L-Arginine Metabolism in Essential Hypertension
Essential hypertension is characterized by impaired endothelial function. Data derived from normotensive subjects with a genetic predisposition to arterial hypertension suggest that endothelial dysfunction is a cause rather than a consequence of the condition. Given that, in normotensive offspring of hypertensive parents, impaired endothelium dependent vasodilation can be restored by supplementation of the nitric oxide (NO) precursor L-arginine, a defect in the L-arginine/NO pathway can be postulated. The investigators at the University of Erlangen-Nuremberg, hypothesize that impaired endothelial function in essential hypertension is associated with alterations in L-arginine metabolism and transport. This study will determine whether metabolism and transport of L-arginine are altered in patients with essential hypertension and whether these potential alterations can be targeted therapeutically.
Allocation: Randomized, Control: Placebo Control, Intervention Model: Crossover Assignment, Masking: Double Blind (Subject, Investigator), Primary Purpose: Treatment
CRC, Medizinische Klinik 4 - Nephrology and Hypertension, University of Erlangen-Nürnberg
University of Erlangen-Nürnberg Medical School
Results (where available)
- Source: http://clinicaltrials.gov/show/NCT00137124
- Information obtained from ClinicalTrials.gov on July 15, 2010
Medical and Biotech [MESH] Definitions
An essential amino acid that is physiologically active in the L-form.
An enzyme that activates arginine with its specific transfer RNA. EC 18.104.22.168.
An enzyme that catalyzes the phosphorylation of the guanidine nitrogen of arginine in the presence of ATP and a divalent cation with formation of phosphorylarginine and ADP. EC 22.214.171.124.
Enzymes that catalyze the methylation of arginine residues of proteins to yield N-mono- and N,N-dimethylarginine. This enzyme is found in many organs, primarily brain and spleen.
Complement C5a, Des-arginine
A derivative of complement C5a, generated when the carboxy-terminal ARGININE is removed by CARBOXYPEPTIDASE B present in normal human serum. C5a des-Arg shows complete loss of spasmogenic activity though it retains some chemotactic ability (CHEMOATTRACTANTS).
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