Specificity of B-type natriuretic peptide assays: Cross-reactivity with different BNP, NT-proBNP, and proBNP peptides

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Specificity of B-type natriuretic peptide assays : Cross-reactivity with different BNP, NT-proBNP, and proBNP peptides. / Saenger, Amy K.; Rodriguez-Fraga, Olaia; Ler, Ranka; Ordonez-Llanos, Jordi; Jaffe, Allan S.; Goetze, Jens Peter; Apple, Fred S.

In: Clinical Chemistry, Vol. 63, No. 1, 2017, p. 351-358.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Saenger, AK, Rodriguez-Fraga, O, Ler, R, Ordonez-Llanos, J, Jaffe, AS, Goetze, JP & Apple, FS 2017, 'Specificity of B-type natriuretic peptide assays: Cross-reactivity with different BNP, NT-proBNP, and proBNP peptides', Clinical Chemistry, vol. 63, no. 1, pp. 351-358. https://doi.org/10.1373/clinchem.2016.263749

APA

Saenger, A. K., Rodriguez-Fraga, O., Ler, R., Ordonez-Llanos, J., Jaffe, A. S., Goetze, J. P., & Apple, F. S. (2017). Specificity of B-type natriuretic peptide assays: Cross-reactivity with different BNP, NT-proBNP, and proBNP peptides. Clinical Chemistry, 63(1), 351-358. https://doi.org/10.1373/clinchem.2016.263749

Vancouver

Saenger AK, Rodriguez-Fraga O, Ler R, Ordonez-Llanos J, Jaffe AS, Goetze JP et al. Specificity of B-type natriuretic peptide assays: Cross-reactivity with different BNP, NT-proBNP, and proBNP peptides. Clinical Chemistry. 2017;63(1):351-358. https://doi.org/10.1373/clinchem.2016.263749

Author

Saenger, Amy K. ; Rodriguez-Fraga, Olaia ; Ler, Ranka ; Ordonez-Llanos, Jordi ; Jaffe, Allan S. ; Goetze, Jens Peter ; Apple, Fred S. / Specificity of B-type natriuretic peptide assays : Cross-reactivity with different BNP, NT-proBNP, and proBNP peptides. In: Clinical Chemistry. 2017 ; Vol. 63, No. 1. pp. 351-358.

Bibtex

@article{fa026281440b4087ab7118a595f37a85,
title = "Specificity of B-type natriuretic peptide assays: Cross-reactivity with different BNP, NT-proBNP, and proBNP peptides",
abstract = "BACKGROUND: B-type natriuretic peptides (BNPs) are used clinically to diagnose and monitor heart failure and are present in the circulation as multiple proBNP-derived fragments. We investigated the specificity of BNP immunoassays with glycosylated and nonglycosylated BNP, N-terminal proBNP (NT-proBNP), and proBNP peptides to probe the cross-reactivity of each assay. METHODS: Nine B-type natriuretic peptides were studied, including synthetic and recombinant BNP (Shionogi, Scios, Mayo), human and synthetic glycosylated and nonglycosylated NT-proBNP (HyTest, Roche Diagnostics), and human glycosylated and nonglycosylated proBNP (HyTest, Scios). Five BNP [Abbott, Abbott POC, Alere, Beckman Coulter, Siemens (Centaur)], 9 NT-proBNP [Ortho-Clinical Diagnostics, Roche, Response, bioMerieux, Siemens (Dimension, Immulite, Stratus CS), Mitsubishi] and 3 research-use-only proBNP immunoassays [Biosite (Alere), Bio-Rad, Goetze] were evaluated. Specificity was assessed by calculating the recovery between baseline and peptide-spiked human plasma pools at target concentrations of 100 ng/L BNP, 300 ng/L proBNP, or 450 ng/L NT-proBNP. All assays were performed in duplicate. RESULTS: BNP and NT-proBNP assays demonstrated substantial cross-reactivity with proBNP peptides. NTproBNP assays do not detect glycosylated forms of either NT-proBNP or proBNP. proBNP assays preferentially detect the BNP 1-32 peptide and have minimal crossreactivity with BNP peptides and glycosylated proBNP. CONCLUSIONS: BNP or NT-proBNP results are not transferable among the current existing immunoassays owing to their differences in cross-reactivity and ability to detect various glycosylated forms of proBNP-derived fragments. Opportunities remain to standardize and harmonize BNP and NT-proBNP assays, as well as to develop specific proBNP assays, to widen their clinical scope of use.",
author = "Saenger, {Amy K.} and Olaia Rodriguez-Fraga and Ranka Ler and Jordi Ordonez-Llanos and Jaffe, {Allan S.} and Goetze, {Jens Peter} and Apple, {Fred S.}",
year = "2017",
doi = "10.1373/clinchem.2016.263749",
language = "English",
volume = "63",
pages = "351--358",
journal = "Clinical Chemistry",
issn = "0009-9147",
publisher = "American Association for Clinical Chemistry, Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - Specificity of B-type natriuretic peptide assays

T2 - Cross-reactivity with different BNP, NT-proBNP, and proBNP peptides

AU - Saenger, Amy K.

