ARG1 (gene): Difference between revisions
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{{Infobox_gene}} | {{Infobox_gene}} | ||
The human '''ARG1''' [[gene]] encodes the [[protein]] '''arginase'''.<ref name="entrez">{{cite web | title = Entrez Gene: Arginase, liver | url = https://www.ncbi.nlm.nih.gov/gene/383 }}</ref> | |||
== Function == | |||
==Function== | |||
[[Arginase]] [[Catalyst|catalyzes]] the [[hydrolysis]] of [[arginine]] to [[ornithine]] and [[urea]]. At least two [[isoform]]s of [[mammal]]ian arginase exist (types I and II) which differ in their [[Tissue (biology)|tissue]] distribution, subcellular localization, [[Immunology|immunologic]] crossreactivity and [[Physiology|physiologic]] function. The type I isoform encoded by this gene, is a [[cytosol]]ic 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 [[Transcription (genetics)|transcript]] variants encoding different isoforms have been found for this gene.<ref>[provided by RefSeq, Sep 2011]</ref> | [[Arginase]] [[Catalyst|catalyzes]] the [[hydrolysis]] of [[arginine]] to [[ornithine]] and [[urea]]. At least two [[isoform]]s of [[mammal]]ian arginase exist (types I and II) which differ in their [[Tissue (biology)|tissue]] distribution, subcellular localization, [[Immunology|immunologic]] crossreactivity and [[Physiology|physiologic]] function. The type I isoform encoded by this gene, is a [[cytosol]]ic 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 [[Transcription (genetics)|transcript]] variants encoding different isoforms have been found for this gene.<ref>[provided by RefSeq, Sep 2011]</ref> | ||
== References == | == References == | ||
{{reflist}} | {{reflist}} | ||
==External links== | == External links == | ||
* {{UCSC gene info|ARG1}} | * {{UCSC gene info|ARG1}} | ||
== Further reading == | == Further reading == | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
*{{ | * {{cite journal | vauthors = Morris CR, Kato GJ, Poljakovic M, Wang X, Blackwelder WC, Sachdev V, Hazen SL, Vichinsky EP, Morris SM, Gladwin MT | title = Dysregulated arginine metabolism, hemolysis-associated pulmonary hypertension, and mortality in sickle cell disease | journal = JAMA | volume = 294 | issue = 1 | pages = 81–90 | date = July 2005 | pmid = 15998894 | pmc = 2065861 | doi = 10.1001/jama.294.1.81 }} | ||
| | * {{cite journal | vauthors = Jiang M, Ding Y, Su Y, Hu X, Li J, Zhang Z | title = Arginase-flotillin interaction brings arginase to red blood cell membrane | journal = FEBS Letters | volume = 580 | issue = 28–29 | pages = 6561–4 | date = December 2006 | pmid = 17113085 | pmc = | doi = 10.1016/j.febslet.2006.11.003 }} | ||
* {{cite journal | vauthors = Morris SM | title = Recent advances in arginine metabolism: roles and regulation of the arginases | journal = British Journal of Pharmacology | volume = 157 | issue = 6 | pages = 922–30 | date = July 2009 | pmid = 19508396 | pmc = 2737650 | doi = 10.1111/j.1476-5381.2009.00278.x }} | |||
* {{cite journal | vauthors = Rotondo R, Bertolotto M, Barisione G, Astigiano S, Mandruzzato S, Ottonello L, Dallegri F, Bronte V, Ferrini S, Barbieri O | title = Exocytosis of azurophil and arginase 1-containing granules by activated polymorphonuclear neutrophils is required to inhibit T lymphocyte proliferation | journal = Journal of Leukocyte Biology | volume = 89 | issue = 5 | pages = 721–7 | date = May 2011 | pmid = 21330347 | pmc = | doi = 10.1189/jlb.1109737 }} | |||
* {{cite journal | vauthors = Shapiro MB, Senapathy P | title = RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression | journal = Nucleic Acids Research | volume = 15 | issue = 17 | pages = 7155–74 | date = September 1987 | pmid = 3658675 | pmc = 306199 | doi = 10.1093/nar/15.17.7155 }} | |||
* {{cite journal | vauthors = Rotondo R, Barisione G, Mastracci L, Grossi F, Orengo AM, Costa R, Truini M, Fabbi M, Ferrini S, Barbieri O | title = IL-8 induces exocytosis of arginase 1 by neutrophil polymorphonuclears in nonsmall cell lung cancer | journal = International Journal of Cancer | volume = 125 | issue = 4 | pages = 887–93 | date = August 2009 | pmid = 19431148 | pmc = | doi = 10.1002/ijc.24448 }} | |||
