NDLI: Interlaboratory Study on Differential Analysis of Protein Glycosylation by Mass Spectrometry: The ABRF Glycoprotein Research Multi-Institutional Study 2012*

Content Provider	PubMed Central
Author	Leymarie, Nancy Griffin, Paula J. Jonscher, Karen Daniel, Kolarich Orlando, Ron Mccomb, Mark Zaia, Joseph Jennifer, Aguilan 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 Heather, Desaire 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, Göran Ly, Mellisa Mann, Benjamin F. Marx, Kristina Yehia, Mechref Meyer, Bernd Möginger, Uwe Christian, Neusüβ Nilsson, Jonas Novotny, Milos V. Nyalwidhe, Julius O. Packer, Nicolle H. Petr, Pompach Bela, Reiz Resemann, Anja Rohrer, Jeffrey S. Ruthenbeck, Alexandra Sanda, Miloslav Schulz, Jan Mirco Ulrike, Schweiger-hufnagel Carina, Sihlbom Song, Ehwang Staples, Gregory O. Suckau, Detlev Tang, Haixu Morten, Thaysen-andersen Viner, Rosa I. An, Yanming Valmu, Leena Wada, Yoshinao Watson, Megan Markus, Windwarder Whittal, Randy Wuhrer, Manfred Zhu, Yiying Zou, Chunxia
Copyright Year	2013
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 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.
Related Links	http://dx.doi.org/10.1074/mcp.M113.030643
Ending Page	2951
Page Count	17
Starting Page	2935
File Format	PDF
ISSN	15359484
e-ISSN	15359484
Journal	Molecular & Cellular Proteomics : MCP
Issue Number	10
Volume Number	12
Language	English
Publisher	The American Society for Biochemistry and Molecular Biology
Publisher Date	2013-10-01
Access Restriction	Open
Rights Holder	The American Society for Biochemistry and Molecular Biology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Analytical Chemistry Molecular Biology Biochemistry

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