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Papers In Press, published online ahead of print August 29, 2000
Department of Pathology, University of Alabama at Birmingham, Birmingham, AL 35294-0019
Corresponding Author: murphy{at}path.uab.edu
Thrombospondin (TSP) induces reorganization of the actin cytoskeleton and restructuring of focal adhesions. This activity is localized to amino acids 17-35 in thrombospondin's N-terminal heparin binding domain and can be replicated by a peptide (hep I) with this sequence. Thrombospondin/hep I stimulate focal adhesion disassembly through a mechanism involving PI-3 kinase activation. However, the receptor for this thrombospondin sequence is unknown. We now report that calreticulin on the cell surface mediates focal adhesion disassembly by thrombospondin/hep I. A 60 kDa protein from endothelial cell detergent extracts has homology and immunoreactivity to calreticulin, binds a hep I affinity column, and neutralizes thrombospondin/hep I-mediated focal adhesion disassembly. Calreticulin on the cell surface was confirmed by biotinylation, confocal microscopy and by FACS analyses. Thrombospondin and calreticulin potentially bind through the hep I sequence, since thrombospondin-calreticulin complex formation can be blocked specifically by hep I peptide. Antibodies to calreticulin and pre-incubation of thrombospondin/hep I with GST-calreticulin block thrombospondin/hep I-mediated focal adhesion disassembly and PI-3 kinase activation, suggesting that calreticulin is a component of the thrombospondin-induced signaling cascade that regulates cytoskeletal organization. These data identify both a novel receptor for the amino terminus of thrombospondin and a distinct role for cell surface calreticulin in cell adhesion.
J. Biol. Chem, 10.1074/jbc.M005951200
Submitted on July 6, 2000
Revised on August 25, 2000
Accepted on August 29, 2000
Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin
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