The protein encoded by this gene is a member of the epidermal growth factor family. It is an autocrine growth factor as well as a mitogen for astrocytes, Schwann cells and fibroblasts. It is related to epidermal growth factor (EGF) and transforming growth factor alpha (TGF-alpha). The protein interacts with an the EGF/TGF-alpha receptor to promote the growth of normal epithelial cells, and it inhibits the growth of certain aggressive carcinoma cell lines. It also functions in mammary gland, oocyte and bone tissue development. This gene is associated with an a psoriasis-like skin phenotype, and is also associated with an other pathological disorders, including various types of cancers and inflammatory conditions.
GTP-binding protein involved in protein trafficking, regulates endocytic recycling and cytoskeleton remodeling. May modulate vesicle budding and uncoating within the Golgi apparatus. Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in the regulation of dendritic spine development (By similarity). Contributes to the regulation of dendritic branching and filopodia extension.
ARG1 is a member of the ureohydrolase family of enzymes. ARG1 can catalyze the hydrolysis of arginine to ornithine and urea. In the urea cycle, ARG1 catalyzes the fifth and final step, a series of biochemical reactions in mammals during which the body disposes of harmful ammonia. ARG1 is a cytosolic enzyme and expressed widely in the liver as part of the urea cycle. Inherited deficiency of this ARG1 causes argininemia, which is an autosomal recessive disorder characterized by hyperammonemia.
Arginase is the focal enzyme of the urea cycle hydrolysing L-arginine to urea and L-ornithine. Emerging studies have identified arginase in the vasculature and have implicated this enzyme in the regulation of nitric oxide (NO) synthesis and the development of vascular disease. Arginase also redirects the metabolism of L-arginine to L-ornithine and the formation of polyamines and L-proline, which are essential for smooth muscle cell growth and collagen synthesis. Arginase is encoded by two recently discovered genes (Arginase I and Arginase II). In most mammals, Arginase 1 (ARG1) also known as Arginase, liver, which functions in the urea cycle, and is located primarily in the cytoplasm of the liver. The second isozyme, Arginase II, has been implicated in the regulation of the arginine/ornithine concentrations in the cell. It is located in mitochondria of several tissues in the body, with most abundance in the kidney and prostate. It may be found at lower levels in macrophages, lactating mammary glands, and brain.
Arginase 1, also known as liver arginase, is a binuclear manganese metalloenzyme. It is a key enzyme of the urea cycle that catalyses the conversion of L-arginine into L-ornithine and urea, the final cytosolic reaction of urea formation in the mammalian liver. Arginase 1 is abundantly expressed in liver, but it is also expressed in cells and tissues that lack a complete urea cycle, including lung. Arginase is a critical regulator of nitric oxide synthesis and vascular function. It is implicated in a variety of human diseases including vascular disease, pulmonary disease, infectious disease, immune cell function and cancer. In humans, hereditary defects in arginase result in an accumulation of arginine in the blood known as hyperarginemia. Arginase deficiency can also result in the accumulation of nitrogen in the form of ammonia, which results in hyperammonemia.
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