a selective inhibitor against dNTP hydrolyzing enzymes (Taq polymerase, dUTPase, MutT), liver arginase and ... "Non-chelating inhibition of the H101N variant of human liver arginase by EDTA". Journal of Inorganic Biochemistry. 98 (8): 1465 ...
Other enzymes containing manganese are arginase and Mn-containing superoxide dismutase (Mn-SOD). Also the enzyme class of ...
Other enzymes containing manganese are arginase and Mn-containing superoxide dismutase (Mn-SOD). Also the enzyme class of ...
Leopoldini M, Russo N, Toscano M (August 2009). "Determination of the catalytic pathway of a manganese arginase enzyme through ...
The Effect of Variation in Dietary Protein upon the Hepatic Arginase of the Rat". Biochemical Journal. 51 (5): 681-686. doi: ...
... arginase, a bimetallic enzyme binuclear Mn2-metalloenzyme arginase, crucial for pathogenesis of the ... Arginase of H. pylori also plays a role in evasion of the pathogen from the host immune system mainly by various proposed ... George G, Kombrabail M, Raninga N, Sau AK (March 2017). "Arginase of Helicobacter Gastric Pathogens Uses a Unique Set of Non- ... mechanisms, arginase competes with host-inducible nitric oxide (NO) synthase for the common substrate L-arginine, and thus ...
M2 macrophages activate arginase 1 (Arg1) that blocks iNOS activity and therefore inhibits nitric oxide production. They also ...
Mregs do not contribute to the production of extracellular matrix because they express low levels of arginase. Mregs show up- ... Mregs also differ from alternatively activated macrophages by producing high levels of nitric oxide and low arginase activity. ... Mregs can also inhibit the arginase activity of alternatively activated macrophages, the proliferation of fibroblasts, and can ...
Arginase deficiency Citrullinemia N-acetylglutamate synthetase deficiency Ornithine translocase deficiency Carbamoyl phosphate ...
L-Ornithine is one of the products of the action of the enzyme arginase on L-arginine, creating urea. Therefore, ornithine is a ...
The compound is found in legumes that contain canavanine, from which it is produced by the action of arginase. The most common- ...
Arginase deficiency is an inherited disorder that causes the amino acid arginine (a building block of proteins) and ammonia to ... In people with arginase deficiency, arginase is damaged or missing, and arginine is not broken down properly. As a result, urea ... Mutations in the ARG1 gene cause arginase deficiency.. Arginase deficiency belongs to a class of genetic diseases called urea ... Arginase deficiency usually becomes evident by about the age of 3. It most often appears as stiffness, especially in the legs, ...
Arginase deficiency is an inherited disorder that causes the amino acid arginine (a building block of proteins) and ammonia to ... In people with arginase deficiency, arginase is damaged or missing, and arginine is not broken down properly. As a result, urea ... Mutations in the ARG1 gene cause arginase deficiency.. Arginase deficiency belongs to a class of genetic diseases called urea ... Arginase deficiency usually becomes evident by about the age of 3. It most often appears as stiffness, especially in the legs, ...
T cell intrinsic role of Arginase 2 in modulating anti-tumor immunity. Add to your list(s) Download to your calendar using vCal ... University of Cambridge , Talks.cam , Immunology in Pathology , T cell intrinsic role of Arginase 2 in modulating anti-tumor ...
Cattle rumen tissue arginase contains only one isoenzyme. Arginase isolated from cattle rumen tissue may be arginase A_4 or A_2 ... The enzyme lost 50% of total activity in 9 days at -30 ºC (in the freezer). The presence of a single anionic form of arginase ... The molecular weight of native arginase, estimated by gel filtration on a Sephadex G-150 column, was 122 500 ± 2500 and those ... The arginase was partially purified from cattle rumen tissue and its properties were investigated and thereafter compared with ...
Arginase, most commonly derived from mammalian sources, has been most often used. However, arginase has failed to inhibit NO ... and was able to lower arginine levels to a much greater extent than arginase. ADI, unlike arginase, was effective in lowering ... ADI had more than 1000 fold higher affinity for arginine (Km ~ 30 µM for ADI vs ~45 mM for arginase), ... Therefore, a systematic biochemical characterization of arginase and arginine deiminase (ADI) derived from M. Hominus was ...
