L-Arginine Metabolism in Essential Hypertension
Summary
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.
Study Design
Allocation: Randomized, Control: Placebo Control, Intervention Model: Crossover Assignment, Masking: Double Blind (Subject, Investigator), Primary Purpose: Treatment
Conditions
Essential Hypertension
Intervention
L-Arginine
Location
CRC, Medizinische Klinik 4 - Nephrology and Hypertension, University of Erlangen-Nürnberg
Erlangen
Germany
91054
Status
Completed
Source
University of Erlangen-Nürnberg Medical School
Results (where available)
Links
- Source: http://clinicaltrials.gov/show/NCT00137124
- Information obtained from ClinicalTrials.gov on July 15, 2010
Medical and Biotech [MESH] Definitions
Arginine
An essential amino acid that is physiologically active in the L-form.
Arginine-trna Ligase
An enzyme that activates arginine with its specific transfer RNA. EC 6.1.1.19.
Arginine Kinase
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 2.7.3.3.
Protein-arginine N-methyltransferases
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).
Clinical Trials
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