ARG1
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Official Full Name
arginase 1
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Overview
Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exist (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type I isoform encoded by this gene, is a cytosolic enzyme and expressed predominantly in the liver as a component of the urea cycle. Inherited deficiency of this enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2011] -
Synonyms
ARG1; arginase 1; arginase-1; arginase, liver; type I arginase; liver-type arginase;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Native Proteins
- Human
- Mouse
- Rabbit
- Rat
- Vigna radiata var. radiata (Mung bean) (Phaseolus aureus)
- Zebrafish
- E. coli
- E.coli
- E.coli expression system
- E.Coli or Yeast
- HEK293
- HEK293T
- Human Cell
- In Vitro Cell Free System
- Mammalian Cell
- Mammalian cells
- Rat Liver
- Wheat Germ
- Yeast
- C
- His
- Flag
- GST
- His (Fc)
- Avi
- His|Myc
- SUMO
- Myc
- DDK
- MYC
- Myc|DDK
- N/A
- N
- Involved Pathway
- Protein Function
- Interacting Protein
- ARG1 Related Articles
- ARG1 Related Research Area
ARG1 involved in several pathways and played different roles in them. We selected most pathways ARG1 participated on our site, such as Arginine biosynthesis, Arginine and proline metabolism, Metabolic pathways, which may be useful for your reference. Also, other proteins which involved in the same pathway with ARG1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Arginine biosynthesis | ASL;GLS;GLUD2;GOT2B;GLS2;CPS1;NAGS;GLUL;OTC |
Arginine and proline metabolism | NOS2A;SAT2;ADC;ALDH9A1A.1;PYCR1A;GAMT;DAO.3;PRODH2;PYCR2 |
Metabolic pathways | GULO;AGPAT4;ALPI;G6PCA.2;GPT2L;ARSB;AADAT;ADKA;NT5C |
Biosynthesis of amino acids | TKTL1;PSAT1;GLULC;TKT;NAGS;ALDOAB;GM5506;AADAT;IDH3G |
Amoebiasis | C9;TLR2;SERPINB9;MUC2;COL4A5;CD1D;Itgam&Itgb2;RAB5C;SERPINB2 |
ARG1 has several biochemical functions, for example, arginase activity, manganese ion binding. Some of the functions are cooperated with other proteins, some of the functions could acted by ARG1 itself. We selected most functions ARG1 had, and list some proteins which have the same functions with ARG1. You can find most of the proteins on our site.
Function | Related Protein |
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arginase activity | ARG2;ARG1 |
manganese ion binding | B4GALT7;DCP2;ABL2;FEN1;MTPAP;GALNT2;GLUL;PAPOLA;ABL1 |
ARG1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ARG1 here. Most of them are supplied by our site. Hope this information will be useful for your research of ARG1.
abh; bec; ESR1; FLOT1; USP53; ATG101; ALDH4A1; midostaurin; GABARAP; MYC; GABARAPL2
- Q&As
- Reviews
Q&As (17)
Ask a questionYes, there is evidence linking ARG1 to metabolic disorders. Argininemia, a disorder caused by ARG1 deficiency, is characterized by disturbances in arginine metabolism. Additionally, dysregulated ARG1 activity has been observed in conditions such as obesity, insulin resistance, and non-alcoholic fatty liver disease (NAFLD). ARG1-mediated alterations in arginine metabolism can impact nitric oxide production, urea cycle function, and other pathways involved in metabolic regulation.
Yes, certain natural substances and dietary factors have been shown to modulate ARG1 activity. For instance, polyphenols found in fruits and vegetables, such as quercetin and resveratrol, have been reported to inhibit ARG1 activity. Additionally, omega-3 fatty acids, present in fish oils, have been found to reduce ARG1 expression and activity in certain tissues.
Although the primary role of ARG1 is in arginine metabolism and urea production, studies have suggested potential links between ARG1 and brain health. For example, alterations in the arginine-ornithine-urea pathway have been observed in disorders like Alzheimer's disease, suggesting a possible involvement of ARG1. However, the mechanisms and implications of ARG1 in brain function and neurological disorders are still being explored.
Yes, mutations in the ARG1 gene can lead to a rare genetic disorder called argininemia. Argininemia is an autosomal recessive disorder characterized by the accumulation of arginine in the blood and tissues due to a deficiency of ARG1 activity. It can cause symptoms such as developmental delay, intellectual disability, seizures, and progressive neurological deterioration.
ARG1 has been implicated in various physiological processes beyond arginine metabolism and the urea cycle. It is involved in wound healing and tissue repair, where it promotes collagen production and fibroblast proliferation. Additionally, ARG1 has been linked to conditions such as asthma and chronic obstructive pulmonary disease (COPD), where increased ARG1 activity in the lungs may contribute to airway constriction and respiratory symptoms.
