L-arginine regulates asymmetric dimethylarginine metabolism by inhibiting dimethylarginine dimethylaminohydrolase activity in hepatic (HepG2) cells
An increase in circulating asymmetric dimethylarginine (ADMA) and a decreased L-arginine/ADMA ratio are associated with reduced endothelial nitric oxide (NO) production and increased risk of vascular disease. We explored relations between ADMA, L-arginine and dimethylarginine dimethylaminohydrolase...
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| Veröffentlicht in: | Cellular and molecular life sciences : CMLS 2006-12, Vol.63 (23), p.2838-2846 |
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| creator | Wang, J Sim, A. S Wang, X. L Wilcken, D. E. L |
| description | An increase in circulating asymmetric dimethylarginine (ADMA) and a decreased L-arginine/ADMA ratio are associated with reduced endothelial nitric oxide (NO) production and increased risk of vascular disease. We explored relations between ADMA, L-arginine and dimethylarginine dimethylaminohydrolase (DDAH) in liver (HepG2) cells. DDAH is the principle enzyme for the metabolism of ADMA. HepG2 cells metabolised 44.8 nmol/h of ADMA per 3.6 x 10⁶ cells in the absence of L-arginine. The metabolism of ADMA at physiological (1μ mol/l, p < 0.01) and at pathological (100μmol/l, p < 0.01) levels was inhibited dose-dependently by L-arginine (0-400μmol/l) in cultured HepG2 cells and increased intracellular ADMA (p = 0.039). L-arginine competitively inhibited DDAH enzyme activity to 5.6 ± 2.0% of the untreated level (p < 0.01). We conclude that L-arginine regulates ADMA metabolism dose-dependently by competing for DDAH thus maintaining the metabolic balance of L-arginine and ADMA, and endothelial NO homeostasis. |
| doi_str_mv | 10.1007/s00018-006-6271-8 |
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S ; Wang, X. L ; Wilcken, D. E. L</creator><creatorcontrib>Wang, J ; Sim, A. S ; Wang, X. L ; Wilcken, D. E. L</creatorcontrib><description>An increase in circulating asymmetric dimethylarginine (ADMA) and a decreased L-arginine/ADMA ratio are associated with reduced endothelial nitric oxide (NO) production and increased risk of vascular disease. We explored relations between ADMA, L-arginine and dimethylarginine dimethylaminohydrolase (DDAH) in liver (HepG2) cells. DDAH is the principle enzyme for the metabolism of ADMA. HepG2 cells metabolised 44.8 nmol/h of ADMA per 3.6 x 10⁶ cells in the absence of L-arginine. The metabolism of ADMA at physiological (1μ mol/l, p < 0.01) and at pathological (100μmol/l, p < 0.01) levels was inhibited dose-dependently by L-arginine (0-400μmol/l) in cultured HepG2 cells and increased intracellular ADMA (p = 0.039). L-arginine competitively inhibited DDAH enzyme activity to 5.6 ± 2.0% of the untreated level (p < 0.01). We conclude that L-arginine regulates ADMA metabolism dose-dependently by competing for DDAH thus maintaining the metabolic balance of L-arginine and ADMA, and endothelial NO homeostasis.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-006-6271-8</identifier><identifier>PMID: 17075694</identifier><language>eng</language><publisher>Switzerland: Basel : Birkhäuser-Verlag</publisher><subject>Amidohydrolases - metabolism ; Arginine - analogs & derivatives ; Arginine - chemistry ; Arginine - metabolism ; Asymmetric dimethylarginine ; Cell Line, Tumor ; dimethylarginine dimethylaminohydrolase ; Enzymatic activity ; Hepatocytes - metabolism ; HepG2 ; Humans ; L-arginine ; Metabolism ; Nitric oxide ; Nitric Oxide - metabolism ; Vascular diseases</subject><ispartof>Cellular and molecular life sciences : CMLS, 2006-12, Vol.63 (23), p.2838-2846</ispartof><rights>Birkhäuser Verlag, Basel 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c449t-321b298e9a96231d0ce107e237370d7515ad0dca3d1c26bc737b46dd4ec382313</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11136430/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11136430/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17075694$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, J</creatorcontrib><creatorcontrib>Sim, A. S</creatorcontrib><creatorcontrib>Wang, X. L</creatorcontrib><creatorcontrib>Wilcken, D. E. L</creatorcontrib><title>L-arginine regulates asymmetric dimethylarginine metabolism by inhibiting dimethylarginine dimethylaminohydrolase activity in hepatic (HepG2) cells</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell Mol Life Sci</addtitle><description>An increase in circulating asymmetric dimethylarginine (ADMA) and a decreased L-arginine/ADMA