Thrombospondin Mediates Focal Adhesion Disassembly through Interactions with Cell Surface Calreticulin
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 stimula...
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| Veröffentlicht in: | The Journal of biological chemistry 2000-11, Vol.275 (46), p.36358-36368 |
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| creator | Goicoechea, Silvia Orr, Anthony Wayne Pallero, Manuel Antonio Eggleton, Paul Murphy-Ullrich, Joanne E. |
| description | 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 glutathioneS-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. |
| doi_str_mv | 10.1074/jbc.M005951200 |
| format | Article |
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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 glutathioneS-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.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M005951200</identifier><identifier>PMID: 10964924</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Antibodies - immunology ; Antibodies - pharmacology ; Biotinylation ; Calcium-Binding Proteins - chemistry ; Calcium-Binding Proteins - immunology ; Calcium-Binding Proteins - isolation & purification ; Calcium-Binding Proteins - metabolism ; Calreticulin ; Cattle ; CD36 Antigens - chemistry ; CD36 Antigens - immunology ; CD36 Antigens - isolation & purification ; CD36 Antigens - metabolism ; Cells, Cultured ; Chromatography, Affinity ; Cytoskeleton - drug effects ; Cytoskeleton - metabolism ; Endothelium, Vascular - chemistry ; Endothelium, Vascular - cytology ; Endothelium, Vascular - drug effects ; Endothelium, Vascular - metabolism ; Enzyme Activation - drug effects ; Flow Cytometry ; Fluorescent Antibody Technique ; Focal Adhesions - chemistry ; Focal Adhesions - drug effects ; Focal Adhesions - metabolism ; Humans ; Macromolecular Substances ; Membrane Proteins - chemistry ; Membrane Proteins - immunology ; Membrane Proteins - isolation & purification ; Membrane Proteins - metabolism ; Peptide Fragments - chemistry ; Peptide Fragments - immunology ; Peptide Fragments - metabolism ; Peptide Fragments - pharmacology ; Phosphatidylinositol 3-Kinases - metabolism ; Ribonucleoproteins - chemistry ; Ribonucleoproteins - immunology ; Ribonucleoproteins - isolation & purification ; Ribonucleoproteins - metabolism ; Sequence Homology, Amino Acid ; Thrombospondins - antagonists & inhibitors ; Thrombospondins - metabolism</subject><ispartof>The Journal of biological chemistry, 2000-11, Vol.275 (46), p.36358-36368</ispartof><rights>2000 © 2000 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-20d9ae2a560a802604d99565642f9b85119d375fa7e2ff25df275a4c602bee6f3</citedby><cites>FETCH-LOGICAL-c499t-20d9ae2a560a802604d99565642f9b85119d375fa7e2ff25df275a4c602bee6f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27907,27908</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10964924$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Goicoechea, Silvia</creatorcontrib><creatorcontrib>Orr, Anthony Wayne</creatorcontrib><creatorcontrib>Pallero, Manuel Antonio</creatorcontrib><creatorcontrib>Eggleton, Paul</creatorcontrib><creatorcontrib>Murphy-Ullrich, Joanne E.</creatorcontrib><title>Thrombospondin Mediates Focal Adhesion Disassembly through Interactions with Cell Surface Calreticulin</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>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 glutathioneS-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.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies - immunology</subject><subject>Antibodies - pharmacology</subject><subject>Biotinylation</subject><subject>Calcium-Binding Proteins - chemistry</subject><subject>Calcium-Binding Proteins - immunology</subject><subject>Calcium-Binding Proteins - isolation & purification</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Calreticulin</subject><subject>Cattle</subject><subject>CD36 Antigens - chemistry</subject><subject>CD36 Antigens - immunology</subject><subject>CD36 Antigens - isolation & purification</subject><subject>CD36 Antigens - metabolism</subject><subject>Cells, Cultured</subject><subject>Chromatography, Affinity</subject><subject>Cytoskeleton - drug effects</subject><subject>Cytoskeleton - metabolism</subject><subject>Endothelium, Vascular - chemistry</subject><subject>Endothelium, Vascular - cytology</subject><subject>Endothelium, Vascular - drug effects</subject><subject>Endothelium, Vascular - metabolism</subject><subject>Enzyme Activation - drug effects</subject><subject>Flow Cytometry</subject><subject>Fluorescent Antibody Technique</subject><subject>Focal Adhesions - chemistry</subject><subject>Focal Adhesions - drug effects</subject><subject>Focal Adhesions - metabolism</subject><subject>Humans</subject><subject>Macromolecular Substances</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - immunology</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - immunology</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptide Fragments - pharmacology</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>Ribonucleoproteins - chemistry</subject><subject>Ribonucleoproteins - immunology</subject><subject>Ribonucleoproteins - isolation & purification</subject><subject>Ribonucleoproteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Thrombospondins - antagonists & inhibitors</subject><subject>Thrombospondins - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kDtPHDEURq2IKCyPljJyQTvLtcf2jku0CQ8JlCJESmd57GvGaB4rezaIf4-jQYIGN7fw-e7jEHLGYM1gIy6eWre-B5BaMg7whawYNHVVS_b3gKwAOKs0l80hOcr5CcoTmn0jhwy0EpqLFQkPXZqGdsq7afRxpPfoo50x06vJ2Z5e-g5znEb6I2abMw5t_0LnEtk_dvR2nDFZN5f_TJ_j3NEt9j39vU_BOqRb2yeco9v3cTwhX4PtM56-1WPy5-rnw_amuvt1fbu9vKuc0HquOHhtkVupwDbAFQivtVRSCR5020jGtK83MtgN8hC49IFvpBVOAW8RVaiPyXrp69KUc8JgdikONr0YBua_MFOEmXdhJfB9Cez27YD-A74YKsD5AnTxsXuOCU0bJ9fhYMpoI5SpVS2bgjULhuW6fxGTyS7i6IrOhG42foqfrfAKiQeGsA</recordid><startdate>20001117</startdate><enddate>20001117</enddate><creator>Goicoechea, Silvia</creator><creator>Orr, Anthony Wayne</creator><creator>Pallero, Manuel Antonio</creator><creator>Eggleton, Paul</creator><creator>Murphy-Ullrich, Joanne E.