Arginase-1 Antibody. Arginase-1, encoded by the ARG1 gene, is a cytosolic metalloenzyme expressed predominantly in hepatocytes ... Anti-Arginase-1 is highly specific for hepatocytes, and is therefore a sensitive and specific marker of benign and malignant ... AntibodyCD44 AntibodyCD5 AntibodyCD2 AntibodyBSEP AntibodyArginase-1 AntibodyAnnexin A1 AntibodyCA-125 Antibody ...
Human arginase I: a potential broad-spectrum anti-cancer agent *J. Anakha ... Angiotensin II-induced arterial thickening, fibrosis and stiffening involves elevated arginase function. PLoS ONE 10, e0121727 ... and metabolized by arginase 1 to produce urea and ornithine. Ornithine is a precursor for the biosynthesis of polyamines and ...
Limiting arginase activity is a possible therapeutic means of controlling obesity-induced vascular and VAT inflammation. ... Obesity-induced vascular inflammation involves elevated arginase activity.. Yao, Lin; Bhatta, Anil; Xu, Zhimin; Chen, Jijun; ... Arginase/metabolismo Gordura Intra-Abdominal/metabolismo Obesidade/complicações Adipócitos/metabolismo Adipócitos/patologia ... Our previous studies showed that arginase 1 (A1) in endothelial cells (ECs) is critically involved in obesity-induced vascular ...
Arginase inhibition supports survival and differentiation of neuronal precursors in adult Alzheimers disease mice ... Our previous results indicated a potential effect of arginase inhibition, with norvaline, on various aspects of neurogenesis in ... To better evaluate this effect, we chronically administered an arginase inhibitor, norvaline, to triple-transgenic and wild- ... Source URL: http://alzped.nia.nih.gov/arginase-inhibition-supports ...
arginase deficiency * exposure to the measles * exposure to the chickenpox * muscle pain or tenderness with increase creatine ...
Arginase (ARG), an enzyme implicated in many cardiovascular diseases, can compete with nitric oxide (NO) synthase for their ... Arginase (ARG), an enzyme implicated in many cardiovascular diseases, can compete with nitric oxide (NO) synthase for their ... Arginase (ARG), an enzyme implicated in many cardiovascular diseases, can compete with nitric oxide (NO) synthase for their ... Arginase (ARG), an enzyme implicated in many cardiovascular diseases, can compete with nitric oxide (NO) synthase for their ...
De Santo C, Cheng P, Beggs A, Egan S, Bessudo A, Mussai F. Metabolic therapy with PEG-arginase induces a sustained complete ... De Santo, C., Cheng, P., Beggs, A., Egan, S., Bessudo, A., & Mussai, F. (2018). Metabolic therapy with PEG-arginase induces a ... De Santo, C, Cheng, P, Beggs, A, Egan, S, Bessudo, A & Mussai, F 2018, Metabolic therapy with PEG-arginase induces a sustained ... keywords = "Arginase , Melanoma , Immunotherapy , Metabolism , BCT-100",. author = "{De Santo}, Carmela and Paul Cheng and ...
Arginase competes with eNOS for L-arginine and has been implicated in the endothelial dysfunction. NIH investigators have ... Level of arginase activity in peritoneal macrophages isolated from the transgenic mice also was also unchanged. However, ArgII ... Useful to study the role of arginase II gene in endothelium.. *Useful for testing the drugs for treatment of the endothelial ... Transgenic Mice Expressing Human Arginase II Gene in Endothelium: Useful for Studying Atherosclerosis and Other Vasculopathies ...
... or arginase (ARG). ... ARG = arginase deficiency;. THN = transient hyperammonemia of ...
MCTR3 reprograms arthritic monocytes to upregulate Arginase-1 and exert pro-resolving and tissue-protective functions in ...
arginase 2. involved_in. IEA. ISO. GO_REF:0000107. (PMID:28614294). (MGI:5908771,PMID:27074721). Ensembl. RGD. PMID:27074721 ...
An arginase inhibitor, OAT-1746, protected the heart against bortezomib- or MM-induced toxicity but did not completely prevent ... Arginase Inhibition Mitigates Bortezomib-Exacerbated Cardiotoxicity in Multiple Myeloma by Aleksandra Paterek ... Objective: Since MM is associated with increased arginase expression, resulting in the consumption of ʟ-arginine, precursor for ... Conclusions: Bortezomib exacerbates MM-mediated LV systolic dysfunction in a mouse model of MM, while an arginase inhibitor ...
Arginase. 3.5.3.1. P05089. P78540. Citrullinemia type II. CIT-II. Secondary. 30529005 ...
