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ADAM12‐mediated focal adhesion formation is differently regulated by β1 and β3 integrins
Author(s) -
Thodeti Charles Kumar,
Fröhlich Camilla,
Nielsen Christian Kamp,
Takada Yoshikazu,
Fässler Reinhard,
Albrechtsen Reidar,
Wewer Ulla M.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.09.024
Subject(s) - integrin , disintegrin , focal adhesion , microbiology and biotechnology , rhoa , cell adhesion , adhesion , chemistry , metalloproteinase , cell , biology , matrix metalloproteinase , signal transduction , biochemistry , organic chemistry
ADAM12, a disintegrin and metalloprotease, has been demonstrated to be upregulated in human malignant tumors and to accelerate the malignant phenotype in a mouse model for breast cancer. ADAM12 is a substrate for β1 integrins and may affect tumor and stromal cell behavior through its binding to β1 integrins. Here, we report that cells deficient in β1 integrin or overexpressing β3 integrin can bind to recombinant full‐length human ADAM12 via β3 integrin. Furthermore, cell binding to ADAM12 via β3 integrin results in the formation of focal adhesions, which are not formed upon β1 integrin‐mediated cell attachment. We also show that RhoA is involved in β3 integrin‐mediated focal adhesion formation.