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


     

Am J Physiol Lung Cell Mol Physiol 276: L341-L350, 1999;
1040-0605/99 $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 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 Google Scholar
Google Scholar
Right arrow Articles by Merker, M. P.
Right arrow Articles by Dawson, C. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Merker, M. P.
Right arrow Articles by Dawson, C. A.
Vol. 276, Issue 2, L341-L350, February 1999

Proline in vasoactive peptides: consequences for peptide hydrolysis in the lung

Marilyn P. Merker, Said H. Audi, Becky M. Brantmeier, Kasem Nithipatikom, Robert S. Goldman, David L. Roerig, and Christopher A. Dawson

Departments of Anesthesiology, Pharmacology/Toxicology, and Physiology, Medical College of Wisconsin, Milwaukee 53226; Department of Biomedical Engineering, Marquette University, Milwaukee 53233; and Veterans Affairs Medical Center, Milwaukee, Wisconsin 53295

To examine the hypothesis that trans isomers of bradykinin and [Gly6]bradykinin are preferentially hydrolyzed by lung peptidases, we studied the fractional inactivation of these peptides in the perfused rat lung using a bioassay after a single-pass bolus injection and high-performance liquid chromatography after lung recirculation. In the bioassay studies, when the peptides passed through the lung, 25.6-fold more bradykinin or 7-fold more [Gly6]bradykinin was required to elicit a contraction equivalent to that produced when the peptides did not pass through the lung. In the recirculation studies, hydrolysis progress curves with rapid and slow phases were observed, with a higher fraction of bradykinin than [Gly6]bradykinin hydrolyzed in the rapid phase. Cyclophilin increased the hydrolysis rate during the slow phase for both peptides. Kinetic analysis indicated that the slowly hydrolyzed peptide fraction, presumably the cis fraction, was 0.13 for bradykinin and 0.43 for [Gly6]bradykinin with cis-trans isomerization rate constants of 0.074 and 0.049 s-1, respectively, consistent with published nuclear magnetic resonance studies.

high-performance liquid chromatography; bradykinin; [6-glycine]bradykinin; lung peptidases; cis-trans isomerase; cyclophilin


This article has been cited by other articles:


Home page
 Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
M. P. Merker, S. H. Audi, R. D. Bongard, B. J. Lindemer, and G. S. Krenz
Influence of pulmonary arterial endothelial cells on quinone redox status: effect of hyperoxia-induced NAD(P)H:quinone oxidoreductase 1
Am J Physiol Lung Cell Mol Physiol, March 1, 2006; 290(3): L607 - L619.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
S. H. Audi, R. D. Bongard, Y. Okamoto, M. P. Merker, D. L. Roerig, and C. A. Dawson
Pulmonary reduction of an intravascular redox polymer
Am J Physiol Lung Cell Mol Physiol, June 1, 2001; 280(6): L1290 - L1299.
[Abstract] [Full Text] [PDF]


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