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Analysis of protein isoforms: Can we do it better?

Authors

  • Miroslava Stastna,

    Corresponding author
    1. Institute of Analytical Chemistry of the ASCR, Brno, Czech Republic
    • Johns Hopkins Bayview Proteomics Center, Department of Medicine, Division of Cardiology, School of Medicine, Johns Hopkins University, Baltimore, MD, USA
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  • Jennifer E. Van Eyk

    1. Johns Hopkins Bayview Proteomics Center, Department of Medicine, Division of Cardiology, School of Medicine, Johns Hopkins University, Baltimore, MD, USA
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  • Colour Online: See the article online to view Fig. 1 in colour.

Correspondence: Dr. Miroslava Stastna, Johns Hopkins University, 5200 Eastern Avenue, Mason F. Lord Bldg., Center Tower, Rm. 601, Baltimore, 21224 MD, USA

E-mail: mstastn1@jhmi.edu

Fax: 410-550-8512

Abstract

Protein isoforms/splice variants can play important roles in various biological processes and can potentially be used as biomarkers or therapeutic targets/mediators. Thus, there is a need for efficient and, importantly, accurate methods to distinguish and quantify specific protein isoforms. Since protein isoforms can share a high percentage of amino acid sequence homology and dramatically differ in their cellular concentration, the task for accuracy and efficiency in methodology and instrumentation is challenging. The analysis of intact proteins has been perceived to provide a more accurate and complete result for isoform identification/quantification in comparison to analysis of the corresponding peptides that arise from protein enzymatic digestion. Recently, novel approaches have been explored and developed that can possess the accuracy and reliability important for protein isoform differentiation and isoform-specific peptide targeting. In this review, we discuss the recent development in methodology and instrumentation for enhanced detection of protein isoforms as well as the examples of their biological importance.

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