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  • Interlaboratory study on differential analysis of protein glycosylation by mass spectrometry: The ABRF glycoprotein research multi-institutional study 2012

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    Author(s)
    Leymarie, Nancy
    Griffin, Paula J
    Jonscher, Karen
    Kolarich, Daniel
    Orlando, Ron
    McComb, Mark
    Zaia, Joseph
    Aguilan, Jennifer
    Alley, William R
    Altmann, Friederich
    Ball, Lauren E
    Basumallick, Lipika
    Bazemore-Walker, Carthene R
    Behnken, Henning
    Blank, Michael A
    Brown, Kristy J
    Bunz, Svenja-Catharina
    Cairo, Christopher W
    Cipollo, John F
    Daneshfar, Rambod
    Desaire, Heather
    Drake, Richard R
    Go, Eden P
    Goldman, Radoslav
    Gruber, Clemens
    Halim, Adnan
    Hathout, Yetrib
    Hensbergen, Paul J
    Horn, David M
    Hurum, Deanna
    Jabs, Wolfgang
    Larson, Goran
    Ly, Mellisa
    Mann, Benjamin F
    Marx, Kristina
    Mechref, Yehia
    Meyer, Bernd
    Moeginger, Uwe
    Neusuess, Christian
    Nilsson, Jonas
    Novotny, Milos V
    Nyalwidhe, Julius O
    Packer, Nicolle H
    Pompach, Petr
    Reiz, Bela
    Resemann, Anja
    Rohrer, Jeffrey S
    Ruthenbeck, Alexandra
    Sanda, Miloslav
    Schulz, Jan Mirco
    Schweiger-Hufnagel, Ulrike
    Sihlbom, Carina
    Song, Ehwang
    Staples, Gregory O
    Suckau, Detlev
    Tang, Haixu
    Thaysen-Andersen, Morten
    Viner, Rosa I
    An, Yanming
    Valmuv, Leena
    Wada, Yoshinao
    Watson, Megan
    Windwarder, Markus
    Whittal, Randy
    Wuhrer, Manfred
    Zhu, Yiying
    Zou, Chunxia
    Griffith University Author(s)
    Kolarich, Daniel
    Packer, Nicki
    Year published
    2013
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    Show full item record
    Abstract
    One of the principal goals of glycoprotein research is to correlate glycan structure and function. Such correlation is necessary in order for one to understand the mechanisms whereby glycoprotein structure elaborates the functions of myriad proteins. The accurate comparison of glycoforms and quantification of glycosites are essential steps in this direction. Mass spectrometry has emerged as a powerful analytical technique in the field of glycoprotein characterization. Its sensitivity, high dynamic range, and mass accuracy provide both quantitative and sequence/structural information. As part of the 2012 ABRF Glycoprotein ...
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    One of the principal goals of glycoprotein research is to correlate glycan structure and function. Such correlation is necessary in order for one to understand the mechanisms whereby glycoprotein structure elaborates the functions of myriad proteins. The accurate comparison of glycoforms and quantification of glycosites are essential steps in this direction. Mass spectrometry has emerged as a powerful analytical technique in the field of glycoprotein characterization. Its sensitivity, high dynamic range, and mass accuracy provide both quantitative and sequence/structural information. As part of the 2012 ABRF Glycoprotein Research Group study, we explored the use of mass spectrometry and ancillary methodologies to characterize the glycoforms of two sources of human prostate specific antigen (PSA). PSA is used as a tumor marker for prostate cancer, with increasing blood levels used to distinguish between normal and cancer states. The glycans on PSA are believed to be biantennary N-linked, and it has been observed that prostate cancer tissues and cell lines contain more antennae than their benign counterparts. Thus, the ability to quantify differences in glycosylation associated with cancer has the potential to positively impact the use of PSA as a biomarker. We studied standard peptide-based proteomics/glycomics methodologies, including LC-MS/MS for peptide/glycopeptide sequencing and label-free approaches for differential quantification. We performed an interlaboratory study to determine the ability of different laboratories to correctly characterize the differences between glycoforms from two different sources using mass spectrometry methods. We used clustering analysis and ancillary statistical data treatment on the data sets submitted by participating laboratories to obtain a consensus of the glycoforms and abundances. The results demonstrate the relative strengths and weaknesses of top-down glycoproteomics, bottom-up glycoproteomics, and glycomics methods.
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    Journal Title
    Molecular and Cellular Proteomics
    Volume
    12
    Issue
    10
    DOI
    https://doi.org/10.1074/mcp.M113.030643
    Copyright Statement
    This research was originally published in Molecular & Cellular Proteomics (MCP). Leymarie et al, Interlaboratory study on differential analysis of protein glycosylation by mass spectrometry: The ABRF glycoprotein research multi-institutional study 2012, Molecular & Cellular Proteomics (MCP), 2013; 12(10): 2935-2951. Copyright the American Society for Biochemistry and Molecular Biology. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitve version.
    Subject
    Biochemistry and cell biology not elsewhere classified
    Publication URI
    http://hdl.handle.net/10072/336542
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    • Journal articles

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