* {{cite journal | vauthors = Salam MT, Bastain TM, Rappaport EB, Islam T, Berhane K, Gauderman WJ, Gilliland FD | title = Genetic variations in nitric oxide synthase and arginase influence exhaled nitric oxide levels in children | journal = Allergy | volume = 66 | issue = 3 | pages = 412–9 | date = March 2011 | pmid = 21039601 | pmc = 3058253 | doi = 10.1111/j.1398-9995.2010.02492.x }} | |||
* {{cite journal | vauthors = Gannon PO, Godin-Ethier J, Hassler M, Delvoye N, Aversa M, Poisson AO, Péant B, Alam Fahmy M, Saad F, Lapointe R, Mes-Masson AM | title = Androgen-regulated expression of arginase 1, arginase 2 and interleukin-8 in human prostate cancer | journal = PLOS One | volume = 5 | issue = 8 | pages = e12107 | date = August 2010 | pmid = 20711410 | pmc = 2920336 | doi = 10.1371/journal.pone.0012107 | editor1-last = Creighton | editor1-first = Chad }} | |||
* {{cite journal | vauthors = Ishikawa T, Harada T, Koi H, Kubota T, Azuma H, Aso T | title = Identification of arginase in human placental villi | journal = Placenta | volume = 28 | issue = 2–3 | pages = 133–8 | year = 2007 | pmid = 16720041 | pmc = | doi = 10.1016/j.placenta.2006.03.015 }} | |||
| title = Dysregulated | |||
| journal = JAMA | |||
| volume = 294 | |||
| issue = 1 | |||
| pages = 81–90 | |||
| | |||
| pmid = 15998894 | |||
| pmc =2065861 | |||
}} | |||
*{{ | |||
| | |||
| title = Arginase-flotillin interaction brings arginase to red blood cell membrane | |||
| journal = FEBS Letters | |||
| volume = 580 | |||
| issue = 28–29 | |||
| pages = | |||
| | |||
| pmid = 17113085 | |||
| pmc = | |||
}} | |||
*{{ | |||
| | |||
| title = Recent advances in arginine metabolism: | |||
| journal = British Journal of Pharmacology | |||
| volume = 157 | |||
| issue = 6 | |||
| pages = | |||
| | |||
| pmid = 19508396 | |||
| pmc =2737650 | |||
}} | |||
*{{ | |||
| | |||
| title = Exocytosis of azurophil and arginase 1-containing granules by activated polymorphonuclear neutrophils is required to inhibit T lymphocyte proliferation | |||
| journal = Journal of Leukocyte Biology | |||
| volume = 89 | |||
| issue = 5 | |||
| pages = | |||
| | |||
| pmid = 21330347 | |||
| pmc = | |||
| doi = 10. | |||
| | |||
| title = RNA splice junctions of different classes of eukaryotes: | |||
| journal = Nucleic Acids Research | |||
| volume = 15 | |||
| issue = 17 | |||
| pages = | |||
| | |||
| pmid = 3658675 | |||
| pmc = 306199 | |||
}} | |||
*{{ | |||
| | |||
| title = IL-8 induces exocytosis of arginase 1 by neutrophil polymorphonuclears in nonsmall cell lung cancer | |||
| journal = International Journal of Cancer | |||
| volume = 125 | |||
| issue = 4 | |||
| pages = | |||
| | |||
| pmid = 19431148 | |||
| pmc = | |||
}} | |||
*{{ | |||
| | |||
| title = Genetic variations in nitric oxide synthase and arginase influence exhaled nitric oxide levels in children | |||
| journal = Allergy | |||
| volume = 66 | |||
| issue = 3 | |||
| pages = | |||
| | |||
| pmid = 21039601 | |||
| pmc =3058253 | |||
}} | |||
*{{ | |||
| | |||
| title = Androgen- | |||
| journal = | |||
| volume = 5 | |||
| issue = 8 | |||
| pages = e12107 | |||
| | |||
| pmid = 20711410 | |||
| pmc =2920336 | |||
}} | |||
*{{ | |||
| | |||
| title = Identification of | |||
| journal = Placenta | |||
| volume = 28 | |||
| issue = 2–3 | |||
| pages = | |||
| year = 2007 | |||
| pmid = 16720041 | |||
| pmc = | |||
}} | |||
{{refend}} | {{refend}} | ||
Latest revision as of 04:31, 11 August 2018
VALUE_ERROR (nil) | |||||||
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Identifiers | |||||||
Aliases | |||||||
External IDs | GeneCards: [1] | ||||||
Orthologs | |||||||
Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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The human ARG1 gene encodes the protein arginase.[1]
Function
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.[2]
References
- ↑ "Entrez Gene: Arginase, liver".
