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MDC-9 is a widely expressed member of the metalloproteinase/disintegrin/cysteine-rich protein family. The disintegrin domain of MDC-9 lacks an RGD motif but has recently been reported to bind the alpha(6)beta(1) integrin; however, it is unclear whether MDC-9 can bind other integrins. In the present study myeloma cells, but not lymphoblastoid cells, were shown to bind to immobilised, recombinantly expressed MDC-9 disintegrin domain (A9dis). Binding was divalent cation-dependent, being supported by Mn(2+) and Ca(2+). Adhesion of myeloma cells to A9dis was completely inhibited by an antibody to the alpha(v)beta(5) integrin but not by antibodies to other subunits. RGD-containing peptides had no effect on binding, suggesting that MDC-9 interacts with alpha(v)beta(5) in an RGD-independent manner. Flow cytometric analyses demonstrated that myeloma cells, but not lymphoblastoid cells, expressed alpha(v)beta(5) on the cell membrane. These data indicated that the disintegrin domain of MDC-9 can function as an adhesion molecule by interacting with an alpha(v)beta(5) integrin.

Original publication

DOI

10.1006/bbrc.2000.4155

Type

Journal article

Journal

Biochem biophys res commun

Publication Date

19/01/2001

Volume

280

Pages

574 - 580

Keywords

ADAM Proteins, Cell Adhesion Molecules, Disintegrins, Flow Cytometry, Humans, Integrins, Lymphoma, Membrane Proteins, Metalloendopeptidases, Multiple Myeloma, Muscle Proteins, Oligopeptides, Peptide Fragments, Protein Binding, Protein Structure, Tertiary, Receptors, Vitronectin, Recombinant Fusion Proteins, Tumor Cells, Cultured