AJP - Regu Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Regul Integr Comp Physiol 278: R897-R904, 2000;
0363-6119/00 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via ISI Web of Science (19)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Duncan, A.-M.
Right arrow Articles by Campbell, D. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Duncan, A.-M.
Right arrow Articles by Campbell, D. J.
Vol. 278, Issue 4, R897-R904, April 2000

Kinins in humans

Ann-Maree Duncan1, Athena Kladis1, Garry L. Jennings2, Anthony M. Dart2, Murray Esler2, and Duncan J. Campbell1

1 St. Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, and 2 Baker Medical Research Institute, Prahran 3181, Australia

The kinin peptide system in humans is complex. Whereas plasma kallikrein generates bradykinin peptides, glandular kallikrein generates kallidin peptides. Moreover, a proportion of kinin peptides is hydroxylated on proline3 of the bradykinin sequence. We established HPLC-based radioimmunoassays for nonhydroxylated and hydroxylated bradykinin and kallidin peptides and their metabolites in blood and urine. Both nonhydroxylated and hydroxylated bradykinin and kallidin peptides were identified in human blood and urine, although the levels in blood were often below the assay detection limit. Whereas kallidin peptides were more abundant than bradykinin peptides in urine, bradykinin peptides were more abundant in blood. Bradykinin and kallidin peptide levels were higher in venous than arterial blood. Angiotensin-converting enzyme inhibition increased blood levels of bradykinin, but not kallidin, peptides. Reactive hyperemia had no effect on antecubital venous levels of bradykinin or kallidin peptide levels. These studies demonstrate differential regulation of the bradykinin and kallidin peptide systems, and indicate that blood levels of bradykinin peptides are more responsive to angiotensin-converting enzyme inhibition than blood levels of kallidin peptides.

bradykinin; kallidin; angiotensin-converting enzyme inhibition; cardiac failure; reactive hyperemia


This article has been cited by other articles:


Home page
 J. Appl. Physiol.Home page
F. Boix, C. Roe, L. Rosenborg, and S. Knardahl
Kinin peptides in human trapezius muscle during sustained isometric contraction and their relation to pain
J Appl Physiol, February 1, 2005; 98(2): 534 - 540.
[Abstract] [Full Text] [PDF]

Home page
 J. Am. Soc. Nephrol.Home page
J.-L. Bascands and J. P. Schanstra
Bradykinin and Renal Fibrosis: Have We ACE'd it?
J. Am. Soc. Nephrol., September 1, 2004; 15(9): 2504 - 2506.
[Full Text] [PDF]

Home page
 IOVSHome page
P. Jeppesen, C. Aalkjaer, and T. Bek
Bradykinin Relaxation in Small Porcine Retinal Arterioles
Invest. Ophthalmol. Vis. Sci., June 1, 2002; 43(6): 1891 - 1896.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
D. J. Campbell, B. Dixon, A. Kladis, M. Kemme, and J. D. Santamaria
Activation of the kallikrein-kinin system by cardiopulmonary bypass in humans
Am J Physiol Regulatory Integrative Comp Physiol, October 1, 2001; 281(4): R1059 - R1070.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online