... arginase 1 (ARG1), microRNA 122 (miR-122), and glutamate dehydrogenase. Skeletal muscle injury was evaluated with fatty acid ...
Moretto, J., Girard, C., and Demougeot, C. (2019). The role of arginase in aging: a systematic review. Exp. Gerontol. 116, 54- ...
MeSH Terms: Animals; Arginase/metabolism; Astrocytes/metabolism*; Brain/metabolism; Cells, Cultured; Chemotaxis/physiology*; ... and an increase in the antioxidant genes Arginase-1 and Nrf2. Overexpression of PK2 in primary astrocytes or in the in vivo ... induced the A2 astrocytic phenotype with upregulation of key protective genes and A2 reactivity markers including Arginase-1 ...
arginase 1; ornt1. = ornithine transporter; oat. = ornithine aminotransferase; p5cs. = Δ1-pyrroline-5-carboxylate synthetase; ...
5. [Arginase as a marker of cancerogenesis. III. Comparison of arginase activity with CEA and Ca 19-9 in liver metastases of ... 2. [Arginase as a marker of cancerogenesis. I. Monitoring patients after resection of colorectal cancer].. Porembska Z; ... 6. [Serum arginase activity in patients with liver cirrhosis and hepatocellular carcinoma].. Chrzanowska A; Mielczarek-Puta M; ... 3. [Arginase a marker of cancerogenesis. II. Monitoring of patients after resection of colorectal liver metastases].. Porembska ...
ARG1: arginase 1 (6q23.2). *BCKDHB: branched-chain keto acid dehydrogenase E1, beta polypeptide (maple syrup urine disease) ( ...
Antibodies for proteins involved in response to mercury ion pathways, according to their Panther/Gene Ontology Classification
  • Obesity-induced vascular inflammation involves elevated arginase activity. (bvsalud.org)
  • Mutations in the ARG1 gene cause arginase deficiency. (medlineplus.gov)
  • The ARG1 gene provides instructions for making an enzyme called arginase. (medlineplus.gov)
  • Arginase-1, encoded by the ARG1 gene, is a cytosolic metalloenzyme expressed predominantly in hepatocytes which plays a key role in the urea cycle by catalyzing the hydrolysis of arginine to ornithine and urea. (femtopath.com)
  • In addition to classical biomarkers, liver injury was assessed by cytokeratin 18 (CK18) cleaved form, high-mobility group box 1, arginase 1 (ARG1), microRNA 122 (miR-122), and glutamate dehydrogenase. (nih.gov)
  • These effects of HFHS, except for weight gain and hyperglycemia , were prevented or reduced in mice lacking EC-A1 or treated with the arginase inhibitor 2-(S)-amino-6-boronohexanoic acid (ABH). (bvsalud.org)
  • To better evaluate this effect, we chronically administered an arginase inhibitor, norvaline, to triple-transgenic and wild-type mice, and applied an advanced immunohistochemistry approach with several biomarkers and bright-field microscopy. (nih.gov)
  • The molecular weight of native arginase, estimated by gel filtration on a Sephadex G-150 column, was 122 500 ± 2500 and those of subunits of the enzyme, estimated by SDS-PAGE and gel filtration on a Sephadex G-100 column, were 44 000 ± 1000 and 34 500 ± 500. (tubitak.gov.tr)
  • Results: Arginase was found to have an alkaline pH optima(~9.5) with little enzyme activity at physiological pH. (medscimonit.com)
  • Arginase (ARG), an enzyme implicated in many cardiovascular diseases, can compete with nitric oxide (NO) synthase for their common substrate, L-arginine. (elsevierpure.com)
  • They have shown for the first time in a mouse model of tough-to-treat optic nerve trauma, that removing the enzyme arginase 2, which increases with injury, decreases neuron death in the retina as well as the degeneration of nerve fibers that connect neurons to each other and ultimately the brain. (nih.gov)
  • Arginase deficiency is an inherited disorder that causes the amino acid arginine (a building block of proteins) and ammonia to accumulate gradually in the blood. (medlineplus.gov)
  • Arginase deficiency usually becomes evident by about the age of 3. (medlineplus.gov)
  • In some affected individuals, signs and symptoms of arginase deficiency may be less severe, and may not appear until later in life. (medlineplus.gov)
  • Arginase deficiency belongs to a class of genetic diseases called urea cycle disorders. (medlineplus.gov)
  • In people with arginase deficiency, arginase is damaged or missing, and arginine is not broken down properly. (medlineplus.gov)
  • The accumulation of ammonia and arginine are believed to cause the neurological problems and other signs and symptoms of arginase deficiency. (medlineplus.gov)
