Predominant plasma clone’

Greeb, J., Shull, G.E., 1989, Molecular cloning of a third isoform of the calmodulin-sensitive plasma membrane Ca2+-transporting ATPase that is expressed predominantly in brain and skeletal muscle. J Biol Chem 264, 18569-18576. 

ADMA is degraded by the enzyme dimethylarginine dimethylaminohydrolase (DDAH), which hydrolyzes ADMA to L-citrulline and dimethylamine [70,83]. Two isoforms of this enzyme have been characterized and cloned to date. DDAH I predominates in tissues that express neuronal NOS and DDAH II predominates in tissues expressing endothelial NOS [70,84]. Activity of DDAH has been shown to be decreased by oxidized low density lipoprotein (LDL) or tumor necrosis factor-a (TNF-a) in vitro yielding increased levels of ADMA. Plasma levels of ADMA were found elevated in hyperhomo-cysteinemia, hypercholesterolemia and in hypertensive patients on a high salt diet [70,72,73]. 

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