Two Proteins Modulating Transendothelial Migration of Leukocytes Recognize Novel Carboxylated Glycans on Endothelial Cells
We recently showed that a class of novel carboxylated N:-glycans was constitutively expressed on endothelial cells. Activated, but not resting, neutrophils expressed binding sites for the novel glycans. We also showed that a mAb against these novel glycans (mAbGB3.1) inhibited leukocyte extravasatio...
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| Veröffentlicht in: | The Journal of immunology (1950) 2001-04, Vol.166 (7), p.4678-4688 |
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| container_title | The Journal of immunology (1950) |
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| creator | Srikrishna, Geetha Panneerselvam, Krishnasamy Westphal, Vibeke Abraham, Violet Varki, Ajit Freeze, Hudson H |
| description | We recently showed that a class of novel carboxylated N:-glycans was constitutively expressed on endothelial cells. Activated, but not resting, neutrophils expressed binding sites for the novel glycans. We also showed that a mAb against these novel glycans (mAbGB3.1) inhibited leukocyte extravasation in a murine model of peritoneal inflammation. To identify molecules that mediated these interactions, we isolated binding proteins from bovine lung by their differential affinity for carboxylated or neutralized glycans. Two leukocyte calcium-binding proteins that bound in a carboxylate-dependent manner were identified as S100A8 and annexin I. An intact N terminus of annexin I and heteromeric assembly of S100A8 with S100A9 (another member of the S100 family) appeared necessary for this interaction. A mAb to S100A9 blocked neutrophil binding to immobilized carboxylated glycans. Purified human S100A8/A9 complex and recombinant human annexin I showed carboxylate-dependent binding to immobilized bovine lung carboxylated glycans and recognized a subset of mannose-labeled endothelial glycoproteins immunoprecipitated by mAbGB3.1. Saturable binding of S100A8/A9 complex to endothelial cells was also blocked by mAbGB3.1. These results suggest that the carboxylated glycans play important roles in leukocyte trafficking by interacting with proteins known to modulate extravasation. |
| doi_str_mv | 10.4049/jimmunol.166.7.4678 |
| format | Article |
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Activated, but not resting, neutrophils expressed binding sites for the novel glycans. We also showed that a mAb against these novel glycans (mAbGB3.1) inhibited leukocyte extravasation in a murine model of peritoneal inflammation. To identify molecules that mediated these interactions, we isolated binding proteins from bovine lung by their differential affinity for carboxylated or neutralized glycans. Two leukocyte calcium-binding proteins that bound in a carboxylate-dependent manner were identified as S100A8 and annexin I. An intact N terminus of annexin I and heteromeric assembly of S100A8 with S100A9 (another member of the S100 family) appeared necessary for this interaction. A mAb to S100A9 blocked neutrophil binding to immobilized carboxylated glycans. Purified human S100A8/A9 complex and recombinant human annexin I showed carboxylate-dependent binding to immobilized bovine lung carboxylated glycans and recognized a subset of mannose-labeled endothelial glycoproteins immunoprecipitated by mAbGB3.1. Saturable binding of S100A8/A9 complex to endothelial cells was also blocked by mAbGB3.1. These results suggest that the carboxylated glycans play important roles in leukocyte trafficking by interacting with proteins known to modulate extravasation.</description><identifier>ISSN: 0022-1767</identifier><identifier>EISSN: 1550-6606</identifier><identifier>DOI: 10.4049/jimmunol.166.7.4678</identifier><identifier>PMID: 11254728</identifier><language>eng</language><publisher>United States: Am Assoc Immnol</publisher><subject>Amino Acid Sequence ; Animals ; Annexin A1 - chemistry ; Annexin A1 - immunology ; Annexin A1 - metabolism ; annexin I ; Antibodies, Monoclonal - metabolism ; Antibodies, Monoclonal - pharmacology ; Antigens, Differentiation - immunology ; Antigens, Differentiation - isolation & purification ; Antigens, Differentiation - metabolism ; Antigens, Differentiation - physiology ; Binding Sites, Antibody ; Binding, Competitive - immunology ; Calcium-Binding Proteins - immunology ; Calcium-Binding Proteins - isolation & purification ; Calcium-Binding Proteins - metabolism ; Calcium-Binding Proteins - physiology ; Calgranulin A ; Calgranulin B ; Carboxylic Acids - metabolism ; Carrier Proteins - isolation & purification ; Carrier Proteins - metabolism ; Carrier Proteins - physiology ; Cattle ; Cell Adhesion - immunology ; Cell Membrane - immunology ; Cell Membrane - metabolism ; Cell Movement - immunology ; Chromatography, Affinity - methods ; Endothelium, Vascular - cytology ; Endothelium, Vascular - immunology ; Endothelium, Vascular - metabolism ; glycans ; Glycopeptides - chemical synthesis ; Glycopeptides - metabolism ; Humans ; Immune Sera - metabolism ; Immune Sera - pharmacology ; Leukocytes - immunology ; Leukocytes - metabolism ; Lung - cytology ; Lung - immunology ; Lung - metabolism ; Mice ; Molecular Sequence Data ; Molecular Weight ; Neutrophils - immunology ; Neutrophils - metabolism ; Polysaccharides - metabolism ; Rabbits ; S100 Proteins - immunology ; S100 Proteins - isolation & purification ; S100 Proteins - metabolism ; S100 Proteins - physiology ; Sequence Homology, Amino Acid</subject><ispartof>The Journal of immunology (1950), 2001-04, Vol.166 (7), p.4678-4688</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c475t-50065a30335fd61f85e7637d4aa0931ccf2f1cc496d2837b3380195c6686da033</citedby><cites>FETCH-LOGICAL-c475t-50065a30335fd61f85e7637d4aa0931ccf2f1cc496d2837b3380195c6686da033</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11254728$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Srikrishna, Geetha</creatorcontrib><creatorcontrib>Panneerselvam, Krishnasamy</creatorcontrib><creatorcontrib>Westphal, Vibeke</creatorcontrib><creatorcontrib>Abraham, Violet</creatorcontrib><creatorcontrib>Varki, Ajit</creatorcontrib><creatorcontrib>Freeze, Hudson H</creatorcontrib><title>Two Proteins Modulating Transendothelial Migration of Leukocytes Recognize Novel Carboxylated Glycans on Endothelial Cells</title><title>The Journal of immunology (1950)</title><addtitle>J Immunol</addtitle><description>We recently showed that a class of novel carboxylated N:-glycans was constitutively expressed on endothelial cells. Activated, but not resting, neutrophils expressed binding sites for the novel glycans. We also showed that a mAb against these novel glycans (mAbGB3.1) inhibited leukocyte extravasation in a murine model of peritoneal inflammation. To identify molecules that mediated these interactions, we isolated binding proteins from bovine lung by their differential affinity for carboxylated or neutralized glycans. Two leukocyte calcium-binding proteins that bound in a carboxylate-dependent manner were identified as S100A8 and annexin I. An intact N terminus of annexin I and heteromeric assembly of S100A8 with S100A9 (another member of the S100 family) appeared necessary for this interaction. A mAb to S100A9 blocked neutrophil binding to immobilized carboxylated glycans. Purified human S100A8/A9 complex and recombinant human annexin I showed carboxylate-dependent binding to immobilized bovine lung carboxylated glycans and recognized a subset of mannose-labeled endothelial glycoproteins immunoprecipitated by mAbGB3.1. Saturable binding of S100A8/A9 complex to endothelial cells was also blocked by mAbGB3.1. These results suggest that the carboxylated glycans play important roles in leukocyte trafficking by interacting with proteins known to modulate extravasation.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Annexin A1 - chemistry</subject><subject>Annexin A1 - immunology</subject><subject>Annexin A1 - metabolism</subject><subject>annexin I</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Antibodies, Monoclonal - pharmacology</subject><subject>Antigens, Differentiation - immunology</subject><subject>Antigens, Differentiation - isolation & purification</subject><subject>Antigens, Differentiation - metabolism</subject><subject>Antigens, Differentiation - physiology</subject><subject>Binding Sites, Antibody</subject><subject>Binding, Competitive - immunology</subject><subject>Calcium-Binding Proteins - immunology</subject><subject>Calcium-Binding Proteins - isolation & purification</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Calcium-Binding Proteins - physiology</subject><subject>Calgranulin A</subject><subject>Calgranulin B</subject><subject>Carboxylic Acids - metabolism</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - metabolism</subject><subject>Carrier Proteins - physiology</subject><subject>Cattle</subject><subject>Cell Adhesion - immunology</subject><subject>Cell Membrane - immunology</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Movement - immunology</subject><subject>Chromatography, Affinity - methods</subject><subject>Endothelium, Vascular - cytology</subject><subject>Endothelium, Vascular - immunology</subject><subject>Endothelium, Vascular - metabolism</subject><subject>glycans</subject><subject>Glycopeptides - chemical synthesis</subject><subject>Glycopeptides - metabolism</subject><subject>Humans</subject><subject>Immune Sera - metabolism</subject><subject>Immune Sera - pharmacology</subject><subject>Leukocytes - immunology</subject><subject>Leukocytes - metabolism</subject><subject>Lung - cytology</subject><subject>Lung - immunology</subject><subject>Lung - metabolism</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Neutrophils - immunology</subject><subject>Neutrophils - metabolism</subject><subject>Polysaccharides - metabolism</subject><subject>Rabbits</subject><subject>S100 Proteins - immunology</subject><subject>S100 Proteins - isolation & purification</subject><subject>S100 Proteins - metabolism</subject><subject>S100 Proteins - physiology</subject><subject>Sequence Homology, Amino Acid</subject><issn>0022-1767</issn><issn>1550-6606</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vEzEQhi0EomnhFyAhn-C0wV5_7hFFpSClgFA4W453NnHxrou92yX99XWVIHrjMnOY53000ovQG0qWnPDmw43v-2mIYUmlXKoll0o_QwsqBKmkJPI5WhBS1xVVUp2h85xvCCGS1PwlOqO0FlzVeoHuN3PE31McwQ8ZX8d2Cnb0ww5vkh0yDG0c9xC8Dfja71I5xQHHDq9h-hXdYYSMf4CLu8HfA_4a7yDglU3b-OdQNNDiq3BwxYNL6vKJawUh5FfoRWdDhtenfYF-frrcrD5X629XX1Yf15XjSoyVKF8Lywhjomsl7bQAJZlqubWkYdS5ru7K5I1sa83UljFNaCOclFq2tsQu0Luj9zbF3xPk0fQ-u_KBHSBO2SjZaMbZ_0GqNFWC6gKyI-hSzDlBZ26T7206GErMYzfmbzemdGOUeeympN6e9NO2h_Zf5lRGAd4fgb3f7WefwOTehlBwauZ5fqJ6ADfTm_s</recordid><startdate>20010401</startdate><enddate>20010401</enddate><creator>Srikrishna, Geetha</creator><creator>Panneerselvam, Krishnasamy</creator><creator>Westphal, Vibeke</creator><creator>Abraham, Violet</creator><creator>Varki, Ajit</creator><creator>Freeze, Hudson H</creator><general>Am Assoc Immnol</general><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><scope>7X8</scope></search><sort><creationdate>20010401</creationdate><title>Two Proteins Modulating Transendothelial Migration of Leukocytes Recognize Novel Carboxylated Glycans on Endothelial Cells</title><author>Srikrishna, Geetha ; Panneerselvam, Krishnasamy ; Westphal, Vibeke ; Abraham, Violet ; Varki, Ajit ; Freeze, Hudson H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c475t-50065a30335fd61f85e7637d4aa0931ccf2f1cc496d2837b3380195c6686da033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Annexin A1 - chemistry</topic><topic>Annexin A1 - immunology</topic><topic>Annexin A1 - metabolism</topic><topic>annexin I</topic><topic>Antibodies, Monoclonal - metabolism</topic><topic>Antibodies, Monoclonal - pharmacology</topic><topic>Antigens, Differentiation - immunology</topic><topic>Antigens, Differentiation - isolation & purification</topic><topic>Antigens, Differentiation - metabolism</topic><topic>Antigens, Differentiation - physiology</topic><topic>Binding Sites, Antibody</topic><topic>Binding, Competitive - immunology</topic><topic>Calcium-Binding Proteins - immunology</topic><topic>Calcium-Binding Proteins - isolation & purification</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Calcium-Binding Proteins - physiology</topic><topic>Calgranulin A</topic><topic>Calgranulin B</topic><topic>Carboxylic Acids - metabolism</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - metabolism</topic><topic>Carrier Proteins - physiology</topic><topic>Cattle</topic><topic>Cell Adhesion - immunology</topic><topic>Cell Membrane - immunology</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Movement - immunology</topic><topic>Chromatography, Affinity - methods</topic><topic>Endothelium, Vascular - cytology</topic><topic>Endothelium, Vascular - immunology</topic><topic>Endothelium, Vascular - metabolism</topic><topic>glycans</topic><topic>Glycopeptides - chemical synthesis</topic><topic>Glycopeptides - metabolism</topic><topic>Humans</topic><topic>Immune Sera - metabolism</topic><topic>Immune Sera - pharmacology</topic><topic>Leukocytes - immunology</topic><topic>Leukocytes - metabolism</topic><topic>Lung - cytology</topic><topic>Lung - immunology</topic><topic>Lung - metabolism</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Neutrophils - immunology</topic><topic>Neutrophils - metabolism</topic><topic>Polysaccharides - metabolism</topic><topic>Rabbits</topic><topic>S100 Proteins - immunology</topic><topic>S100 Proteins - isolation & purification</topic><topic>S100 Proteins - metabolism</topic><topic>S100 