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J. Biol. Chem., Vol. 275, Issue 46, 36358-36368, November 17, 2000
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From the Department of Pathology, Division of Molecular and
Cellular Pathology and the Cell Adhesion and Matrix Research Center,
University of Alabama at Birmingham, Birmingham, Alabama 35294 and
the § MRC Immunochemistry Unit, Department of Biochemistry,
University of Oxford, Oxford OX1 3RE
England, United Kingdom
Thrombospondin induces reorganization of the
actin cytoskeleton and restructuring of focal adhesions. This activity
is localized to amino acids 17-35 in the N-terminal heparin-binding
domain of thrombospondin and can be replicated by a peptide (hep
I) with this sequence. Thrombospondin/hep I stimulate focal adhesion
disassembly through a mechanism involving phosphoinositide 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 fluorescence-activated cell sorting
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 preincubation of thrombospondin/hep I with glutathione
S-transferase-calreticulin block thrombospondin/hep
I-mediated focal adhesion disassembly and phosphoinositide 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 N
terminus of thrombospondin and a distinct role for cell surface
calreticulin in cell adhesion.
Thrombospondin Mediates Focal Adhesion Disassembly through
Interactions with Cell Surface Calreticulin*
,,
*
This work was supported by National Institutes of Health
Grant HL44575, by an American Heart Association Established
Investigatorship, Genentech special awardee (to J. E. M. U.), and by
Arthritis Research Campaign Grant EO521 (to P. E.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
These two authors contributed equally to this work.
¶
To whom correspondence should be addressed: Dept. of
Pathology, University of Alabama at Birmingham, G038 Volker Hall, 1670 University Blvd., Birmingham, AL 35294-0019. Tel.: 205-934-0415; Fax:
205-934-1775; E-mail: murphy@uab.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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