@article{8b7882f05a4f11dd8d9f000ea68e967b,
title = "ADAM12-mediated focal adhesion formation is differently regulated by beta1 and beta3 integrins.",
abstract = "ADAM12, adisintegrin 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 beta1 integrins and may affect tumor and stromal cell behavior through its binding to beta1 integrins. Here, we report that cells deficient in beta1 integrin or overexpressing beta3 integrin can bind to recombinant full-length human ADAM12 via beta3 integrin. Furthermore, cell binding to ADAM12 via beta3 integrin results in the formation of focal adhesions, which are not formed upon beta1 integrin-mediated cell attachment. We also show that RhoA is involved in beta3 integrin-mediated focal adhesion formation.",
author = "Thodeti, {Charles Kumar} and Camilla Frohlich and Nielsen, {Christian Kamp} and Yoshikazu Takada and Reinhard F{\"a}ssler and Reidar Albrechtsen and Wewer, {Ulla M}",
note = "Keywords: ADAM Proteins; Antigens, CD29; Cell Line, Tumor; Focal Adhesions; Humans; Integrin beta3; Membrane Proteins; Recombinant Proteins; Up-Regulation; rhoA GTP-Binding Protein",
year = "2005",
doi = "10.1016/j.febslet.2005.09.024",
language = "English",
volume = "579",
pages = "5589--95",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "25",
}
