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Kinins in humans.

A M Duncan1, A Kladis, G L Jennings

  • 1St. Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia.

American Journal of Physiology. Regulatory, Integrative and Comparative Physiology
|April 6, 2000
PubMed
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The human kinin peptide system involves bradykinin and kallidin peptides, with distinct levels in blood and urine. Angiotensin-converting enzyme inhibition specifically boosts bradykinin peptide levels.

Area of Science:

  • Biochemistry
  • Physiology
  • Pharmacology

Background:

  • The kinin peptide system is crucial in human physiology, involving plasma kallikrein (producing bradykinin) and glandular kallikrein (producing kallidin).
  • Kinin peptides can exist in nonhydroxylated and hydroxylated forms, adding complexity to their measurement and function.
  • Understanding the differential regulation and physiological levels of these peptides is essential for comprehending their roles in various bodily functions.

Purpose of the Study:

  • To establish and validate sensitive assays for quantifying nonhydroxylated and hydroxylated bradykinin and kallidin peptides and their metabolites.
  • To investigate the presence and levels of these kinin peptides in human blood and urine under basal conditions.
  • To explore the differential regulation of bradykinin and kallidin peptide systems, particularly in response to physiological stimuli and pharmacological interventions.

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Main Methods:

  • Development and application of High-Performance Liquid Chromatography (HPLC)-based radioimmunoassays (RIAs) for precise quantification.
  • Analysis of kinin peptide and metabolite concentrations in human blood (arterial and venous) and urine samples.
  • Investigation of the effects of angiotensin-converting enzyme (ACE) inhibition and reactive hyperemia on kinin peptide levels.

Main Results:

  • Both nonhydroxylated and hydroxylated bradykinin and kallidin peptides were detected in human blood and urine.
  • Kallidin peptides were more abundant in urine, while bradykinin peptides predominated in blood.
  • Bradykinin and kallidin levels were higher in venous compared to arterial blood, and ACE inhibition selectively increased bradykinin peptide levels.

Conclusions:

  • The study demonstrates distinct quantitative profiles and differential regulation between bradykinin and kallidin peptide systems.
  • Blood levels of bradykinin peptides are more sensitive to angiotensin-converting enzyme inhibition than those of kallidin peptides.
  • These findings provide novel insights into the complex kinin peptide system and its modulation in humans.