- ↑ [provided by RefSeq, Sep 2011]
External links
- Human ARG1 genome location and ARG1 gene details page in the UCSC Genome Browser.
Further reading
- Morris CR, Kato GJ, Poljakovic M, Wang X, Blackwelder WC, Sachdev V, Hazen SL, Vichinsky EP, Morris SM, Gladwin MT (July 2005). "Dysregulated arginine metabolism, hemolysis-associated pulmonary hypertension, and mortality in sickle cell disease". JAMA. 294 (1): 81–90. doi:10.1001/jama.294.1.81. PMC 2065861. PMID 15998894.
- Jiang M, Ding Y, Su Y, Hu X, Li J, Zhang Z (December 2006). "Arginase-flotillin interaction brings arginase to red blood cell membrane". FEBS Letters. 580 (28–29): 6561–4. doi:10.1016/j.febslet.2006.11.003. PMID 17113085.
- Morris SM (July 2009). "Recent advances in arginine metabolism: roles and regulation of the arginases". British Journal of Pharmacology. 157 (6): 922–30. doi:10.1111/j.1476-5381.2009.00278.x. PMC 2737650. PMID 19508396.
- Rotondo R, Bertolotto M, Barisione G, Astigiano S, Mandruzzato S, Ottonello L, Dallegri F, Bronte V, Ferrini S, Barbieri O (May 2011). "Exocytosis of azurophil and arginase 1-containing granules by activated polymorphonuclear neutrophils is required to inhibit T lymphocyte proliferation". Journal of Leukocyte Biology. 89 (5): 721–7. doi:10.1189/jlb.1109737. PMID 21330347.
- Shapiro MB, Senapathy P (September 1987). "RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression". Nucleic Acids Research. 15 (17): 7155–74. doi:10.1093/nar/15.17.7155. PMC 306199. PMID 3658675.
- Rotondo R, Barisione G, Mastracci L, Grossi F, Orengo AM, Costa R, Truini M, Fabbi M, Ferrini S, Barbieri O (August 2009). "IL-8 induces exocytosis of arginase 1 by neutrophil polymorphonuclears in nonsmall cell lung cancer". International Journal of Cancer. 125 (4): 887–93. doi:10.1002/ijc.24448. PMID 19431148.
- Salam MT, Bastain TM, Rappaport EB, Islam T, Berhane K, Gauderman WJ, Gilliland FD (March 2011). "Genetic variations in nitric oxide synthase and arginase influence exhaled nitric oxide levels in children". Allergy. 66 (3): 412–9. doi:10.1111/j.1398-9995.2010.02492.x. PMC 3058253. PMID 21039601.
- Gannon PO, Godin-Ethier J, Hassler M, Delvoye N, Aversa M, Poisson AO, Péant B, Alam Fahmy M, Saad F, Lapointe R, Mes-Masson AM (August 2010). Creighton C, ed. "Androgen-regulated expression of arginase 1, arginase 2 and interleukin-8 in human prostate cancer". PLOS One. 5 (8): e12107. doi:10.1371/journal.pone.0012107. PMC 2920336. PMID 20711410.
- Ishikawa T, Harada T, Koi H, Kubota T, Azuma H, Aso T (2007). "Identification of arginase in human placental villi". Placenta. 28 (2–3): 133–8. doi:10.1016/j.placenta.2006.03.015. PMID 16720041.
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