Cross-Linking of Cell Surface Receptors Enhances Cooperativity of Molecular Adhesion

Cooperativity of molecular adhesion has been proposed as a mechanism for enhanced binding strength of adhesion molecules on the cell surface. Direct evidence for its mechanism, however, has been lacking until now. Atomic force microscopy (AFM) was used to measure the adhesive strength between concan...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biophysical journal 2000-06, Vol.78 (6), p.2814-2820
Hauptverfasser: Chen, Aileen, Moy, Vincent T.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 2820
container_issue 6
container_start_page 2814
container_title Biophysical journal
container_volume 78
creator Chen, Aileen
Moy, Vincent T.
description Cooperativity of molecular adhesion has been proposed as a mechanism for enhanced binding strength of adhesion molecules on the cell surface. Direct evidence for its mechanism, however, has been lacking until now. Atomic force microscopy (AFM) was used to measure the adhesive strength between concanavalin A (Con A) coupled to an AFM tip and Con A receptors on the surface of NIH3T3 fibroblast cells. Cross-linking of receptors with either glutaraldehyde or 3,3′-dithio-bis(sulfosuccinimidylproprionate) (DTSSP) led to an increase in adhesion that could be attributed to enhanced cooperativity among adhesion complexes. An increase in loading rate due to greater stiffness of fixed cells also contributed to the twofold increase in binding strength. These results show that receptor cross-linking can greatly contribute to a total increase in cell adhesion by creating a shift toward cooperative binding of receptors.
doi_str_mv 10.1016/S0006-3495(00)76824-X
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1300869</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S000634950076824X</els_id><sourcerecordid>71140183</sourcerecordid><originalsourceid>FETCH-LOGICAL-c556t-37a4a1a874713ee3ca7d2a9b0e69e69a3e0d14b990982f038a98e09d261390143</originalsourceid><addsrcrecordid>eNqFkV9rFDEUxYModq1-BGXwQfRh6s2_mclLpQy1FVYEW6FvIZu5002dTdZkZqHf3ky3lOpLIZCH_M7JvecQ8pbCEQVafb4AgKrkQsmPAJ_qqmGivHpGFlQKVgI01XOyeEAOyKuUbgAok0BfkgMKDatVJRbkso0hpXLp_G_nr4vQFy0OQ3Exxd5YLH6ixe0YYipO_dp4i6loQ9hiNKPbufF2FnwPA9ppMLE46daYXPCvyYveDAnf3N-H5NfX08v2vFz-OPvWnixLK2U1lrw2wlDT1KKmHJFbU3fMqBVgpfIxHKGjYqUUqIb1wBujGgTVsYpyBVTwQ3K8991Oqw12Fv0YzaC30W1MvNXBOP3vi3drfR12mvI5IZUNPtwbxPBnwjTqjUs2B2A8hinpmlIBtOEZfP8feBOm6PNymlFZM8klZEjuITtnGrF_mISCnkvTd6XpuRENoO9K01dZ9-7xGo9U-5Yy8GUPYA5z5zDqZB3mNjoX0Y66C-6JL_4CErmm-w</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>215725350</pqid></control><display><type>article</type><title>Cross-Linking of Cell Surface Receptors Enhances Cooperativity of Molecular Adhesion</title><source>MEDLINE</source><source>Cell Press Free Archives</source><source>ScienceDirect Journals (5 years ago - present)</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Chen, Aileen ; Moy, Vincent T.</creator><creatorcontrib>Chen, Aileen ; Moy, Vincent T.</creatorcontrib><description>Cooperativity of molecular adhesion has been proposed as a mechanism for enhanced binding strength of adhesion molecules on the cell surface. Direct evidence for its mechanism, however, has been lacking until now. Atomic force microscopy (AFM) was used to measure the adhesive strength between concanavalin A (Con A) coupled to an AFM tip and Con A receptors on the surface of NIH3T3 fibroblast cells. Cross-linking of receptors with either glutaraldehyde or 3,3′-dithio-bis(sulfosuccinimidylproprionate) (DTSSP) led to an increase in adhesion that could be attributed to enhanced cooperativity among adhesion complexes. An increase in loading rate due to greater stiffness of fixed cells also contributed to the twofold increase in binding strength. These results show that receptor cross-linking can greatly contribute to a total increase in cell adhesion by creating a shift toward cooperative binding of receptors.