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10.1016/j.tips.2015.03.006 http://scihub22266oqcxt.onion/10.1016/j.tips.2015.03.006 C4461463!4461463 !25930708     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25930708 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Trends+Pharmacol+Sci 2015 ; 36 (6 ): 395-405 Nephropedia Template TP {{tp|p=25930708 |t=2015. Arginase: an old enzyme with new tricks |pdf=|usr=}}{{25930708 }} gab.com Text Arginase: an old enzyme with new tricks JO: Trends Pharmacol Sci http://www.kidney.de/pget.php?&tw=1&pmid=25930708 #FOAvip Arginase has roots in early life-forms. It converts L-arginine to urea and ornithine. The former provides protection against NH3; the latter serves to stimulate cell growth and other physiological functions. Excessive arginase activity in mammals has been associated with cardiovascular and nervous system dysfunction and disease. Two relevant aspects of this elevated activity may be involved in these disease states. First, excessive arginase activity reduces the supply of L-arginine needed by nitric oxide (NO) synthase to produce NO. Second, excessive production of ornithine leads to vascular structural problems and neural toxicity. Recent research has identified inflammatory agents and reactive oxygen species (ROS) as drivers of this pathologic elevation of arginase activity and expression. We review the involvement of arginase in cardiovascular and nervous system dysfunction, and discuss potential therapeutic interventions targeting excess arginase. Twit Text FOAVip Arginase: an old enzyme with new tricks ????Trends Pharmacol Sci http://www.kidney.de/pget.php?&tw=1&pmid=25930708 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25930708 #FOAvip English Wikipedia <ref>{{Cite pmid|25930708 }}</ref> Arginase: an old enzyme with new tricks #MMPMID25930708 Caldwell RB ; Toque HA ; Narayanan SP ; Caldwell RW Trends Pharmacol Sci 2015[Jun]; 36 (6 ): 395-405 PMID25930708 show ga Arginase has roots in early life-forms. It converts L-arginine to urea and ornithine. The former provides protection against NH3; the latter serves to stimulate cell growth and other physiological functions. Excessive arginase activity in mammals has been associated with cardiovascular and nervous system dysfunction and disease. Two relevant aspects of this elevated activity may be involved in these disease states. First, excessive arginase activity reduces the supply of L-arginine needed by nitric oxide (NO) synthase to produce NO. Second, excessive production of ornithine leads to vascular structural problems and neural toxicity. Recent research has identified inflammatory agents and reactive oxygen species (ROS) as drivers of this pathologic elevation of arginase activity and expression. We review the involvement of arginase in cardiovascular and nervous system dysfunction, and discuss potential therapeutic interventions targeting excess arginase. |Animals [MESH] |Arginase/antagonists & inhibitors/genetics/*metabolism [MESH] |Cardiovascular Diseases/enzymology/*metabolism [MESH] |Humans [MESH] |Nervous System Diseases/enzymology/*metabolism [MESH]Arginase: an old enzyme with new tricks (epmc).pdf DeepDyve Pubget Overpricing