Diverse matrix metalloproteinase functions regulate cancer amoeboid migration View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2014-12

AUTHORS

Jose L. Orgaz, Pahini Pandya, Rimple Dalmeida, Panagiotis Karagiannis, Berta Sanchez-Laorden, Amaya Viros, Jean Albrengues, Frank O. Nestle, Anne J. Ridley, Cedric Gaggioli, Richard Marais, Sophia N. Karagiannis, Victoria Sanz-Moreno

ABSTRACT

Rounded-amoeboid cancer cells use actomyosin contractility driven by Rho-ROCK and JAK-STAT3 to migrate efficiently. It has been suggested that rounded-amoeboid cancer cells do not require matrix metalloproteinases (MMPs) to invade. Here we compare MMP levels in rounded-amoeboid and elongated-mesenchymal melanoma cells. Surprisingly, we find that rounded-amoeboid melanoma cells secrete higher levels of several MMPs, including collagenase MMP-13 and gelatinase MMP-9. As a result, rounded-amoeboid melanoma cells degrade collagen I more efficiently than elongated-mesenchymal cells. Furthermore, using a non-catalytic mechanism, MMP-9 promotes rounded-amoeboid 3D migration through regulation of actomyosin contractility via CD44 receptor. MMP-9 is upregulated in a panel of rounded-amoeboid compared with elongated-mesenchymal melanoma cell lines and its levels are controlled by ROCK-JAK-STAT3 signalling. MMP-9 expression increases during melanoma progression and it is particularly prominent in the invasive fronts of lesions, correlating with cell roundness. Therefore, rounded-amoeboid cells use both catalytic and non-catalytic activities of MMPs for invasion. More... »

PAGES

4255

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/ncomms5255

    DOI

    http://dx.doi.org/10.1038/ncomms5255

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1048945971

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/24963846


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