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(00)76824-X</identifier><identifier>PMID: 10827964</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>3T3 Cells ; Animals ; Cell Adhesion - drug effects ; Cell Adhesion - physiology ; Cellular biology ; Concanavalin A - metabolism ; Cross-Linking Reagents ; Glutaral - pharmacology ; Mice ; Microscopy, Atomic Force ; Models, Biological ; Receptors, Cell Surface - physiology ; Receptors, Concanavalin A - drug effects ; Receptors, Concanavalin A - physiology ; Succinimides - pharmacology</subject><ispartof>Biophysical journal, 2000-06, Vol.78 (6), p.2814-2820</ispartof><rights>2000 The Biophysical Society</rights><rights>Copyright Biophysical Society Jun 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c556t-37a4a1a874713ee3ca7d2a9b0e69e69a3e0d14b990982f038a98e09d261390143</citedby><cites>FETCH-LOGICAL-c556t-37a4a1a874713ee3ca7d2a9b0e69e69a3e0d14b990982f038a98e09d261390143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1300869/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-3495(00)76824-X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3548,27923,27924,45994,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10827964$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chen, Aileen</creatorcontrib><creatorcontrib>Moy, Vincent T.</creatorcontrib><title>Cross-Linking of Cell Surface Receptors Enhances Cooperativity of Molecular Adhesion</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>Cooperativity of molecular adhesion has been proposed as a mechanism for enhanced binding strength of adhesion molecules on the cell surface. Direct evidence for its mechanism, however, has been lacking until now. Atomic force microscopy (AFM) was used to measure the adhesive strength between concanavalin A (Con A) coupled to an AFM tip and Con A receptors on the surface of NIH3T3 fibroblast cells. Cross-linking of receptors with either glutaraldehyde or 3,3′-dithio-bis(sulfosuccinimidylproprionate) (DTSSP) led to an increase in adhesion that could be attributed to enhanced cooperativity among adhesion complexes. An increase in loading rate due to greater stiffness of fixed cells also contributed to the twofold increase in binding strength. These results show that receptor cross-linking can greatly contribute to a total increase in cell adhesion by creating a shift toward cooperative binding of receptors.</description><subject>3T3 Cells</subject><subject>Animals</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell Adhesion - physiology</subject><subject>Cellular biology</subject><subject>Concanavalin A - metabolism</subject><subject>Cross-Linking Reagents</subject><subject>Glutaral - pharmacology</subject><subject>Mice</subject><subject>Microscopy, Atomic Force</subject><subject>Models, Biological</subject><subject>Receptors, Cell Surface - physiology</subject><subject>Receptors, Concanavalin A - drug effects</subject><subject>Receptors, Concanavalin A - physiology</subject><subject>Succinimides - pharmacology</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkV9rFDEUxYModq1-BGXwQfRh6s2_mclLpQy1FVYEW6FvIZu5002dTdZkZqHf3ky3lOpLIZCH_M7JvecQ8pbCEQVafb4AgKrkQsmPAJ_qqmGivHpGFlQKVgI01XOyeEAOyKuUbgAok0BfkgMKDatVJRbkso0hpXLp_G_nr4vQFy0OQ3Exxd5YLH6ixe0YYipO_dp4i6loQ9hiNKPbufF2FnwPA9ppMLE46daYXPCvyYveDAnf3N-H5NfX08v2vFz-OPvWnixLK2U1lrw2wlDT1KKmHJFbU3fMqBVgpfIxHKGjYqUUqIb1wBujGgTVsYpyBVTwQ3K8991Oqw12Fv0YzaC30W1MvNXBOP3vi3drfR12mvI5IZUNPtwbxPBnwjTqjUs2B2A8hinpmlIBtOEZfP8feBOm6PNymlFZM8klZEjuITtnGrF_mISCnkvTd6XpuRENoO9K01dZ9-7xGo9U-5Yy8GUPYA5z5zDqZB3mNjoX0Y66C-6JL_4CErmm-w</recordid><startdate>20000601</startdate><enddate>20000601</enddate><creator>Chen, Aileen</creator><creator>Moy, Vincent T.