Arginase 1/ARG1/liver Arginase Products

Description

Arginase 1 (ARG1), also known as liver arginase, is a metalloenzyme that is a member of the ureohydrolase superfamily and arginase family (1). ARG1 is known for its role in the urea cycle in catalyzing the conversion of L-arginine into urea and L-ornithine (1). Arginase has two distinct isoforms, with ARG1 being expressed primarily in the liver and ARG2 in extrahepatic tissues (1). Human ARG1 is synthesized as 322 amino acids (aa) in length with a theoretical molecular weight of 35 kDa (1,2). Three ARG1 monomers can form a highly active homotrimer of 105 kDa (1). A key structural feature of the arginase protein is the binuclear magnesium (Mn2+) ions at its core (1).

Arginase and nitric oxidase synthase (NOS) compete for the same L-arginine substrate, creating a delicate balance between pathways (1). Furthermore, bioavailability of L-arginine and ARG1 expression has been implicated in several pathologies including vascular disease, neuronal disease, cardiovascular disease, immune dysfunction, inflammation, and cancer (1,3-5). For instance, ARG1 functions as a macrophage marker, defining the M2 population, while inducible nitric oxide synthase (iNOS) characterizes the M1 population; impaired M1/M2 polarization and changes in ARG1 expression is observed in diseases such as arteriogenesis, asthma, pulmonary fibrosis, and inflammatory bowel disease (1,3). In humans, arginase deficiency, known as argininemia, is an autosomal recessive metabolic disorder characterized by elevated ammonia (hyperammonemia) levels and arginine accumulation (6). Given that many arginase-associated diseases are characterized by upregulation in expression of ARG1, ARG2, or both, arginase inhibitors are currently being studied as a potential therapeutic approach (1,4).

References

1. S Clemente, G., van Waarde, A., F Antunes, I., Domling, A., & H Elsinga, P. (2020). Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective. International Journal of Molecular Sciences. https://doi.org/10.3390/ijms21155291

2. Uniprot (P05089)

3. Kieler, M., Hofmann, M., & Schabbauer, G. (2021). More than just protein building blocks: How amino acids and related metabolic pathways fuel macrophage polarization. The FEBS Journal. Advance online publication. https://doi.org/10.1111/febs.15715

4. Shosha, E., Fouda, A. Y., Narayanan, S. P., Caldwell, R. W., & Caldwell, R. B. (2020). Is the Arginase Pathway a Novel Therapeutic Avenue for Diabetic Retinopathy?. Journal of Clinical Medicine. https://doi.org/10.3390/jcm9020425

5. Correale J. (2021). Immunosuppressive Amino-Acid Catabolizing Enzymes in Multiple Sclerosis. Frontiers in Immunology. https://doi.org/10.3389/fimmu.2020.600428

6. Morales, J. A., & Sticco, K. L. (2020). Arginase Deficiency. In StatPearls. StatPearls Publishing.

Bioinformatics

Entrez	11846 Mouse 29221 Rat 383 Human
Uniprot	AAH05321 Human AAH20653.1 Human NM_000045 Human NP_000036 Human NP_000036.2 Human P05089 Human P07824 Rat
Product By Gene ID	383
Alternate Names	ARG1 arginase 1 arginase, liver arginase-1 arginase-1 EC 3.5.3.1 EC:3.5.3.1 Liver-type arginase Type I arginase

Research Areas for Arginase 1/ARG1/liver Arginase

Find related products by research area and learn more about each of the different research areas below.

Cancer
Cellular Markers
Chromatin Research
Lipid and Metabolism