Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution

DOI PDF 被引用文献17件
  • Susann Schenk
    1Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
  • Edith Hintermann
    1Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
  • Martin Bilban
    1Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
  • Naohiko Koshikawa
    1Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
  • Carlo Hojilla
    2Ontario Cancer Institute/University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 2M9
  • Rama Khokha
    2Ontario Cancer Institute/University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 2M9
  • Vito Quaranta
    1Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037

書誌事項

公開日
2003-04-14
DOI
  • 10.1083/jcb.200208145
公開者
Rockefeller University Press

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説明

<jats:p>Extracellular matrix (ECM) fragments or cryptic sites unmasked by proteinases have been postulated to affect tissue remodeling and cancer progression. Therefore, the elucidation of their identities and functions is of great interest. Here, we show that matrix metalloproteinases (MMPs) generate a domain (DIII) from the ECM macromolecule laminin-5. Binding of a recombinant DIII fragment to epidermal growth factor receptor stimulates downstream signaling (mitogen-activated protein kinase), MMP-2 gene expression, and cell migration. Appearance of this cryptic ECM ligand in remodeling mammary gland coincides with MMP-mediated involution in wild-type mice, but not in tissue inhibitor of metalloproteinase 3 (TIMP-3)–deficient mice, supporting physiological regulation of DIII liberation. These findings indicate that ECM cues may operate via direct stimulation of receptor tyrosine kinases in tissue remodeling, and possibly cancer invasion.</jats:p>

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