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20001117</creationdate><title>Thrombospondin Mediates Focal Adhesion Disassembly through Interactions with Cell Surface Calreticulin</title><author>Goicoechea, Silvia ; Orr, Anthony Wayne ; Pallero, Manuel Antonio ; Eggleton, Paul ; Murphy-Ullrich, Joanne E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c499t-20d9ae2a560a802604d99565642f9b85119d375fa7e2ff25df275a4c602bee6f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies - immunology</topic><topic>Antibodies - pharmacology</topic><topic>Biotinylation</topic><topic>Calcium-Binding Proteins - chemistry</topic><topic>Calcium-Binding Proteins - immunology</topic><topic>Calcium-Binding Proteins - isolation & purification</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Calreticulin</topic><topic>Cattle</topic><topic>CD36 Antigens - chemistry</topic><topic>CD36 Antigens - immunology</topic><topic>CD36 Antigens - isolation & purification</topic><topic>CD36 Antigens - metabolism</topic><topic>Cells, Cultured</topic><topic>Chromatography, Affinity</topic><topic>Cytoskeleton - drug effects</topic><topic>Cytoskeleton - metabolism</topic><topic>Endothelium, Vascular - chemistry</topic><topic>Endothelium, Vascular - cytology</topic><topic>Endothelium, Vascular - drug effects</topic><topic>Endothelium, Vascular - metabolism</topic><topic>Enzyme Activation - drug effects</topic><topic>Flow Cytometry</topic><topic>Fluorescent Antibody Technique</topic><topic>Focal Adhesions - chemistry</topic><topic>Focal Adhesions - drug effects</topic><topic>Focal Adhesions - metabolism</topic><topic>Humans</topic><topic>Macromolecular Substances</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - immunology</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Membrane Proteins - metabolism</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - immunology</topic><topic>Peptide Fragments - metabolism</topic><topic>Peptide Fragments - pharmacology</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>Ribonucleoproteins - chemistry</topic><topic>Ribonucleoproteins - immunology</topic><topic>Ribonucleoproteins - isolation & purification</topic><topic>Ribonucleoproteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Thrombospondins - antagonists & inhibitors</topic><topic>Thrombospondins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goicoechea, Silvia</creatorcontrib><creatorcontrib>Orr, Anthony Wayne</creatorcontrib><creatorcontrib>Pallero, Manuel Antonio</creatorcontrib><creatorcontrib>Eggleton, Paul</creatorcontrib><creatorcontrib>Murphy-Ullrich, Joanne E.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goicoechea, Silvia</au><au>Orr, Anthony Wayne</au><au>Pallero, Manuel Antonio</au><au>Eggleton, Paul</au><au>Murphy-Ullrich, Joanne E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thrombospondin Mediates Focal Adhesion Disassembly through Interactions with Cell Surface Calreticulin</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2000-11-17</date><risdate>2000</risdate><volume>275</volume><issue>46</issue><spage>36358</spage><epage>36368</epage><pages>36358-36368</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>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 glutathioneS-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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10964924</pmid><doi>10.1074/jbc.M005951200</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2000-11, Vol.275 (46), p.36358-36368 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Antibodies - immunology Antibodies - pharmacology Biotinylation Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - immunology Calcium-Binding Proteins - isolation & purification Calcium-Binding Proteins - metabolism Calreticulin Cattle CD36 Antigens - chemistry CD36 Antigens - immunology CD36 Antigens - isolation & purification CD36 Antigens - metabolism Cells, Cultured Chromatography, Affinity Cytoskeleton - drug effects Cytoskeleton - metabolism Endothelium, Vascular - chemistry Endothelium, Vascular - cytology Endothelium, Vascular - drug effects Endothelium, Vascular - metabolism Enzyme Activation - drug effects Flow Cytometry Fluorescent Antibody Technique Focal Adhesions - chemistry Focal Adhesions - drug effects Focal Adhesions - metabolism Humans Macromolecular Substances Membrane Proteins - chemistry Membrane Proteins - immunology Membrane Proteins - isolation & purification Membrane Proteins - metabolism Peptide Fragments - chemistry Peptide Fragments - immunology Peptide Fragments - metabolism Peptide Fragments - pharmacology Phosphatidylinositol 3-Kinases - metabolism Ribonucleoproteins - chemistry Ribonucleoproteins - immunology Ribonucleoproteins - isolation & purification Ribonucleoproteins - metabolism Sequence Homology, Amino Acid Thrombospondins - antagonists & inhibitors Thrombospondins - metabolism |
| title | Thrombospondin Mediates Focal Adhesion Disassembly through Interactions with Cell Surface Calreticulin |
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