Regulation of integrin activity by MIA

Richard Bauer, Martin J Humphries, Reinhard Fässler, Andreas Winklmeier, Sue E. Craig, Anja Katrin Bosserhoff

    Research output: Contribution to journalArticlepeer-review

    Abstract

    MIA (melanoma inhibitory activity) has been identified as a small protein secreted from malignant melanoma cells, which interacts with extracellular matrix proteins including fibronectin. Here, we show that MIA negatively regulates the activity of the mitogen-activated protein kinase pathway in malignant melanoma. Using far Western blotting and co-immunoprecipitation we searched for MIA-binding cell surface proteins. We found that MIA interacts with integrin α4β1 and α5β1, leading to down-regulation of integrin activity and reduction of mitogen-activated protein kinase signaling. These findings also suggest that MIA may play a role in tumor progression and the spread of malignant melanomas via mediating detachment of cells from extracellular matrix molecules by modulating integrin activity. Inhibiting MIA functions in vivo may therefore provide a novel therapeutic strategy for metastatic melanoma disease. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.
    Original languageEnglish
    Pages (from-to)11669-11677
    Number of pages8
    JournalJournal of Biological Chemistry
    Volume281
    Issue number17
    DOIs
    Publication statusPublished - 28 Apr 2006

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