Glycation of extracellular matrix proteins impairs migration of immune cells
The immune response during aging and diabetes is disturbed and may be due to the altered migration of immune cells in an aged tissue. Our study should prove the hypothesis that age and diabetes‐related advanced glycation end products (AGEs) have an impact on the migration and adhesion of human T‐cel...
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| Veröffentlicht in: | Wound repair and regeneration 2014-03, Vol.22 (2), p.239-245 |
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| creator | Haucke, Elisa Navarrete-Santos, Alexander Simm, Andreas Silber, Rolf-Edgar Hofmann, Britt |
| description | The immune response during aging and diabetes is disturbed and may be due to the altered migration of immune cells in an aged tissue. Our study should prove the hypothesis that age and diabetes‐related advanced glycation end products (AGEs) have an impact on the migration and adhesion of human T‐cells. To achieve our purpose, we used in vitro AGE‐modified proteins (soluble albumin and fibronectin [FN]), as well as human collagen obtained from bypass graft. A Boyden chamber was used to study cell migration. Migrated Jurkat T‐cells were analyzed by flow cytometry and cell adhesion by crystal violet staining. Actin polymerization was determined by phalloidin‐Alexa‐fluor 488‐labeled antibody and fluorescence microscopy. We found that significantly fewer cells (50%, p = 0.003) migrated through methylglyoxal modified FN. The attachment to FN in the presence of AGE‐bovine serum albumin (BSA) was also reduced (p |
| doi_str_mv | 10.1111/wrr.12144 |
| format | Article |
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Our study should prove the hypothesis that age and diabetes‐related advanced glycation end products (AGEs) have an impact on the migration and adhesion of human T‐cells. To achieve our purpose, we used in vitro AGE‐modified proteins (soluble albumin and fibronectin [FN]), as well as human collagen obtained from bypass graft. A Boyden chamber was used to study cell migration. Migrated Jurkat T‐cells were analyzed by flow cytometry and cell adhesion by crystal violet staining. Actin polymerization was determined by phalloidin‐Alexa‐fluor 488‐labeled antibody and fluorescence microscopy. We found that significantly fewer cells (50%, p = 0.003) migrated through methylglyoxal modified FN. The attachment to FN in the presence of AGE‐bovine serum albumin (BSA) was also reduced (p < 0.05). In ex vivo experiments, isolated collagen from human vein graft material negatively affected the migration of the cells depending on the grade of AGE modification of the collagen. Collagen with a low AGE level reduced the cell migration by 30%, and collagen with a high AGE level by 60%. Interaction of the cells with an AGE‐modified matrix, but not with soluble AGEs like BSA‐AGE per se, was responsible for a disturbed migration. The reduced migration was accompanied by an impaired actin polymerization. We conclude that AGEs‐modified matrix protein inhibits cell migration and adhesion of Jurkat T‐cells.</description><identifier>ISSN: 1067-1927</identifier><identifier>EISSN: 1524-475X</identifier><identifier>DOI: 10.1111/wrr.12144</identifier><identifier>PMID: 24635174</identifier><language>eng</language><publisher>United States: Blackwell Publishing Ltd</publisher><subject>Cell Adhesion ; Cell Movement ; Cells, Cultured ; Collagen - immunology ; Collagen - metabolism ; Extracellular Matrix Proteins - immunology ; Extracellular Matrix Proteins - metabolism ; Female ; Fibronectins - immunology ; Fibronectins - metabolism ; Flow Cytometry ; Glycation End Products, Advanced - immunology ; Glycation End Products, Advanced - metabolism ; Humans ; Male ; Receptor for Advanced Glycation End Products ; Receptors, Immunologic - immunology ; Receptors, Immunologic - metabolism ; Wound Healing</subject><ispartof>Wound repair and regeneration, 2014-03, Vol.22 (2), p.239-245</ispartof><rights>2014 by the Wound Healing Society</rights><rights>2014 by the Wound Healing Society.