AU - Rodriguez-Fraga, Olaia

AU - Ler, Ranka

AU - Ordonez-Llanos, Jordi

AU - Jaffe, Allan S.

AU - Goetze, Jens Peter

AU - Apple, Fred S.

PY - 2017

Y1 - 2017

N2 - BACKGROUND: B-type natriuretic peptides (BNPs) are used clinically to diagnose and monitor heart failure and are present in the circulation as multiple proBNP-derived fragments. We investigated the specificity of BNP immunoassays with glycosylated and nonglycosylated BNP, N-terminal proBNP (NT-proBNP), and proBNP peptides to probe the cross-reactivity of each assay. METHODS: Nine B-type natriuretic peptides were studied, including synthetic and recombinant BNP (Shionogi, Scios, Mayo), human and synthetic glycosylated and nonglycosylated NT-proBNP (HyTest, Roche Diagnostics), and human glycosylated and nonglycosylated proBNP (HyTest, Scios). Five BNP [Abbott, Abbott POC, Alere, Beckman Coulter, Siemens (Centaur)], 9 NT-proBNP [Ortho-Clinical Diagnostics, Roche, Response, bioMerieux, Siemens (Dimension, Immulite, Stratus CS), Mitsubishi] and 3 research-use-only proBNP immunoassays [Biosite (Alere), Bio-Rad, Goetze] were evaluated. Specificity was assessed by calculating the recovery between baseline and peptide-spiked human plasma pools at target concentrations of 100 ng/L BNP, 300 ng/L proBNP, or 450 ng/L NT-proBNP. All assays were performed in duplicate. RESULTS: BNP and NT-proBNP assays demonstrated substantial cross-reactivity with proBNP peptides. NTproBNP assays do not detect glycosylated forms of either NT-proBNP or proBNP. proBNP assays preferentially detect the BNP 1-32 peptide and have minimal crossreactivity with BNP peptides and glycosylated proBNP. CONCLUSIONS: BNP or NT-proBNP results are not transferable among the current existing immunoassays owing to their differences in cross-reactivity and ability to detect various glycosylated forms of proBNP-derived fragments. Opportunities remain to standardize and harmonize BNP and NT-proBNP assays, as well as to develop specific proBNP assays, to widen their clinical scope of use.

AB - BACKGROUND: B-type natriuretic peptides (BNPs) are used clinically to diagnose and monitor heart failure and are present in the circulation as multiple proBNP-derived fragments. We investigated the specificity of BNP immunoassays with glycosylated and nonglycosylated BNP, N-terminal proBNP (NT-proBNP), and proBNP peptides to probe the cross-reactivity of each assay. METHODS: Nine B-type natriuretic peptides were studied, including synthetic and recombinant BNP (Shionogi, Scios, Mayo), human and synthetic glycosylated and nonglycosylated NT-proBNP (HyTest, Roche Diagnostics), and human glycosylated and nonglycosylated proBNP (HyTest, Scios). Five BNP [Abbott, Abbott POC, Alere, Beckman Coulter, Siemens (Centaur)], 9 NT-proBNP [Ortho-Clinical Diagnostics, Roche, Response, bioMerieux, Siemens (Dimension, Immulite, Stratus CS), Mitsubishi] and 3 research-use-only proBNP immunoassays [Biosite (Alere), Bio-Rad, Goetze] were evaluated. Specificity was assessed by calculating the recovery between baseline and peptide-spiked human plasma pools at target concentrations of 100 ng/L BNP, 300 ng/L proBNP, or 450 ng/L NT-proBNP. All assays were performed in duplicate. RESULTS: BNP and NT-proBNP assays demonstrated substantial cross-reactivity with proBNP peptides. NTproBNP assays do not detect glycosylated forms of either NT-proBNP or proBNP. proBNP assays preferentially detect the BNP 1-32 peptide and have minimal crossreactivity with BNP peptides and glycosylated proBNP. CONCLUSIONS: BNP or NT-proBNP results are not transferable among the current existing immunoassays owing to their differences in cross-reactivity and ability to detect various glycosylated forms of proBNP-derived fragments. Opportunities remain to standardize and harmonize BNP and NT-proBNP assays, as well as to develop specific proBNP assays, to widen their clinical scope of use.

U2 - 10.1373/clinchem.2016.263749

DO - 10.1373/clinchem.2016.263749

M3 - Journal article

C2 - 28062628

AN - SCOPUS:85008512386

VL - 63

SP - 351

EP - 358

JO - Clinical Chemistry

JF - Clinical Chemistry

SN - 0009-9147

IS - 1

ER -

ID: 196139618