Genetic and dietary control of plasma tissue kallikrein secretion and urinary kinins exretion in man
Identifieur interne : 008D15 ( Main/Exploration ); précédent : 008D14; suivant : 008D16Genetic and dietary control of plasma tissue kallikrein secretion and urinary kinins exretion in man
Auteurs : Michel Azizi [France] ; Costanza Emanueli [Royaume-Uni] ; Severine Peyrard [France] ; Paolo Maddedu [Royaume-Uni] ; Francois Alhenc-Gelas [France] ; Duncan J. Campbell [Australie]Source :
- Journal of hypertension [ 0263-6352 ] ; 2008.
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- Pascal (Inist)
- Wicri :
English descriptors
- KwdEn :
Abstract
Objectives Tissue kallikrein is a major kinin-forming enzyme involved in artery and kidney functions. Urinary tissue kallikrein activity (UKLKa) reflects renal tissue kallikrein activity and depends on Na and K intake, and genetic factors, especially the tissue kallikrein-inactivating polymorphism, R53H. The effect of these factors on the level of kinin peptides is, however, not known. Moreover, a circulating form of tissue kallikrein is present in human plasma but its origin and regulation are unknown. Methods We used a crossover study to investigate UKLKa, plasma tissue kallikrein (pTK), and urinary kallidin peptides and metabolites (Uki) in 10 R53H and 30 R53R normotensive male subjects randomly assigned to either a 1-week low Na-high K or a high Na-low K diet. Results UKLKa was 50-60% lower in R53H than R53R subjects and was increased by the low Na-high K diet. pTK was also 45-55% lower in R53H than R53R subjects and was increased by the low Na-high K diet. Uki was slightly but significantly higher under the low Na-high K than the high Na-low K diet, but did not differ between genotypes. Conclusion These observations indicate that pTK levels are genetically determined and regulated by Na and K diet, in parallel with UKLKa; this suggests that circulating tissue kallikrein originates mainly from the kidney, and can contribute to circulatory adaptation to dietary ions. Uki is influenced by the Na and K diet, suggesting that kinins participate in renal adaptation to ion intake, but do not quantitatively reflect tissue kallikrein activity in urine, or presumably, in the kidney.
Affiliations:
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cardiovascular disease</term>
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<term>Polymorphism</term>
<term>Potassium</term>
<term>Sodium</term>
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<keywords scheme="Pascal" xml:lang="fr"><term>Pathologie de l'appareil circulatoire</term>
<term>Kinine</term>
<term>Homme</term>
<term>Polymorphisme</term>
<term>Potassium</term>
<term>Sodium</term>
<term>Hypertension artérielle</term>
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<front><div type="abstract" xml:lang="en">Objectives Tissue kallikrein is a major kinin-forming enzyme involved in artery and kidney functions. Urinary tissue kallikrein activity (UKLKa) reflects renal tissue kallikrein activity and depends on Na and K intake, and genetic factors, especially the tissue kallikrein-inactivating polymorphism, R53H. The effect of these factors on the level of kinin peptides is, however, not known. Moreover, a circulating form of tissue kallikrein is present in human plasma but its origin and regulation are unknown. Methods We used a crossover study to investigate UKLKa, plasma tissue kallikrein (pTK), and urinary kallidin peptides and metabolites (Uki) in 10 R53H and 30 R53R normotensive male subjects randomly assigned to either a 1-week low Na-high K or a high Na-low K diet. Results UKLKa was 50-60% lower in R53H than R53R subjects and was increased by the low Na-high K diet. pTK was also 45-55% lower in R53H than R53R subjects and was increased by the low Na-high K diet. Uki was slightly but significantly higher under the low Na-high K than the high Na-low K diet, but did not differ between genotypes. Conclusion These observations indicate that pTK levels are genetically determined and regulated by Na and K diet, in parallel with UKLKa; this suggests that circulating tissue kallikrein originates mainly from the kidney, and can contribute to circulatory adaptation to dietary ions. Uki is influenced by the Na and K diet, suggesting that kinins participate in renal adaptation to ion intake, but do not quantitatively reflect tissue kallikrein activity in urine, or presumably, in the kidney.</div>
</front>
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