  • Hyperargininemia due to liver arginase deficiency. (medlineplus.gov)
  • Sun A, Crombez EA, Wong D. Arginase Deficiency. (medlineplus.gov)
  • examine the neurological changes associated with hyperargininemia using an arginase-1-deficient mouse. (jci.org)
  • Silica exposure induces arginase I expression in rat lung. (cdc.gov)
  • For instance, in non-cancerous cells arginine is synthesized in cells from citrulline via argininosuccinate synthase 1 (ASS1) and argininosuccinate lyase in the urea cycle 8 , and metabolized by arginase 1 to produce urea and ornithine. (nature.com)
  • Increased arginase can also provide ornithine for synthesis of polyamines via ornithine decarboxylase (ODC) and proline/collagen via ornithine aminotransferase (OAT), leading to vascular cell proliferation and collagen formation, respectively.We hypothesized that elevated arginase activity is involved in Ang II-induced arterial thickening, fibrosis, and stiffness and that limiting its activity can prevent these changes. (elsevierpure.com)
  • Anti-Arginase-1 is highly specific for hepatocytes, and is therefore a sensitive and specific marker of benign and malignant hepatic tumors. (femtopath.com)
  • They find that dysmyelination occurs shortly after birth but can be corrected by restoring hepatic arginase-1 via adeno-associated virus-mediated gene delivery, suggested a potential therapeutic approach that merits further study. (jci.org)
  • Comparison of arginase activity with CEA and Ca 19-9 in liver metastases of colorectal cancer]. (nih.gov)
  • 6. [Serum arginase activity in patients with liver cirrhosis and hepatocellular carcinoma]. (nih.gov)
  • Manganese is a cofactor for many enzymes, including manganese superoxide dismutase, arginase, and pyruvate carboxylase [ 1 , 2 ]. (nih.gov)
  • Better model system to study functional significance of arginase II. (nih.gov)
  • 4. L-arginine as a factor increasing arginase significance in diagnosis of primary and metastatic colorectal cancer. (nih.gov)
  • The arginase was partially purified from cattle rumen tissue and its properties were investigated and thereafter compared with those of other tissue arginases. (tubitak.gov.tr)
  • The presence of a single anionic form of arginase in cattle rumen tissue was demonstrated by DEAE-sephacel chromatography. (tubitak.gov.tr)
  • Cattle rumen tissue arginase contains only one isoenzyme. (tubitak.gov.tr)
  • Arginase isolated from cattle rumen tissue may be arginase A_4 or A_2 form when it is compared with those of other tissue arginase isoenzymes. (tubitak.gov.tr)
  • ADI, unlike arginase, was effective in lowering extracellular arginine in tissue culture media and inhibit NO production by the murine macrophage cell line N-9 in response to gamma interferon and LPS stimulation. (medscimonit.com)
  • MCTR3 reprograms arthritic monocytes to upregulate Arginase-1 and exert pro-resolving and tissue-protective functions in experimental arthritis. (logosbio.com)
  • This was accompanied by increased arginase activity and A1 expression in vascular ECs and increased expression of tumor necrosis factor -α (TNF-α), monocyte chemoattractant protein-1 (MCP-1), interleukin-10 ( IL-10 ), vascular cell adhesion molecule-1 ( VCAM-1 ), and intercellular adhesion molecule-1 ( ICAM-1 ) mRNA and protein in both VAT and ECs. (bvsalud.org)
  • Limiting arginase activity is a possible therapeutic means of controlling obesity -induced vascular and VAT inflammation . (bvsalud.org)
  • Level of arginase activity in peritoneal macrophages isolated from the transgenic mice also was also unchanged. (nih.gov)
  • 1. Serum arginase activity in postsurgical monitoring of patients with colorectal carcinoma. (nih.gov)
  • Our previous results indicated a potential effect of arginase inhibition, with norvaline, on various aspects of neurogenesis in triple-transgenic mice. (nih.gov)
  • Our previous studies showed that arginase 1 (A1) in endothelial cells (ECs) is critically involved in obesity -induced vascular dysfunction. (bvsalud.org)
  • Useful to study the role of arginase II gene in endothelium. (nih.gov)
  • The cover image shows restoration of basal dendritic arbors of layer V pyramidal tract neurons in an AAV-treated arginase-1-deficient mouse. (jci.org)
  • ADI had more than 1000 fold higher affinity for arginine (Km ~ 30 µM for ADI vs ~45 mM for arginase), and was able to lower arginine levels to a much greater extent than arginase. (medscimonit.com)
