JournalLaboratory investigation; a journal of technical methods and pathology
PubMed ID16894352
A disintegrin and metalloproteinase (ADAM)15 is upregulated in some tissues undergoing remodeling. This glycoprotein is characterized by adhesive function through its interaction with members of the integrin family and protease properties. The goal of this work was to describe the tissue distribution of ADAM15 and its spatial relationship with its ... More
Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases.
AuthorsPoghosyan Z, Robbins SM, Houslay MD, Webster A, Murphy G, Edwards DR
JournalJ Biol Chem
PubMed ID11741929
'The adamalysins (ADAMs) are transmembrane glycoproteins involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules. Many ADAM cytoplasmic domains are proline-rich and have potential phosphorylation sites. We show here that the cytoplasmic domain of ADAM15, metargidin, can interact specifically with Src family protein-tyrosine kinases (PTKs) and ... More
Expression of a disintegrin-like protein in cultured human vascular cells and in vivo.
AuthorsHerren B, Raines EW, Ross R
JournalFASEB J
PubMed ID9039960
Metalloproteinase-like, disintegrin-like, and cysteine-rich proteins (MDCs) are potential novel regulators of cell-cell and cell-matrix interactions, as well as of matrix degradation. We have asked whether MDCs are expressed in cultured diploid vascular cells, and have identified MDC 15 in human aortic smooth muscle (SMC) and umbilical vein endothelium (HUVEC). MDC ... More
ADAM15 disintegrin is associated with aggressive prostate and breast cancer disease.
AuthorsKuefer R, Day KC, Kleer CG, Sabel MS, Hofer MD, Varambally S, Zorn CS, Chinnaiyan AM, Rubin MA, Day ML
JournalNeoplasia
PubMed ID16756724
The aim of the current study was to evaluate the expression of ADAM15 disintegrin (ADAM15) in a broad spectrum of human tumors. The transcript for ADAM15 was found to be highly upregulated in a variety of tumor cDNA expression arrays. ADAM15 protein expression was examined in tissue microarrays (TMAs) consisting ... More
ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin.
AuthorsHam C, Levkau B, Raines EW, Herren B
JournalExp Cell Res
PubMed ID12243749
ADAM15 belongs to the family of proteins containing disintegrin and metalloprotease domains (ADAM) that have been implicated in cell adhesion via integrin binding and shedding of cell surface molecules. Here we provide the first report on the localization of an ADAM in adherens junctions. We show that ADAM15 colocalizes with ... More
ADAM15 decreases integrin alphavbeta3/vitronectin-mediated ovarian cancer cell adhesion and motility in an RGD-dependent fashion.
AuthorsBeck V, Herold H, Benge A, Luber B, Hutzler P, Tschesche H, Kessler H, Schmitt M, Geppert HG, Reuning U
JournalInt J Biochem Cell Biol
PubMed ID15618016
We have recently described that integrin alphavbeta3 upon interaction with its major extracellular matrix ligand vitronectin induces adhesion, motility, and proliferation of human ovarian cancer cells. Due to the important function of alphavbeta3 in cancer cell biology, it has been the effort of many scientific approaches to specifically target alphavbeta3-mediated ... More