Development of quantitative mass spectrometric immunoassay for serum amyloid A

Olgica Trenchevska; Hussein N. Yassine; Chad Borges; Randall W. Nelson; Dobrin Nedelkov

doi:10.1080/1354750X.2016.1201533

Development of quantitative mass spectrometric immunoassay for serum amyloid A

Olgica Trenchevska, Hussein N. Yassine, Chad Borges, Randall W. Nelson, Dobrin Nedelkov

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

Objective: Proteins can exist as multiple proteoforms in vivo that can have important roles in physiological and pathological states. Methods: We present the development and characterization of mass spectrometric immunoassay (MSIA) for quantitative determination of serum amyloid A (SAA) proteoforms. Results: Intra- and inter-day precision revealed CVs <10%. Against existing SAA ELISA, the developed MSIA showed good correlation according to the Altman–Bland plot. Individual concentrations of the SAA proteoforms across a cohort of 170 samples revealed 7 diverse SAA polymorphic types and 12 different proteoforms. Conclusion: The new SAA MSIA enables parallel analysis of SAA polymorphisms and quantification of all expressed SAA proteoforms, in a high-throughput and time-efficient manner.

Original language	English (US)
Pages (from-to)	743-751
Number of pages	9
Journal	Biomarkers
Volume	21
Issue number	8
DOIs	https://doi.org/10.1080/1354750X.2016.1201533
State	Published - Nov 16 2016

Keywords

Baseline concentration
inflammation biomarker
mass spectrometry
polymorphism
posttranslational modifications
proteoforms

ASJC Scopus subject areas

Biochemistry
Clinical Biochemistry
Health, Toxicology and Mutagenesis

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10.1080/1354750X.2016.1201533

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title = "Development of quantitative mass spectrometric immunoassay for serum amyloid A",

abstract = "Objective: Proteins can exist as multiple proteoforms in vivo that can have important roles in physiological and pathological states. Methods: We present the development and characterization of mass spectrometric immunoassay (MSIA) for quantitative determination of serum amyloid A (SAA) proteoforms. Results: Intra- and inter-day precision revealed CVs <10%. Against existing SAA ELISA, the developed MSIA showed good correlation according to the Altman–Bland plot. Individual concentrations of the SAA proteoforms across a cohort of 170 samples revealed 7 diverse SAA polymorphic types and 12 different proteoforms. Conclusion: The new SAA MSIA enables parallel analysis of SAA polymorphisms and quantification of all expressed SAA proteoforms, in a high-throughput and time-efficient manner.",

keywords = "Baseline concentration, inflammation biomarker, mass spectrometry, polymorphism, posttranslational modifications, proteoforms",

author = "Olgica Trenchevska and Yassine, {Hussein N.} and Chad Borges and Nelson, {Randall W.} and Dobrin Nedelkov",

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T1 - Development of quantitative mass spectrometric immunoassay for serum amyloid A

AU - Trenchevska, Olgica

AU - Yassine, Hussein N.

AU - Borges, Chad

AU - Nelson, Randall W.

AU - Nedelkov, Dobrin

PY - 2016/11/16

Y1 - 2016/11/16

N2 - Objective: Proteins can exist as multiple proteoforms in vivo that can have important roles in physiological and pathological states. Methods: We present the development and characterization of mass spectrometric immunoassay (MSIA) for quantitative determination of serum amyloid A (SAA) proteoforms. Results: Intra- and inter-day precision revealed CVs <10%. Against existing SAA ELISA, the developed MSIA showed good correlation according to the Altman–Bland plot. Individual concentrations of the SAA proteoforms across a cohort of 170 samples revealed 7 diverse SAA polymorphic types and 12 different proteoforms. Conclusion: The new SAA MSIA enables parallel analysis of SAA polymorphisms and quantification of all expressed SAA proteoforms, in a high-throughput and time-efficient manner.

AB - Objective: Proteins can exist as multiple proteoforms in vivo that can have important roles in physiological and pathological states. Methods: We present the development and characterization of mass spectrometric immunoassay (MSIA) for quantitative determination of serum amyloid A (SAA) proteoforms. Results: Intra- and inter-day precision revealed CVs <10%. Against existing SAA ELISA, the developed MSIA showed good correlation according to the Altman–Bland plot. Individual concentrations of the SAA proteoforms across a cohort of 170 samples revealed 7 diverse SAA polymorphic types and 12 different proteoforms. Conclusion: The new SAA MSIA enables parallel analysis of SAA polymorphisms and quantification of all expressed SAA proteoforms, in a high-throughput and time-efficient manner.

KW - Baseline concentration

KW - inflammation biomarker

KW - mass spectrometry

KW - polymorphism

KW - posttranslational modifications

KW - proteoforms

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Development of quantitative mass spectrometric immunoassay for serum amyloid A

Abstract

Keywords

ASJC Scopus subject areas

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