  • Material/Methods: The murine macrophage cell line N-9 was treated with either arginase or arginine deiminase to determine the effect on intracellular and extracellular arginine and nitric oxide production. (medscimonit.com)
  • In people with arginase deficiency, arginase is damaged or missing, and arginine is not broken down properly. (medlineplus.gov)
  • People with arginase deficiency may also have developmental delay, loss of developmental milestones, and intellectual disability. (nih.gov)
  • People with Arginase deficiency may be placed on a very low-protein diet with the help of a registered metabolic dietitian. (nih.gov)
  • Arginase deficiency belongs to a class of genetic diseases called urea cycle disorders. (medlineplus.gov)
  • Arginase deficiency usually becomes evident by about the age of 3. (medlineplus.gov)
  • If untreated, arginase deficiency usually progresses to severe spasticity, loss of ambulation, complete loss of bowel and bladder control, and severe intellectual disability. (nih.gov)
  • Restoring Ureagenesis in Hepatocytes by CRISPR/Cas9-mediated Genomic Addition to Arginase-deficient Induced Pluripotent Stem Cells. (medscape.com)
  • Arginase competes with eNOS for L-arginine and has been implicated in the endothelial dysfunction. (nih.gov)
  • Arginase competes with NOS for L-arginine to produce urea and ornithine , limiting NO production . (bvsalud.org)
  • Our previous results indicated a potential effect of arginase inhibition, with norvaline, on various aspects of neurogenesis in triple-transgenic mice. (nih.gov)
  • Furthermore, AGEs impair vascular function that can be reversed by arginase inhibition. (bvsalud.org)
  • Arginase deficiency in untreated individuals is characterized by episodic hyperammonemia of variable degree that is infrequently severe enough to be life threatening or to cause death. (nih.gov)
  • Therefore, AGEs may be pivotal in arginase deleterious effects in diabetic VD, providing a novel therapeutic target. (bvsalud.org)
  • Rescue of the Functional Alterations of Motor Cortical Circuits in Arginase Deficiency by Neonatal Gene Therapy. (medscape.com)
  • Useful to study the role of arginase II gene in endothelium. (nih.gov)
  • Interestingly, blood cell gene expression in the apoE-/- fed 60% fat showed an 11-fold increase in arginase II (AII) and no increase in arginase I (AI). (cdc.gov)
  • Increased arginase gene expression in the blood and tissue (apoE-/- only) are likely associated with the development of atherosclerosis. (cdc.gov)
  • Arginase deficiency is an inherited disorder that causes the amino acid arginine (a building block of proteins) and ammonia to accumulate gradually in the blood. (medlineplus.gov)
  • As stated previously, plasma arginine levels can be low under conditions of stress, for example following surgery, when this amino acid is excessively catabolized by arginase. (medscape.com)
  • High levels of LDH appear to indirectly indicate that two other proteins, hemoglobin and arginase, have broken out of red blood cells. (nih.gov)
  • Arginase deficiency is a genetic disease, which means that it is caused by one or more genes not working correctly. (nih.gov)
  • In conclusion, AGEs increase arginase activity probably through the ERK1/2/ p38 MAPK pathway due to increased arginase I expression. (bvsalud.org)
  • In conclusion, increased circulating arginase activity and reduced arginine are likely the result of liver and/ or tissue injury. (cdc.gov)
  • Therefore we studied systemic changes in arginase and arginine metabolism in a model of atherosclerosis. (cdc.gov)
  • however, AGEs' role in arginase regulation is unknown. (bvsalud.org)
  • In some affected individuals, signs and symptoms of arginase deficiency may be less severe, and may not appear until later in life. (medlineplus.gov)
  • The accumulation of ammonia and arginine are believed to cause the neurological problems and other signs and symptoms of arginase deficiency. (medlineplus.gov)
  • The human arginases and arginase deficiency. (medscape.com)
  • 6. Arginase in human urogenital tumors. (nih.gov)
  • Arginase deficiency with lethal neonatal expression: evidence for the glutamine hypothesis of cerebral edema. (medscape.com)
  • Immunodetection of arginase revealed MGA-induced protein expression for arginase I. In aortic rings, MGA pretreatment impaired acetylcholine (ACh)-induced vasorelaxation , which was reversed by ABH. (bvsalud.org)
  • Better model system to study functional significance of arginase II. (nih.gov)