State of the art of immunoassay methods for B-type natriuretic peptides: An update. (April 2015)

• Record Type: Journal Article
• Authors: Clerico, Aldo; Franzini, Maria; Masotti, Silvia; Prontera, Concetta; Passino, Claudio
• Is Part Of: Critical reviews in clinical laboratory sciences. Volume 52:Number 2(2015:Mar./Apr.)
• Page Start: 56
• Page End: 69
• Publication Date: 2015-04
• Subjects: Diagnosis, laboratory -- Periodicals; Medicine, Clinical -- Periodicals; 616.07
• DOI: 10.3109/10408363.2014.987720
• Languages: English
• ISSNs: 1040-8363

Abstract

<abstract> <title>Abstract</title> <p>The aim of this review article is to give an update on the state of the art of the immunoassay methods for the measurement of B-type natriuretic peptide (BNP) and its related peptides. Using chromatographic procedures, several studies reported an increasing number of circulating peptides related to BNP in human plasma of patients with heart failure. These peptides may have reduced or even no biological activity. Furthermore, other studies have suggested that, using immunoassays that are considered specific for BNP, the precursor of the peptide hormone, proBNP, constitutes a major portion of the peptide measured in plasma of patients with heart failure. Because BNP immunoassay methods show large (up to 50%) systematic differences in values, the use of identical decision values for all immunoassay methods, as suggested by the most recent international guidelines, seems unreasonable. Since proBNP significantly cross-reacts with all commercial immunoassay methods considered specific for BNP, manufacturers should test and clearly declare the degree of cross-reactivity of glycosylated and non-glycosylated proBNP in their BNP immunoassay methods. Clinicians should take into account that there are large systematic differences between methods when they compare results from different laboratories that use different BNP immunoassays. On the other hand, clinical laboratories should take part in external quality assessment (EQA) programs to evaluate the bias of their method in comparison to other BNP methods. Finally, the authors believe that the development of more specific methods for the active peptide, BNP<sub>1–32</sub>, should reduce the systematic differences between methods and result in better harmonization of results.</p> </abstract>