Real-time Analysis of Very Late Antigen-4 Affinity Modulation by Shear
Shear promotes endothelial recruitment of leukocytes, cell activation, and transmigration. Mechanical stress on cells caused by shear can induce a rapid integrin conformational change and activation, followed by an increase in binding to the extracellular matrix. The molecular mechanism of increased...
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| Veröffentlicht in: | The Journal of biological chemistry 2004-09, Vol.279 (37), p.38277-38286 |
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| container_title | The Journal of biological chemistry |
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| creator | Zwartz, Gordon J. Chigaev, Alexandre Dwyer, Denise C. Foutz, Terry D. Edwards, Bruce S. Sklar, Larry A. |
| description | Shear promotes endothelial recruitment of leukocytes, cell activation, and transmigration. Mechanical stress on cells caused by shear can induce a rapid integrin conformational change and activation, followed by an increase in binding to the extracellular matrix. The molecular mechanism of increased avidity is unknown. We have shown previously that the affinity of the α4β1 integrin, very late antigen-4 (VLA-4), measured with an LDV-containing small molecule, varies with cellular avidity, measured from cell disaggregation rates. In this study, we measured in real time affinity changes of VLA-4 in response to shear. The resulting affinity was comparable with the state mediated by receptor signaling and corresponded in time with intracellular Ca2+ responses. Ca2+ ionophores and N,N′-[1,2-ethanediyl-bis(oxy-2,1-phenylene)]bis[N-[2-[(acetyloxy)methoxy]-2-oxoethyl]]-, bis[(acetyloxy)methyl]ester demonstrate that the affinity regulation of VLA-4 in the presence of shear was related to Ca2+ signaling. Pertussis toxin treatment implicates Gi in an unknown pathway that connects shear, Ca2+ elevation, VLA-4 affinity, and cell avidity. |
| doi_str_mv | 10.1074/jbc.M402944200 |
| format | Article |
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Mechanical stress on cells caused by shear can induce a rapid integrin conformational change and activation, followed by an increase in binding to the extracellular matrix. The molecular mechanism of increased avidity is unknown. We have shown previously that the affinity of the α4β1 integrin, very late antigen-4 (VLA-4), measured with an LDV-containing small molecule, varies with cellular avidity, measured from cell disaggregation rates. In this study, we measured in real time affinity changes of VLA-4 in response to shear. The resulting affinity was comparable with the state mediated by receptor signaling and corresponded in time with intracellular Ca2+ responses. Ca2+ ionophores and N,N′-[1,2-ethanediyl-bis(oxy-2,1-phenylene)]bis[N-[2-[(acetyloxy)methoxy]-2-oxoethyl]]-, bis[(acetyloxy)methyl]ester demonstrate that the affinity regulation of VLA-4 in the presence of shear was related to Ca2+ signaling. Pertussis toxin treatment implicates Gi in an unknown pathway that connects shear, Ca2+ elevation, VLA-4 affinity, and cell avidity.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M402944200</identifier><identifier>PMID: 15226304</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Calcium - chemistry ; Calcium - metabolism ; Calibration ; Cell Movement ; Dose-Response Relationship, Drug ; Egtazic Acid - analogs & derivatives ; Egtazic Acid - pharmacology ; Flow Cytometry ; GTP-Binding Protein alpha Subunits, Gi-Go - metabolism ; Humans ; Integrin alpha4beta1 - chemistry ; Ionophores - chemistry ; Ionophores - pharmacology ; Kinetics ; Ligands ; Models, Biological ; Pertussis Toxin - pharmacology ; Protein Binding ; Protein Conformation ; Signal Transduction ; Stress, Mechanical ; Temperature ; Time Factors ; Transfection ; U937 Cells</subject><ispartof>The Journal of biological chemistry, 2004-09, Vol.279 (37), p.38277-38286</ispartof><rights>2004 © 2004 ASBMB. 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Mechanical stress on cells caused by shear can induce a rapid integrin conformational change and activation, followed by an increase in binding to the extracellular matrix. The molecular mechanism of increased avidity is unknown. We have shown previously that the affinity of the α4β1 integrin, very late antigen-4 (VLA-4), measured with an LDV-containing small molecule, varies with cellular avidity, measured from cell disaggregation rates. In this study, we measured in real time affinity changes of VLA-4 in response to shear. The resulting affinity was comparable with the state mediated by receptor signaling and corresponded in time with intracellular Ca2+ responses. Ca2+ ionophores and N,N′-[1,2-ethanediyl-bis(oxy-2,1-phenylene)]bis[N-[2-[(acetyloxy)methoxy]-2-oxoethyl]]-, bis[(acetyloxy)methyl]ester demonstrate that the affinity regulation of VLA-4 in the presence of shear was related to Ca2+ signaling. Pertussis toxin treatment implicates Gi in an unknown pathway that connects shear, Ca2+ elevation, VLA-4 affinity, and cell avidity.