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2784-441a2b2a86292e65e56c25e0a18d3f97ecaac4d4767b3312a459251d9058023</citedby><cites>FETCH-LOGICAL-c2784-441a2b2a86292e65e56c25e0a18d3f97ecaac4d4767b3312a459251d9058023</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fwrr.12144$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fwrr.12144$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,782,786,1419,27931,27932,45581,45582</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24635174$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Haucke, Elisa</creatorcontrib><creatorcontrib>Navarrete-Santos, Alexander</creatorcontrib><creatorcontrib>Simm, Andreas</creatorcontrib><creatorcontrib>Silber, Rolf-Edgar</creatorcontrib><creatorcontrib>Hofmann, Britt</creatorcontrib><title>Glycation of extracellular matrix proteins impairs migration of immune cells</title><title>Wound repair and regeneration</title><addtitle>Wound Repair Regen</addtitle><description>The immune response during aging and diabetes is disturbed and may be due to the altered migration of immune cells in an aged tissue. Our study should prove the hypothesis that age and diabetes‐related advanced glycation end products (AGEs) have an impact on the migration and adhesion of human T‐cells. To achieve our purpose, we used in vitro AGE‐modified proteins (soluble albumin and fibronectin [FN]), as well as human collagen obtained from bypass graft. A Boyden chamber was used to study cell migration. Migrated Jurkat T‐cells were analyzed by flow cytometry and cell adhesion by crystal violet staining. Actin polymerization was determined by phalloidin‐Alexa‐fluor 488‐labeled antibody and fluorescence microscopy. We found that significantly fewer cells (50%, p = 0.003) migrated through methylglyoxal modified FN. The attachment to FN in the presence of AGE‐bovine serum albumin (BSA) was also reduced (p < 0.05). In ex vivo experiments, isolated collagen from human vein graft material negatively affected the migration of the cells depending on the grade of AGE modification of the collagen. Collagen with a low AGE level reduced the cell migration by 30%, and collagen with a high AGE level by 60%. Interaction of the cells with an AGE‐modified matrix, but not with soluble AGEs like BSA‐AGE per se, was responsible for a disturbed migration. The reduced migration was accompanied by an impaired actin polymerization. We conclude that AGEs‐modified matrix protein inhibits cell migration and adhesion of Jurkat T‐cells.</description><subject>Cell Adhesion</subject><subject>Cell Movement</subject><subject>Cells, Cultured</subject><subject>Collagen - immunology</subject><subject>Collagen - metabolism</subject><subject>Extracellular Matrix Proteins - immunology</subject><subject>Extracellular Matrix Proteins - metabolism</subject><subject>Female</subject><subject>Fibronectins - immunology</subject><subject>Fibronectins - metabolism</subject><subject>Flow Cytometry</subject><subject>Glycation End Products, Advanced - immunology</subject><subject>Glycation End Products, Advanced - metabolism</subject><subject>Humans</subject><subject>Male</subject><subject>Receptor for Advanced Glycation End Products</subject><subject>Receptors, Immunologic - immunology</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Wound Healing</subject><issn>1067-1927</issn><issn>1524-475X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMFPwjAUxhujEUQP_gNmRz0M2q5du6MhigbEBA14a8rWmeq6YbsF-O8tDrj5Lu8dft_3vnwAXCPYR34Ga2v7CCNCTkAXUUxCwujHqb9hzEKUYNYBF859QQgpTfg56GASRxQx0gWTUbFNZa2rMqjyQG1qK1NVFE0hbWBkbfUmWNmqVrp0gTYrqa0LjP60R4k2pilVsBO5S3CWy8Kpq_3ugbfHh_fhUzh5HT0P7ydhihn36QiSeIklj3GCVUwVjVNMFZSIZ1GeMJVKmZKMsJgtowhhSWiCKcoSSDnEUQ_ctq4-2E-jXC2Mdrv_slRV4wSikMccMsg9eteiqa2csyoXK6uNtFuBoNhVJ3x14q86z97sbZulUdmRPHTlgUELrHWhtv87icVsdrAMW4V2tdocFdJ-i5hFjIrFdCRQNB2OX-ZjMY9-AQz-h3c</recordid><startdate>201403</startdate><enddate>201403</enddate><creator>Haucke, Elisa</creator><creator>Navarrete-Santos, Alexander</creator><creator>Simm, Andreas</creator><creator>Silber, Rolf-Edgar</creator><creator>Hofmann, Britt</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>201403</creationdate><title>Glycation of extracellular matrix proteins impairs migration of immune cells</title><author>Haucke, Elisa ; Navarrete-Santos, Alexander ; Simm, Andreas ; Silber, Rolf-Edgar ; Hofmann, Britt</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2784-441a2b2a86292e65e56c25e0a18d3f97ecaac4d4767b3312a459251d9058023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Cell Adhesion</topic><topic>Cell Movement</topic><topic>Cells, Cultured</topic><topic>Collagen - immunology</topic><topic>Collagen - metabolism</topic><topic>Extracellular Matrix Proteins - immunology</topic><topic>Extracellular Matrix Proteins - metabolism</topic><topic>Female</topic><topic>Fibronectins - immunology</topic><topic>Fibronectins - metabolism</topic><topic>Flow Cytometry</topic><topic>Glycation End Products, Advanced - immunology</topic><topic>Glycation End Products, Advanced - metabolism</topic><topic>Humans</topic><topic>Male</topic><topic>Receptor for Advanced Glycation End Products</topic><topic>Receptors, Immunologic - immunology</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Wound Healing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Haucke, Elisa</creatorcontrib><creatorcontrib>Navarrete-Santos, Alexander</creatorcontrib><creatorcontrib>Simm, Andreas</creatorcontrib><creatorcontrib>Silber, Rolf-Edgar</creatorcontrib><creatorcontrib>Hofmann, Britt</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Wound repair and regeneration</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Haucke, Elisa</au><au>Navarrete-Santos, Alexander</au><au>Simm, Andreas</au><au>Silber, Rolf-Edgar</au><au>Hofmann, Britt</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glycation of extracellular matrix proteins impairs migration of immune cells</atitle><jtitle>Wound repair and regeneration</jtitle><addtitle>Wound Repair Regen</addtitle><date>2014-03</date><risdate>2014</risdate><volume>22</volume><issue>2</issue><spage>239</spage><epage>245</epage><pages>239-245</pages><issn>1067-1927</issn><eissn>1524-475X</eissn><abstract>The immune response during aging and diabetes is disturbed and may be due to the altered migration of immune cells in an aged tissue. Our study should prove the hypothesis that age and diabetes‐related advanced glycation end products (AGEs) have an impact on the migration and adhesion of human T‐cells. To achieve our purpose, we used in vitro AGE‐modified proteins (soluble albumin and fibronectin [FN]), as well as human collagen obtained from bypass graft. A Boyden chamber was used to study cell migration. Migrated Jurkat T‐cells were analyzed by flow cytometry and cell adhesion by crystal violet staining. Actin polymerization was determined by phalloidin‐Alexa‐fluor 488‐labeled antibody and fluorescence microscopy. We found that significantly fewer cells (50%, p = 0.003) migrated through methylglyoxal modified FN. The attachment to FN in the presence of AGE‐bovine serum albumin (BSA) was also reduced (p < 0.05). In ex vivo experiments, isolated collagen from human vein graft material negatively affected the migration of the cells depending on the grade of AGE modification of the collagen. Collagen with a low AGE level reduced the cell migration by 30%, and collagen with a high AGE level by 60%. Interaction of the cells with an AGE‐modified matrix, but not with soluble AGEs like BSA‐AGE per se, was responsible for a disturbed migration. The reduced migration was accompanied by an impaired actin polymerization. We conclude that AGEs‐modified matrix protein inhibits cell migration and adhesion of Jurkat T‐cells.</abstract><cop>United States</cop><pub>Blackwell Publishing Ltd</pub><pmid>24635174</pmid><doi>10.1111/wrr.12144</doi><tpages>7</tpages></addata></record> |
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| subjects | Cell Adhesion Cell Movement Cells, Cultured Collagen - immunology Collagen - metabolism Extracellular Matrix Proteins - immunology Extracellular Matrix Proteins - metabolism Female Fibronectins - immunology Fibronectins - metabolism Flow Cytometry Glycation End Products, Advanced - immunology Glycation End Products, Advanced - metabolism Humans Male Receptor for Advanced Glycation End Products Receptors, Immunologic - immunology Receptors, Immunologic - metabolism Wound Healing |
| title | Glycation of extracellular matrix proteins impairs migration of immune cells |
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