</creator><general>Elsevier Inc</general><general>Biophysical Society</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>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>S0X</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000601</creationdate><title>Cross-Linking of Cell Surface Receptors Enhances Cooperativity of Molecular Adhesion</title><author>Chen, Aileen ; Moy, Vincent T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c556t-37a4a1a874713ee3ca7d2a9b0e69e69a3e0d14b990982f038a98e09d261390143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>3T3 Cells</topic><topic>Animals</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell Adhesion - physiology</topic><topic>Cellular biology</topic><topic>Concanavalin A - metabolism</topic><topic>Cross-Linking Reagents</topic><topic>Glutaral - pharmacology</topic><topic>Mice</topic><topic>Microscopy, Atomic Force</topic><topic>Models, Biological</topic><topic>Receptors, Cell Surface - physiology</topic><topic>Receptors, Concanavalin A - drug effects</topic><topic>Receptors, Concanavalin A - physiology</topic><topic>Succinimides - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Aileen</creatorcontrib><creatorcontrib>Moy, Vincent T.</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>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies &amp; Aerospace Collection</collection><collection>Agricultural &amp; Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies &amp; Aerospace Database</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Aileen</au><au>Moy, Vincent T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cross-Linking of Cell Surface Receptors Enhances Cooperativity of Molecular Adhesion</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2000-06-01</date><risdate>2000</risdate><volume>78</volume><issue>6</issue><spage>2814</spage><epage>2820</epage><pages>2814-2820</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>Cooperativity of molecular adhesion has been proposed as a mechanism for enhanced binding strength of adhesion molecules on the cell surface. Direct evidence for its mechanism, however, has been lacking until now. Atomic force microscopy (AFM) was used to measure the adhesive strength between concanavalin A (Con A) coupled to an AFM tip and Con A receptors on the surface of NIH3T3 fibroblast cells. Cross-linking of receptors with either glutaraldehyde or 3,3′-dithio-bis(sulfosuccinimidylproprionate) (DTSSP) led to an increase in adhesion that could be attributed to enhanced cooperativity among adhesion complexes. An increase in loading rate due to greater stiffness of fixed cells also contributed to the twofold increase in binding strength. These results show that receptor cross-linking can greatly contribute to a total increase in cell adhesion by creating a shift toward cooperative binding of receptors.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10827964</pmid><doi>10.1016/S0006-3495(00)76824-X</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0006-3495
ispartof Biophysical journal, 2000-06, Vol.78 (6), p.2814-2820
issn 0006-3495
1542-0086
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1300869
source MEDLINE; Cell Press Free Archives; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; PubMed Central
subjects 3T3 Cells
Animals
Cell Adhesion - drug effects
Cell Adhesion - physiology
Cellular biology
Concanavalin A - metabolism
Cross-Linking Reagents
Glutaral - pharmacology
Mice
Microscopy, Atomic Force
Models, Biological
Receptors, Cell Surface - physiology
Receptors, Concanavalin A - drug effects
Receptors, Concanavalin A - physiology
Succinimides - pharmacology
title Cross-Linking of Cell Surface Receptors Enhances Cooperativity of Molecular Adhesion
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-13T06%3A15%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cross-Linking%20of%20Cell%20Surface%20Receptors%20Enhances%20Cooperativity%20of%20Molecular%20Adhesion&rft.jtitle=Biophysical%20journal&rft.au=Chen,%20Aileen&rft.date=2000-06-01&rft.volume=78&rft.issue=6&rft.spage=2814&rft.epage=2820&rft.pages=2814-2820&rft.issn=0006-3495&rft.eissn=1542-0086&rft_id=info:doi/10.1016/S0006-3495(00)76824-X&rft_dat=%3Cproquest_pubme%3E71140183%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=215725350&rft_id=info:pmid/10827964&rft_els_id=S000634950076824X&rfr_iscdi=true