ratio are associated with reduced endothelial nitric oxide (NO) production and increased risk of vascular disease. We explored relations between ADMA, L-arginine and dimethylarginine dimethylaminohydrolase (DDAH) in liver (HepG2) cells. DDAH is the principle enzyme for the metabolism of ADMA. HepG2 cells metabolised 44.8 nmol/h of ADMA per 3.6 x 10⁶ cells in the absence of L-arginine. The metabolism of ADMA at physiological (1μ mol/l, p < 0.01) and at pathological (100μmol/l, p < 0.01) levels was inhibited dose-dependently by L-arginine (0-400μmol/l) in cultured HepG2 cells and increased intracellular ADMA (p = 0.039). L-arginine competitively inhibited DDAH enzyme activity to 5.6 ± 2.0% of the untreated level (p < 0.01). We conclude that L-arginine regulates ADMA metabolism dose-dependently by competing for DDAH thus maintaining the metabolic balance of L-arginine and ADMA, and endothelial NO homeostasis.</description><subject>Amidohydrolases - metabolism</subject><subject>Arginine - analogs & derivatives</subject><subject>Arginine - chemistry</subject><subject>Arginine - metabolism</subject><subject>Asymmetric dimethylarginine</subject><subject>Cell Line, Tumor</subject><subject>dimethylarginine dimethylaminohydrolase</subject><subject>Enzymatic activity</subject><subject>Hepatocytes - metabolism</subject><subject>HepG2</subject><subject>Humans</subject><subject>L-arginine</subject><subject>Metabolism</subject><subject>Nitric oxide</subject><subject>Nitric Oxide - metabolism</subject><subject>Vascular diseases</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNplkc1u1DAUhS0EoqXwAGwgYoFgEbj-ie2sKlRBizQSC6jEznJsT-IqsQc7qZTn4IXxaEbD38r29XeO7_VB6DmGdxhAvM8AgGUNwGtOBK7lA3SOGYG6BYEfHvdcku9n6EnOdwVuJOGP0RkWIBresnP0c1Pr1Pvgg6uS65dRzy5XOq_T5ObkTWV92QzreKLKUXdx9HmqurXyYfCdn33o_ydPhcmHOKw2xVFnV2kz-3s_77XV4HZ6Lq-8uXG7a_K2Mm4c81P0aKvH7J4d1wt0--njt6ubevPl-vPVh01tGGvnmhLckVa6VrecUGzBOAzCESqoACsa3GgL1mhqsSG8M6XcMW4tc4bKIqAX6PLgu1u6yVnjwpz0qHbJTzqtKmqv_r4JflB9vFcYY8oZheLw-uiQ4o_F5VlNPu9n0MHFJavy96UXEAV89Q94F5cUynSKMi4lSCAFwgfIpJhzcttTKxjUPnB1CFyVwNU-cCWL5sWfM_xWHBMuwMsDsNVR6T75rG6_EsC0-LGGSU5_AehStAg</recordid><startdate>200612</startdate><enddate>200612</enddate><creator>Wang, J</creator><creator>Sim, A. 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S</au><au>Wang, X. L</au><au>Wilcken, D. E. L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>L-arginine regulates asymmetric dimethylarginine metabolism by inhibiting dimethylarginine dimethylaminohydrolase activity in hepatic (HepG2) cells</atitle><jtitle>Cellular and molecular life sciences : CMLS</jtitle><addtitle>Cell Mol Life Sci</addtitle><date>2006-12</date><risdate>2006</risdate><volume>63</volume><issue>23</issue><spage>2838</spage><epage>2846</epage><pages>2838-2846</pages><issn>1420-682X</issn><eissn>1420-9071</eissn><abstract>An increase in circulating asymmetric dimethylarginine (ADMA) and a decreased L-arginine/ADMA ratio are associated with reduced endothelial nitric oxide (NO) production and increased risk of vascular disease. We explored relations between ADMA, L-arginine and dimethylarginine dimethylaminohydrolase (DDAH) in liver (HepG2) cells. DDAH is the principle enzyme for the metabolism of ADMA. HepG2 cells metabolised 44.8 nmol/h of ADMA per 3.6 x 10⁶ cells in the absence of L-arginine. The metabolism of ADMA at physiological (1μ mol/l, p < 0.01) and at pathological (100μmol/l, p < 0.01) levels was inhibited dose-dependently by L-arginine (0-400μmol/l) in cultured HepG2 cells and increased intracellular ADMA (p = 0.039). L-arginine competitively inhibited DDAH enzyme activity to 5.6 ± 2.0% of the untreated level (p < 0.01). We conclude that L-arginine regulates ADMA metabolism dose-dependently by competing for DDAH thus maintaining the metabolic balance of L-arginine and ADMA, and endothelial NO homeostasis.</abstract><cop>Switzerland</cop><pub>Basel : Birkhäuser-Verlag</pub><pmid>17075694</pmid><doi>10.1007/s00018-006-6271-8</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amidohydrolases - metabolism Arginine - analogs & derivatives Arginine - chemistry Arginine - metabolism Asymmetric dimethylarginine Cell Line, Tumor dimethylarginine dimethylaminohydrolase Enzymatic activity Hepatocytes - metabolism HepG2 Humans L-arginine Metabolism Nitric oxide Nitric Oxide - metabolism Vascular diseases |
| title | L-arginine regulates asymmetric dimethylarginine metabolism by inhibiting dimethylarginine dimethylaminohydrolase activity in hepatic (HepG2) cells |
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