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[New insights into arginase. Part II. Role in physiology and pathology].
Postepy Hig Med Dosw (Online). 2008 May 14; 62:214-21.PH

Abstract

Arginase (amidinohydrolase, EC 3.5.3.1) is known as the last enzyme in the urea cycle in the liver, but it is also present in extrahepatic tissues. Arginase hydrolyzes L-arginine to L-ornithine and urea and its biochemical and physiological role varies depending on the organism and tissue. Besides its participation in ammonia detoxification, arginase is involved in the synthesis of polyamines, crucial for the proper course of many metabolic processes, proline, the main connective tissues protein, and glutamates, amino acids which take part in nitric metabolism, important in the nervous system and also a substrate for protein synthesis. The competition of arginase with nitric oxide synthase (NOS) for the common substrate L-arginine indicates its participation in the regulation of nitric oxide (NO) synthesis. The physiological role of arginase and its common occurrence indicate its engagement in many pathologies. Due to its competition with NOS for arginine and its participation in proline synthesis, arginase plays an important role in such diseases as cerebral stroke, trauma, inflammation, and depression, whereas its participation in polyamine synthesis indicates arginase's engagement in the development of neoplastic diseases in the human organism.

Authors+Show Affiliations

Katedra i Zakład Biochemii Akademii Medycznej w Warszawie.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

English Abstract
Journal Article
Review

Language

pol

PubMed ID

18480737

Citation

Mielczarek-Puta, Magdalena, et al. "[New Insights Into Arginase. Part II. Role in Physiology and Pathology]." Postepy Higieny I Medycyny Doswiadczalnej (Online), vol. 62, 2008, pp. 214-21.
Mielczarek-Puta M, Chrzanowska A, Graboń W, et al. [New insights into arginase. Part II. Role in physiology and pathology]. Postepy Hig Med Dosw (Online). 2008;62:214-21.
Mielczarek-Puta, M., Chrzanowska, A., Graboń, W., & Barańczyk-Kuźma, A. (2008). [New insights into arginase. Part II. Role in physiology and pathology]. Postepy Higieny I Medycyny Doswiadczalnej (Online), 62, 214-21.
Mielczarek-Puta M, et al. [New Insights Into Arginase. Part II. Role in Physiology and Pathology]. Postepy Hig Med Dosw (Online). 2008 May 14;62:214-21. PubMed PMID: 18480737.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - [New insights into arginase. Part II. Role in physiology and pathology]. AU - Mielczarek-Puta,Magdalena, AU - Chrzanowska,Alicja, AU - Graboń,Wojciech, AU - Barańczyk-Kuźma,Anna, Y1 - 2008/05/14/ PY - 2007/09/18/received PY - 2008/04/15/accepted PY - 2008/5/16/pubmed PY - 2008/6/18/medline PY - 2008/5/16/entrez SP - 214 EP - 21 JF - Postepy higieny i medycyny doswiadczalnej (Online) JO - Postepy Hig Med Dosw (Online) VL - 62 N2 - Arginase (amidinohydrolase, EC 3.5.3.1) is known as the last enzyme in the urea cycle in the liver, but it is also present in extrahepatic tissues. Arginase hydrolyzes L-arginine to L-ornithine and urea and its biochemical and physiological role varies depending on the organism and tissue. Besides its participation in ammonia detoxification, arginase is involved in the synthesis of polyamines, crucial for the proper course of many metabolic processes, proline, the main connective tissues protein, and glutamates, amino acids which take part in nitric metabolism, important in the nervous system and also a substrate for protein synthesis. The competition of arginase with nitric oxide synthase (NOS) for the common substrate L-arginine indicates its participation in the regulation of nitric oxide (NO) synthesis. The physiological role of arginase and its common occurrence indicate its engagement in many pathologies. Due to its competition with NOS for arginine and its participation in proline synthesis, arginase plays an important role in such diseases as cerebral stroke, trauma, inflammation, and depression, whereas its participation in polyamine synthesis indicates arginase's engagement in the development of neoplastic diseases in the human organism. SN - 1732-2693 UR - https://www.unboundmedicine.com/medline/citation/18480737/[New_insights_into_arginase__Part_II__Role_in_physiology_and_pathology]_ L2 - http://www.phmd.pl/fulltxt.php?ICID=857205 DB - PRIME DP - Unbound Medicine ER -