Literature DB >> 27308834

Development of quantitative mass spectrometric immunoassay for serum amyloid A.

Olgica Trenchevska1, Hussein N Yassine2, Chad R Borges1, Randall W Nelson1, Dobrin Nedelkov1.   

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.

Entities:  

Keywords:  Baseline concentration; inflammation biomarker; mass spectrometry; polymorphism; posttranslational modifications; proteoforms

Year:  2016        PMID： 27308834      PMCID： PMC5253327          DOI： 10.1080/1354750X.2016.1201533

Source DB:  PubMed          Journal:  Biomarkers        ISSN： 1354-750X            Impact factor:   2.658


  55 in total

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Review 3.  C-reactive protein and serum amyloid A protein in neonatal infections.

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Review 7.  Amyloid precursors and amyloidosis in inflammatory arthritis.

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8.  Serum amyloid A1 alleles and plasma concentrations of serum amyloid A.

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9.  Detection of novel truncated forms of human serum amyloid A protein in human plasma.

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10.  Genetic effects on baseline values of C-reactive protein and serum amyloid a protein: a comparison of monozygotic and dizygotic twins.

Authors:  Alex J MacGregor; J Ruth Gallimore; Tim D Spector; Mark B Pepys
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