Hypertension, Vol 21, 155-165, Copyright © 1993 by American Heart Association
DJ Campbell, A Kladis and AM Duncan
The bradykinin peptide system is a tissue-based system with potent
cardiovascular and renal effects. To investigate the regulation of this
system, we developed a highly sensitive amino terminal-directed
radioimmunoassay that, with high performance liquid chromatography, enables
the measurement of bradykinin-(1-7), bradykinin-(1-8), and
bradykinin-(1-9). Together with a carboxy terminal-directed
radioimmunoassay, we characterized bradykinin peptides in rat kidney and
blood. The predominant bradykinin peptides in kidney were bradykinin-(1-9)
(approximately 100 fmol/g wet weight of tissue) and bradykinin-(1-7)
(approximately 70 fmol/g), with low levels of bradykinin-(1-8)
(approximately 8 fmol/g) and bradykinin-(4-9) (approximately 12 fmol/g)
detectable; bradykinin-(2-9) and bradykinin- (3-9) were below the limits of
detection. In blood, the levels of bradykinin-(1-9) were very low
(approximately 2 fmol/ml), and other bradykinin peptides were below the
limits of detection. Ile,Ser- bradykinin and Met,Ile,Ser-bradykinin were
below the limits of detection in both kidney and blood, indicating that
T-kininogen makes no detectable contribution to renal or circulating
bradykinin peptides. Administration of the angiotensin converting enzyme
inhibitor perindopril was associated with an approximate twofold increase
in renal levels of bradykinin-(1-8) and bradykinin-(1-9) and a decrease in
the bradykinin-(1-7)/bradykinin-(1-9) ratio. The amino terminal- directed
radioimmunoassay was also applied to heart, aorta, brown adipose tissue,
adrenal lung, and brain. For these tissues, bradykinin- (1-7) and
bradykinin-(1-9) were of similar abundance (16-340 fmol/g), with lower
levels of bradykinin-(1-8). These studies demonstrate that tissue levels of
bradykinin peptides are much higher than circulating levels, consistent
with their formation at a local tissue site. Of peptides derived from
K-kininogen, bradykinin-(1-9) is the predominant bioactive peptide in all
tissues, and a major pathway of bradykinin-(1- 9) metabolism involves the
formation of bradykinin-(1-7). In kidney, angiotensin converting enzyme
plays an important role in bradykinin-(1- 9) metabolism, and increased
bradykinin-(1-9) and bradykinin-(1-8) levels may mediate in part the renal
effects of converting enzyme inhibition.
ARTICLES
Bradykinin peptides in kidney, blood, and other tissues of the rat
St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
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