</description><subject>Calcium - chemistry</subject><subject>Calcium - metabolism</subject><subject>Calibration</subject><subject>Cell Movement</subject><subject>Dose-Response Relationship, Drug</subject><subject>Egtazic Acid - analogs & derivatives</subject><subject>Egtazic Acid - pharmacology</subject><subject>Flow Cytometry</subject><subject>GTP-Binding Protein alpha Subunits, Gi-Go - metabolism</subject><subject>Humans</subject><subject>Integrin alpha4beta1 - chemistry</subject><subject>Ionophores - chemistry</subject><subject>Ionophores - pharmacology</subject><subject>Kinetics</subject><subject>Ligands</subject><subject>Models, Biological</subject><subject>Pertussis Toxin - pharmacology</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Signal Transduction</subject><subject>Stress, Mechanical</subject><subject>Temperature</subject><subject>Time Factors</subject><subject>Transfection</subject><subject>U937 Cells</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMtLxDAQh4Mo7vq4epQexFvXyaNNelzEF6wIvvAW0nSyG-lDk67S_97KLnhyLgPD9_sxfIScUJhRkOLivbSzewGsEIIB7JApBcVTntG3XTIFYDQtWKYm5CDGdxhHFHSfTGjGWM5BTMn1I5o67X2Dybw19RB9TDqXvGIYkoXpf6-9X2KbimTunG99PyT3XbWuTe-7NimH5GmFJhyRPWfqiMfbfUherq-eL2_TxcPN3eV8kVohoE-VcxSxrDKLPAOHFSDPC8OhsJZLl9uiREYrZw1TzIE0LoPclLLgNKfCCn5Izje9H6H7XGPsdeOjxbo2LXbrqKkCqjKpRnC2AW3oYgzo9EfwjQmDpqB_zenRnP4zNwZOt83rssHqD9-qGoGzDbDyy9W3D6hL39kVNprJQnOpuWJSjpjaYDhq-PIYdLQeW4vVGLG9rjr_3ws_k3-HeA</recordid><startdate>20040910</startdate><enddate>20040910</enddate><creator>Zwartz, Gordon J.</creator><creator>Chigaev, Alexandre</creator><creator>Dwyer, Denise C.</creator><creator>Foutz, Terry D.</creator><creator>Edwards, Bruce S.</creator><creator>Sklar, Larry A.</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><scope>7T5</scope><scope>H94</scope></search><sort><creationdate>20040910</creationdate><title>Real-time Analysis of Very Late Antigen-4 Affinity Modulation by Shear</title><author>Zwartz, Gordon J. ; Chigaev, Alexandre ; Dwyer, Denise C. ; Foutz, Terry D. ; Edwards, Bruce S. ; Sklar, Larry A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-8ff1eebd5ce350fed0e369a309cc37f6c9be21dfca282f07af506ab7931614c43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Calcium - chemistry</topic><topic>Calcium - metabolism</topic><topic>Calibration</topic><topic>Cell Movement</topic><topic>Dose-Response Relationship, Drug</topic><topic>Egtazic Acid - analogs & derivatives</topic><topic>Egtazic Acid - pharmacology</topic><topic>Flow Cytometry</topic><topic>GTP-Binding Protein alpha Subunits, Gi-Go - metabolism</topic><topic>Humans</topic><topic>Integrin alpha4beta1 - chemistry</topic><topic>Ionophores - chemistry</topic><topic>Ionophores - pharmacology</topic><topic>Kinetics</topic><topic>Ligands</topic><topic>Models, Biological</topic><topic>Pertussis Toxin - pharmacology</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Signal Transduction</topic><topic>Stress, Mechanical</topic><topic>Temperature</topic><topic>Time Factors</topic><topic>Transfection</topic><topic>U937 Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zwartz, Gordon J.</creatorcontrib><creatorcontrib>Chigaev, Alexandre</creatorcontrib><creatorcontrib>Dwyer, Denise C.</creatorcontrib><creatorcontrib>Foutz, Terry D.</creatorcontrib><creatorcontrib>Edwards, Bruce S.</creatorcontrib><creatorcontrib>Sklar, Larry A.</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><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zwartz, Gordon J.</au><au>Chigaev, Alexandre</au><au>Dwyer, Denise C.</au><au>Foutz, Terry D.</au><au>Edwards, Bruce S.</au><au>Sklar, Larry A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Real-time Analysis of Very Late Antigen-4 Affinity Modulation by Shear</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-09-10</date><risdate>2004</risdate><volume>279</volume><issue>37</issue><spage>38277</spage><epage>38286</epage><pages>38277-38286</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Shear promotes endothelial recruitment of leukocytes, cell activation, and transmigration. Mechanical stress on cells caused by shear can induce a rapid integrin conformational change and activation, followed by an increase in binding to the extracellular matrix. The molecular mechanism of increased avidity is unknown. We have shown previously that the affinity of the α4β1 integrin, very late antigen-4 (VLA-4), measured with an LDV-containing small molecule, varies with cellular avidity, measured from cell disaggregation rates. In this study, we measured in real time affinity changes of VLA-4 in response to shear. The resulting affinity was comparable with the state mediated by receptor signaling and corresponded in time with intracellular Ca2+ responses. Ca2+ ionophores and N,N′-[1,2-ethanediyl-bis(oxy-2,1-phenylene)]bis[N-[2-[(acetyloxy)methoxy]-2-oxoethyl]]-, bis[(acetyloxy)methyl]ester demonstrate that the affinity regulation of VLA-4 in the presence of shear was related to Ca2+ signaling. 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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Calcium - chemistry Calcium - metabolism Calibration Cell Movement Dose-Response Relationship, Drug Egtazic Acid - analogs & derivatives Egtazic Acid - pharmacology Flow Cytometry GTP-Binding Protein alpha Subunits, Gi-Go - metabolism Humans Integrin alpha4beta1 - chemistry Ionophores - chemistry Ionophores - pharmacology Kinetics Ligands Models, Biological Pertussis Toxin - pharmacology Protein Binding Protein Conformation Signal Transduction Stress, Mechanical Temperature Time Factors Transfection U937 Cells |
| title | Real-time Analysis of Very Late Antigen-4 Affinity Modulation by Shear |
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