Abstract: A gain-of-function retroviral cDNA screen reveals that Coco, a secreted antagonist of TGF-? ligands, induces solitary mammary carcinoma cells, which have disseminated to others sites and undergone an extended period of dormancy, to exit from dormancy at lung metastatic sites. Evidence indicates that Coco awakens tumor progenitor cells that have extravasated into the lung by inhibiting stroma-derived Bone Morphogenetic Proteins (BMP). Whereas Coco enhances the manifestation of traits associated with cancer stem cells, activation of canonical BMP signaling suppresses these processes. Expression of Coco correlates with lung metastatic capacity in a number of human breast cancer cell lines and induces a gene expression signature that predicts metastatic relapse to the lung but not to the bone in advanced primary tumors.

Abstract: Inhibitors of a6b4 integrin that target beta 4 are used as therapeutic agents to inhibit tumorigensis in individuals, including humans, of tumors that express a6b4 integrin. The therapeutic agent may be an antibody or a small molecule, for example a laminin-5 analog, which binds to a6b4 integrin and inhibits its normal function. The therapeutic agent may also be a chemical species that interferes with the production of beta 4, including for example an antisense or RNAi species. The therapeutic agent is administered to the tissue or patient in a therapeutically effective amount. The therapeutic agent may be used as a single agent or in combination with other therapies, especially those directed toward suppressing the activity of RPTKs known to cooperate with a6b4, including but not limited to ErbB2, EGF-R, Met, and Ron.

Abstract: The present invention provides a substantially pure integrin characterized in that it consists of an .alpha..sub.v and a .beta..sub.1 subunit. The receptor binds to fibronectin and GRGDSPK but does not bind to vitronectin. The .alpha..sub.v .beta..sub.1 receptor can be used to determine the presence of ligands for the receptor.

Abstract: The present invention provides a substantially pure integrin-type receptor characterized in that it consists of an .alpha..sub.v and a .beta..sub.1 subunit. The .alpha..sub.v .beta..sub.1 integrin binds to fibronectin and GRGDSPK but does not bind to vitronectin. The .alpha..sub.v .beta..sub.1 integrin can be used to determine the presence of a .alpha..sub.v .beta..sub.1 ligand and to develop adhesion peptides specific for the various integrins. The presence of the .alpha..sub.v .beta..sub.1 integrin can be used to assess ability of cells to adhere to fibronectin.