Yes, there are diseases associated with abnormal ARG1 activity. Argininemia is a rare genetic disorder characterized by a deficiency of ARG1 activity, leading to the accumulation of arginine in the blood and tissues. This can cause neurological impairments, developmental delays, and other symptoms. Additionally, altered ARG1 expression or activity has been implicated in conditions such as asthma, allergic inflammation, and certain types of cancer.
Yes, the function of ARG1 can be inhibited or blocked using specific inhibitors. Some compounds, such as Nω-hydroxy-L-arginine (NOHA) and S-(2-boronoethyl)-L-cysteine (BEC), have been found to selectively inhibit ARG1 activity. These inhibitors can be useful in studying the biological role of ARG1 and developing potential therapeutic strategies.
Yes, genetic variations or mutations in the ARG1 gene can alter its activity or function. In argininemia, for instance, mutations in the ARG1 gene lead to reduced or absent ARG1 activity, resulting in the accumulation of arginine. Similarly, other genetic variations may affect ARG1 expression levels, enzymatic activity, or stability, potentially influencing its role in various physiological processes and disease conditions.
Yes, ARG1 activity can be targeted for therapeutic interventions. In certain diseases, such as cancer and immune-mediated disorders, inhibiting ARG1 can be beneficial. By blocking ARG1 activity, the depletion of arginine can be prevented, allowing for enhanced T cell function and immune responses. Additionally, targeting ARG1 in MDSCs can alleviate immunosuppression and improve anti-tumor immunity. Several approaches, including small molecule inhibitors and immunotherapies, are being explored to modulate ARG1 activity for therapeutic purposes.
Yes, ARG1 is involved in wound healing and tissue repair processes. In certain immune cells, such as macrophages, ARG1 expression is upregulated during wound healing. ARG1-expressing macrophages contribute to tissue repair by promoting angiogenesis and collagen deposition. Additionally, ARG1-derived urea can support cell proliferation and tissue remodeling. However, the exact mechanisms and contributions of ARG1 in wound healing are still being studied.
Yes, there might be a link between ARG1 and cardiovascular diseases. Studies have suggested that ARG1 activity in blood vessels and endothelial cells may contribute to vascular dysfunction and hypertension. By modulating the availability of arginine and the production of nitric oxide, ARG1 can impact endothelial function and blood vessel dilation, which are important factors in cardiovascular health.
ARG1 can interact with various cellular pathways and proteins. One important interaction is between ARG1 and nitric oxide synthase (NOS), particularly inducible NOS (iNOS). ARG1 and iNOS compete for the common substrate arginine, and their activities can reciprocally regulate each other. The balance between ARG1 and iNOS activity is critical for the production of arginine-derived metabolites, such as urea and nitric oxide, which have diverse physiological effects.
Yes, there is ongoing research to develop drugs targeting ARG1. For example, in cancer immunotherapy, scientists are exploring the use of ARG1 inhibitors to enhance anti-tumor immune responses. By blocking ARG1 activity in tumor-associated immune cells, the aim is to alleviate immunosuppression and enhance the efficacy of immune checkpoint inhibitors or other cancer therapies.
Yes, there are pharmacological inhibitors of ARG1 that have been identified and are under investigation. Some examples include nor-NOHA (N-omega-hydroxy-nor-L-arginine) and BEC (Bis-2-(5-phenylacetamido-1,3,4-thiadiazol-2-yl)ethyl sulfide). These inhibitors have shown promising results in preclinical studies and are being evaluated for their potential in treating diseases associated with aberrant ARG1 activity.
Yes, ARG1 activity can be regulated by post-translational modifications, although the extent and significance of such modifications are still being investigated. For instance, phosphorylation of ARG1 on specific residues has been found to modulate its activity. Other post-translational modifications, such as acetylation and ubiquitination, may also influence ARG1 stability and function.
ARG1 is primarily expressed in the liver, although it can also be found in other tissues such as the kidneys, intestines, and immune cells, including macrophages. In these tissues, ARG1 plays a crucial role in regulating arginine metabolism and urea production.
Yes, certain natural compounds and dietary factors have been found to modulate ARG1 activity. For instance, polyphenols, such as quercetin and resveratrol, have been shown to inhibit ARG1 activity. Dietary factors like high-protein diets can also affect ARG1 expression and activity. However, more research is needed to fully understand the extent of these modulatory effects and their therapeutic implications.
Customer Reviews (8)
Write a reviewThey may offer educational resources such as technical guides, protocols, and application notes, which can aid researchers in understanding the principles, techniques, and potential applications of ARG1 protein in their studies.
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