Proteins - physiology</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Srikrishna, Geetha</creatorcontrib><creatorcontrib>Panneerselvam, Krishnasamy</creatorcontrib><creatorcontrib>Westphal, Vibeke</creatorcontrib><creatorcontrib>Abraham, Violet</creatorcontrib><creatorcontrib>Varki, Ajit</creatorcontrib><creatorcontrib>Freeze, Hudson H</creatorcontrib><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><collection>MEDLINE - Academic</collection><jtitle>The Journal of immunology (1950)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Srikrishna, Geetha</au><au>Panneerselvam, Krishnasamy</au><au>Westphal, Vibeke</au><au>Abraham, Violet</au><au>Varki, Ajit</au><au>Freeze, Hudson H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two Proteins Modulating Transendothelial Migration of Leukocytes Recognize Novel Carboxylated Glycans on Endothelial Cells</atitle><jtitle>The Journal of immunology (1950)</jtitle><addtitle>J Immunol</addtitle><date>2001-04-01</date><risdate>2001</risdate><volume>166</volume><issue>7</issue><spage>4678</spage><epage>4688</epage><pages>4678-4688</pages><issn>0022-1767</issn><eissn>1550-6606</eissn><abstract>We recently showed that a class of novel carboxylated N:-glycans was constitutively expressed on endothelial cells. Activated, but not resting, neutrophils expressed binding sites for the novel glycans. We also showed that a mAb against these novel glycans (mAbGB3.1) inhibited leukocyte extravasation in a murine model of peritoneal inflammation. To identify molecules that mediated these interactions, we isolated binding proteins from bovine lung by their differential affinity for carboxylated or neutralized glycans. Two leukocyte calcium-binding proteins that bound in a carboxylate-dependent manner were identified as S100A8 and annexin I. An intact N terminus of annexin I and heteromeric assembly of S100A8 with S100A9 (another member of the S100 family) appeared necessary for this interaction. A mAb to S100A9 blocked neutrophil binding to immobilized carboxylated glycans. Purified human S100A8/A9 complex and recombinant human annexin I showed carboxylate-dependent binding to immobilized bovine lung carboxylated glycans and recognized a subset of mannose-labeled endothelial glycoproteins immunoprecipitated by mAbGB3.1. Saturable binding of S100A8/A9 complex to endothelial cells was also blocked by mAbGB3.1. These results suggest that the carboxylated glycans play important roles in leukocyte trafficking by interacting with proteins known to modulate extravasation.</abstract><cop>United States</cop><pub>Am Assoc Immnol</pub><pmid>11254728</pmid><doi>10.4049/jimmunol.166.7.4678</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of immunology (1950), 2001-04, Vol.166 (7), p.4678-4688 |
| issn | 0022-1767 1550-6606 |
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| subjects | Amino Acid Sequence Animals Annexin A1 - chemistry Annexin A1 - immunology Annexin A1 - metabolism annexin I Antibodies, Monoclonal - metabolism Antibodies, Monoclonal - pharmacology Antigens, Differentiation - immunology Antigens, Differentiation - isolation & purification Antigens, Differentiation - metabolism Antigens, Differentiation - physiology Binding Sites, Antibody Binding, Competitive - immunology Calcium-Binding Proteins - immunology Calcium-Binding Proteins - isolation & purification Calcium-Binding Proteins - metabolism Calcium-Binding Proteins - physiology Calgranulin A Calgranulin B Carboxylic Acids - metabolism Carrier Proteins - isolation & purification Carrier Proteins - metabolism Carrier Proteins - physiology Cattle Cell Adhesion - immunology Cell Membrane - immunology Cell Membrane - metabolism Cell Movement - immunology Chromatography, Affinity - methods Endothelium, Vascular - cytology Endothelium, Vascular - immunology Endothelium, Vascular - metabolism glycans Glycopeptides - chemical synthesis Glycopeptides - metabolism Humans Immune Sera - metabolism Immune Sera - pharmacology Leukocytes - immunology Leukocytes - metabolism Lung - cytology Lung - immunology Lung - metabolism Mice Molecular Sequence Data Molecular Weight Neutrophils - immunology Neutrophils - metabolism Polysaccharides - metabolism Rabbits S100 Proteins - immunology S100 Proteins - isolation & purification S100 Proteins - metabolism S100 Proteins - physiology Sequence Homology, Amino Acid |
| title | Two Proteins Modulating Transendothelial Migration of Leukocytes Recognize Novel Carboxylated Glycans on Endothelial Cells |
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