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A 2D-DIGE Approach To Identify Proteins Involved in Inside-Out Control of Integrins

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    A 2D-DIGE Approach To Identify Proteins Involved in Inside-Out Control of Integrins
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    Department of Respiratory Medicine, University Medical Center, Utrecht, The Netherlands, and Department of Metabolic and Endocrine Diseases, University Medical Center, Utrecht, WKZ, and Netherlands Metabolomics Centre, The Netherlands
    * To whom correspondence should be addressed: Laurien H. Ulfman, Department of Respiratory Medicine, University Medical Center, H.02.128, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands.
    †Department of Respiratory Medicine.
    ‡Department of Metabolic and Endocrine Diseases, and Netherlands Metabolomics Centre.
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    Journal of Proteome Research

    Cite this: J. Proteome Res. 2009, 8, 8, 3824–3833
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    https://doi.org/10.1021/pr8010815
    Published June 8, 2009
    Copyright © 2009 American Chemical Society
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    Abstract

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    Leukocyte integrins are functionally regulated by “inside-out” signaling, meaning that stimulus-induced signaling pathways act on the intracellular integrin tail and induce activation of the receptor at the outside. Both a change in conformation (affinity) and in clustering (avidity/valency) of the receptors has been described to occur. This inside-out signaling is essential for adequate migration of leukocytes to inflammatory sites; however, the exact underlying mechanism is not known. We used two variants of a mouse acute lymphocytic leukemia cell line (L1210), a suspension (L1210-S) and an adherent (L1210-A) variant that were characterized by nonactivated and activated integrins (β1, β2 and β3), respectively. L1210-S and L1210-A cells were compared on protein expression profiles by two-dimensional fluorescence difference in-gel electrophoresis (2D-DIGE). We found 86 protein spots that were more than 1.25-fold different between L1210-A and L1210-S. Only 4 protein spots were more than 2.5-fold different. We identified 29 proteins by mass spectrometry among which were gelsolin, L-plastin, and Rho GTPase dissociation inhibitor 2. These proteins were upregulated in the L1210-A cells versus L1210-S, which was verified by Western blot analysis. Overexpression of gelsolin in U937 resulted in increased high affinity integrin expression and cell adhesion. Comparison of functionally different cell lines from similar origin by 2D-DIGE might be a successful approach to identify regulatory proteins involved in integrin inside-out control.

    Copyright © 2009 American Chemical Society

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    Supporting Information

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    2D-DIGE analysis of L1210-S and L1210-A; BVA match analysis of L1210 gels; scatter plots of L1210-S and -A; table of differentially expressed proteins; MS/MS spectra of single peptide identifications; table of mass spectrometry and database search results; table of function keywords from Swiss-Prot of identified proteins. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cited By

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    This article is cited by 19 publications.

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    Journal of Proteome Research

    Cite this: J. Proteome Res. 2009, 8, 8, 3824–3833
    Click to copy citationCitation copied!
    https://doi.org/10.1021/pr8010815
    Published June 8, 2009
    Copyright © 2009 American Chemical Society
    Request reuse permissions

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