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Single-Step Procedure for the Isolation of Proteins at Near-Native Conditions from Mammalian Tissue for Proteomic Analysis on Antibody Microarrays

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Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Proteome Res. 2010, 9, 2, 963-971
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    Single-Step Procedure for the Isolation of Proteins at Near-Native Conditions from Mammalian Tissue for Proteomic Analysis on Antibody Microarrays
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    Division of Functional Genome Analysis, Deutsches Krebsforschungszentrum (DKFZ), Im Neuenheimer Feld 580, 69120 Heidelberg, Germany, and Department of General Surgery, University of Heidelberg, Im Neuenheimer Feld 110, 69120 Heidelberg, Germany
    * Corresponding author: Mohamed Saiel Saeed Alhamdani, Functional Genome Analysis, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 580, D-69120 Heidelberg, Germany. Tel.: [49] (6221) 42-4684. Fax: [49] (6221) 42-4687. E-mail: [email protected]
    †Deutsches Krebsforschungszentrum (DKFZ).
    ‡University of Heidelberg.
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    Journal of Proteome Research

    Cite this: J. Proteome Res. 2010, 9, 2, 963–971
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    https://doi.org/10.1021/pr900844q
    Published January 5, 2010
    Copyright © 2010 American Chemical Society
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    Abstract

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    The process of extracting comprehensive proteome representations is a crucial step for many proteomic studies. While antibody microarrays are an evolving and promising methodology in proteomics, the issue of protein extraction from tissues for this kind of analysis has never been addressed. Here, we describe a single-step extraction buffer for the isolation of proteins from mammalian tissues under native conditions in an effective and reproducible manner. Protein was extracted from cell lines BxPC-3 and SU.86.86, rat organs (pancreas, liver, heart and lung) and human pancreatic cancer tissues using several buffer systems that contained individual nonionic or zwitterionic detergents in comparison to commercial extraction buffers. Also, detergent combinations were used that included at least one polymeric phenylethylene glycol, a long-chain amidosulfobetaine, cholate and a zwitterionic detergent. Extracts were analyzed for protein quantity and quality. The detergent cocktails exhibited superior extraction capacity. Additionally, they demonstrated a substantially higher recovery of membrane and compartmental proteins as well as much better preservation of protein functionality. Also, they did not interfere with subsequent analysis steps such as labeling. In Western blot and antibody microarray assays, they outperformed the other buffer systems, indicating that they should also be useful for other types of proteomic studies.

    Copyright © 2010 American Chemical Society

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    Supporting Information

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    Figure 1S, antibody microarray results of the other 28 proteins for which no Western blot experiments were conducted. The values are arbitrary units (AU) of the mean of the sum of medians for signal intensities from three arrays. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Journal of Proteome Research

    Cite this: J. Proteome Res. 2010, 9, 2, 963–971
    Click to copy citationCitation copied!
    https://doi.org/10.1021/pr900844q
    Published January 5, 2010
    Copyright © 2010 American Chemical Society
    Request reuse permissions

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