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Received on November 11, 2007
Accepted on February 13, 2008
Proteomics and Protein Markers |
1 HyTest Ltd., Turku, Finland
2 Department of Biochemistry, Moscow State University, Moscow, Russia
3 Moscow Research Institute of Medical Ecology, Moscow, Russia
4 67 City Hospital, Moscow, Russia
5 Moscow State Medico-Stomatological University, Moscow, Russia
6 Hennepin County Medical Center, University of Minnesota School of Medicine, Department of Laboratory Medicine and Pathology, Minneapolis, MN
* To whom correspondence should be addressed. E-mail: karina.seferian{at}hytest.fi.
BACKGROUND: Brain natriuretic peptide (BNP) or NT-proBNP (N-terminal fragment of BNP precursor) measurements are recommended as aids in diagnosis and prognosis of patients with heart failure. Recently it has been shown that proBNP is O-glycosylated in human blood. The goal of this study was to map sites on the NT-proBNP molecule that should be recognized by antibodies used in optimal NT-proBNP assays.
METHODS: We analyzed endogenous NT-proBNP by several immunochemical methods using a broad panel of monoclonal antibodies specific to different epitopes of the NT-proBNP molecule.
RESULTS: Treatment of endogenous NT-proBNP by a mixture of glycosidases resulted in significant improvement of the interaction between deglycosylated NT-proBNP and monoclonal antibodies (MAbs) specific to the mid-fragment of the molecule. MAbs specific to the N- and C-terminal parts of NT-proBNP (epitopes 13–24 and 63–76) were able to recognize glycosylated and deglycosylated protein with similar efficiency.
CONCLUSIONS: The central part of endogenous NT-proBNP is glycosylated, making it almost "invisible" for the antibodies specific to the mid-fragment of the molecule. Thus sandwich assays using even one antibody (poly- or monoclonal) specific to the central part of the molecule could underestimate the real concentration of endogenous NT-proBNP. MAbs specific to the N- and C-terminal parts of NT-proBNP (epitopes 13–24 and 63–76) are the best candidates to be used in an assay for optimal NT-proBNP immunodetection.
The following articles in journals at HighWire Press have cited this article:
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  A. K. Saenger, D. A. Dalenberg, S. C. Bryant, S. K. Grebe, and A. S. Jaffe Pediatric Brain Natriuretic Peptide Concentrations Vary with Age and Sex and Appear to Be Modulated by Testosterone Clin. Chem., October 1, 2009; 55(10): 1869 - 1875. [Abstract] [Full Text] [PDF]
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J. Mair Clinical Significance of Pro-B-Type Natriuretic Peptide Glycosylation and Processing Clin. Chem., March 1, 2009; 55(3): 394 - 397. [Full Text] [PDF]
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A. G. Semenov, A. B. Postnikov, N. N. Tamm, K. R. Seferian, N. S. Karpova, M. N. Bloshchitsyna, E. V. Koshkina, M. I. Krasnoselsky, D. V. Serebryanaya, and A. G. Katrukha Processing of Pro-Brain Natriuretic Peptide Is Suppressed by O-Glycosylation in the Region Close to the Cleavage Site Clin. Chem., March 1, 2009; 55(3): 489 - 498. [Abstract] [Full Text] [PDF]
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 L. Frankenstein, A. Remppis, M. Nelles, B. Schaelling, D. Schellberg, H. Katus, and C. Zugck Relation of N-terminal pro-brain natriuretic peptide levels and their prognostic power in chronic stable heart failure to obesity status Eur. Heart J., November 1, 2008; 29(21): 2634 - 2640. [Abstract] [Full Text] [PDF]
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J. P. Goetze, U. Dahlstrom, J. F. Rehfeld, and U. Alehagen Impact of Epitope Specificity and Precursor Maturation in Pro-B-Type Natriuretic Peptide Measurement Clin. Chem., November 1, 2008; 54(11): 1780 - 1787. [Abstract] [Full Text] [PDF]
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