ADAM15 Is Functionally Associated with the Metastatic Progression of Human Bladder Cancer

• Published in: PloS one Vol. 11; no. 3; p. e0150138
• Main Authors: Lorenzatti Hiles, Guadalupe, Bucheit, Amanda, Rubin, John R., Hayward, Alexandra, Cates, Angelica L., Day, Kathleen C., El-Sawy, Layla, Kunju, L. Priya, Daignault, Stephanie, Lee, Cheryl T., Liebert, Monica, Hussain, Maha, Day, Mark L.
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 01.03.2016; Public Library of Science (PLoS)
• Subjects: Aberration; ADAM Proteins - genetics; ADAM Proteins - metabolism; Adhesion; Analysis; Biological activity; Biology and Life Sciences; Bladder; Bladder cancer; Breast cancer; Cancer; Cancer metastasis; Cancer therapies; Catalysis; Cell adhesion; Cell adhesion & migration; Cell adhesion molecules; Cell Line, Tumor; Cell migration; Cell Movement - genetics; Cell Proliferation - genetics; Databases, Genetic; Development and progression; Disease Progression; Endothelium; Epidermal growth factor; Gene expression; Genomes; Growth factors; Health aspects; Humans; Immunoreactivity; Invasiveness; Kinases; Medicine and Health Sciences; Membrane Proteins - genetics; Membrane Proteins - metabolism; Metastases; Neoplasm Metastasis - genetics; Neoplasm Metastasis - pathology; Neoplasm Staging; Prostate cancer; Quality; Research and Analysis Methods; Risk factors; Signaling; Staining; Switches; Tissues; Tumor cell lines; Tumor cells; Tumors; Urinary bladder; Urinary Bladder Neoplasms - genetics; Urinary Bladder Neoplasms - metabolism; Urinary Bladder Neoplasms - pathology; Viability; Wound Healing - genetics; Xenografts; Ann Arbor Michigan; United States > US; Michigan

ADAM15 is a member of a family of catalytically active disintegrin membrane metalloproteinases that function as molecular signaling switches, shed membrane bound growth factors and/or cleave and inactivate cell adhesion molecules. Aberrant metalloproteinase function of ADAM15 may contribute to tumor...