Clinical Chemistry
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 51: 708-718, 2005. First published February 17, 2005; 10.1373/clinchem.2004.039891
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
clinchem.2004.039891v1
51/4/708    most recent
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 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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Web of Science (4)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ala-Kopsala, M.
Right arrow Articles by Vuolteenaho, O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ala-Kopsala, M.
Right arrow Articles by Vuolteenaho, O.
Related Collections
Right arrow Proteomics and Protein Markers
(Clinical Chemistry. 2005;51:708-718.)
© 2005 American Association for Clinical Chemistry, Inc.

Proteomics and Protein Markers

Single Assay for Amino-Terminal Fragments of Cardiac A- and B-Type Natriuretic Peptides

Minna Ala-Kopsala1, Heikki Ruskoaho2, Juhani Leppäluoto1, Leila Seres3, Reka Skoumal3, Miklos Toth3,4,5, Ferenc Horkay5 and Olli Vuolteenaho1,a

Departments of1 Physiology and 2 Pharmacology and Toxicology, Biocenter Oulu, University of Oulu, Oulu, Finland.
3 The First Department of Internal Medicine, Semmelweis University, Budapest, Hungary.
4 Molecular Genetic Research Group of the Hungarian Academy of Sciences, Budapest, Hungary.
5 Gyorgy Gottsegen National Institute of Cardiology, Budapest, Hungary.

aAddress correspondence to this author at: Department of Physiology, Faculty of Medicine, PO Box 5000, University of Oulu, Oulu FIN-90014, Finland. Fax 358-8-5375320; e-mail olli.vuolteenaho{at}oulu.fi.

Background: High circulating concentrations of N-terminal fragments of A- and B-type natriuretic peptides (NT-proANP and NT-proBNP) identify patients with impaired cardiac function. ProANP-derived peptides are particularly sensitive to increased preload of the heart and proBNP-derived peptides to increased afterload; therefore, combining the information from the ANP and BNP systems into a single analyte could produce an assay with increased diagnostic and prognostic power.

Methods: We prepared a hybrid peptide containing peptide sequences from both NT-proBNP and NT-proANP (referred to as NT-proXNP) by recombinant techniques and used it to develop a RIA combining weighed concentrations of NT-proANP and NT-proBNP into a new virtual analyte, NT-proXNP. We used the novel method to measure the circulating concentrations in healthy persons and in patients with cardiac disorders. We also characterized the assay by HPLC analysis of the immunoreactive molecular forms in human plasma and serum.

Results: The results from the novel assay correlated well with independent home-made NT-proANP and NT-proBNP assays (r2 = 0.75–0.85) as well with the arithmetic sum of NT-proANP and NT-proBNP (r2 = 0.92). Patients with valvular heart disease (VHD) and coronary artery disease (CAD) had significantly increased NT-proXNP concentrations. The areas under the curve (AUC) of the NT-proXNP assay in detecting VHD and CAD (0.961 and 0.924, respectively) were significantly larger than the AUC of either NT-proANP (0.947 and 0.872) or NT-proBNP (0.913 and 0.782) assays. HPLC analysis showed that the novel NT-proXNP assay detects two major classes of circulating immunoreactivity corresponding to peptides derived from NT-proANP and NT-proBNP.

Conclusions: Our novel immunoassay mimics the physiologic signaling system working in the body by converging the information obtained from the activation of ANP and BNP into a single virtual analyte, NT-proXNP. It appears to have a diagnostic efficiency equal to or slightly better than that of individual NT-proANP or NT-proBNP assays.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2005 by the American Association for Clinical Chemistry.