Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases
| Autor: | Patrick Vallance, Joanne Santa Maria, I. G. Charles, Ann Chubb, Guy St. J. Whitley, Raymond J. MacAllister, James Leiper |
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| Jazyk: | angličtina |
| Rok vydání: | 1999 |
| Předmět: |
Gene isoform
Biochemistry & Molecular Biology Methylarginine DNA Complementary Arginine Hydrolases Molecular Sequence Data Biology Endothelial NOS Biochemistry Nitric oxide Amidohydrolases chemistry.chemical_compound Rapid amplification of cDNA ends Animals Humans Amino Acid Sequence Cloning Molecular Molecular Biology Base Sequence Sequence Homology Amino Acid Cell Biology Dimethylargininase Recombinant Proteins Rats Isoenzymes chemistry Asymmetric dimethylarginine Research Article |
| Popis: | Methylarginines inhibit nitric oxide synthases (NOS). Cellular concentrations of methylarginines are determined in part by the activity of dimethylarginine dimethylaminohydrolase (DDAH; EC 3.5.3.18). We have cloned human DDAH and identified and expressed a second novel DDAH isoform (DDAH I and II respectively). DDAH I predominates in tissues that express neuronal NOS. DDAH II predominates in tissues expressing endothelial NOS. These results strengthen the hypothesis that methylarginine concentration is actively regulated and identify molecular targets for the tissue and cell-specific regulation of methylarginine concentration. |
| Databáze: | OpenAIRE |
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