Trenchevska, Olgica

Preferred name
Trenchevska, Olgica
Official Name
Trenchevska, Olgica
Main Affiliation
Email
olja@pmf.ukim.mk

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2010 - 20114

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Now showing 1 - 4 of 4
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    Item type:Publication,
    Quantitative mass spectrometry evaluation of human retinol binding protein 4 and related variants
    (Public Library of Science (PLoS), 2011-03-30)
    Kiernan, Urban A
    ;
    Phillips, David A
    ;
    ;
    Nedelkov, Dobrin
    Retinol Binding Protein 4 (RBP4) is an exciting new biomarker for the determination of insulin resistance and type 2 diabetes. It is known that circulating RBP4 resides in multiple variants which may provide enhanced clinical utility, but conventional immunoassay methods are blind to such differences. A Mass Spectrometric immunoassay (MSIA) technology that can quantitate total RBP4 as well as individual isoforms may provide an enhanced analysis for this biomarker.
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    Mass spectrometric immunoassay for quantitative determination of protein biomarker isoforms
    (American Chemical Society (ACS), 2010-11-05)
    ;
    Kamcheva, Elena
    ;
    Nedelkov, Dobrin
    Protein biomarkers are essential in assessing pathogenic processes. The impetus for finding new biomarkers has been accelerated by the arrival of the "omics" technologies. However, equally important is the rediscovery of existing biomarkers with these new approaches as novel variants can be discovered that can improve their utility. Presented here is a mass spectrometric immunoassay method for quantitative determination of β-2-microglobulin, an established biomarker used in the diagnosis of active rheumatoid arthritis and kidney disease, and its structural variant, cleaved at and deficient in lysine-58 (ΔK58-b2m). β-Lactoglobulin was incorporated into the assay as an internal reference standard, serving as normalization point for β-2-microglobulin quantification. The precision, linearity, and recovery characteristics of the assay were established. The new assay was also benchmarked against existing β-2-microglobulin ELISA. The assay was utilized to determine the individual concentration of β-2-microglobulin and its variant across a larger cohort of samples, demonstrating the ability to simultaneously quantify both proteins.
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    Targeted quantitative mass spectrometric immunoassay for human protein variants
    (Springer Science and Business Media LLC, 2011-04-08)
    ;
    Nedelkov, Dobrin
    Post-translational modifications and genetic variations give rise to protein variants that significantly increase the complexity of the human proteome. Modified proteins also play an important role in biological processes. While sandwich immunoassays are routinely used to determine protein concentrations, they are oblivious to protein variants that may serve as biomarkers with better sensitivity and specificity than their wild-type proteins. Mass spectrometry, coupled to immunoaffinity separations, can provide an efficient mean for simultaneous detection and quantification of protein variants.
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    Mass spectrometric immunoassay for quantitative determination of transthyretin and its variants
    (Wiley, 2011-09)
    ;
    Kamcheva, Elena
    ;
    Nedelkov, Dobrin
    Transthyretin (TTR, or prealbumin) is a tetrameric protein found in plasma and cerebrospinal fluid. Its major role is to transport thyroid hormones (thyroxin-T4) and retinol (through association with retinol-binding protein). TTR has been studied extensively due to the great number of point mutations that result in sequence heterogeneity. Many of these variants are associated with pathological conditions that result in extracellular deposition of amyloid fibers in tissues. In this work, we have developed a rapid mass spectrometric immunoassay for determination and quantification of TTR and its variants from human serum and plasma samples. The assay was fully characterized in terms of its precision, linearity and recovery characteristics. The new assay was also compared with a conventional TTR ELISA. Furthermore, we have applied the optimized method to analyze TTR and its modifications in 44 human plasma samples, and in the process optimized a method for TTR proteolytic digestion and identification of point mutations.