The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast growth factor
E-SELECTIN is an inducible cell-adhesion molecule on endothelial cells, which mediates the binding of neutrophils and functions as a Ca 2+ -dependent lectin 1–3 . We have recently identified a 150K glycoprotein as the major ligand for E-selectin on myeloid cells, using a recombinant antibody-like fo...
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| Veröffentlicht in: | Nature (London) 1995-02, Vol.373 (6515), p.615-620 |
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| creator | Steegmaler, Martin Levinovitz, Agneta Isenmann, Sandra Borges, Eric Lenter, Martin Kocher, Hans P. Kleuser, Beate Vestweber, Dletmar |
| description | E-SELECTIN is an inducible cell-adhesion molecule on endothelial cells, which mediates the binding of neutrophils and functions as a Ca
2+
-dependent lectin
1–3
. We have recently identified a 150K glycoprotein as the major ligand for E-selectin on myeloid cells, using a recombinant antibody-like form of mouse E-selectin as an affinity probe
4,5
. Here we report the isolation of a mouse complementary DNA for this E-selectin ligand (ESL-1). The predicted amino-acid sequence of ESL-1 is 94% identical (over 1,078 amino acids) to the recently identified chicken cysteine-rich fibroblast growth-factor receptor
6
, except for a unique 70-amino-acid amino-terminal domain of mature ESL-1. Fucosylation of ESL-1 is imperative for affinity isolation with E-selectin-IgG. A fucosylated, recombinant antibody-like form of ESL-1, but not of L-selectin, supports adhesion of E-selectin-transfected Chinese hamster ovary cells. Antibodies against ESL-1 block the binding of mouse myeloid cells to E-selectin. ESL-1, with a structure essentially identical to that of a receptor, thus functions as a cell adhesion ligand of E-selectin. |
| doi_str_mv | 10.1038/373615a0 |
| format | Article |
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2+
-dependent lectin
1–3
. We have recently identified a 150K glycoprotein as the major ligand for E-selectin on myeloid cells, using a recombinant antibody-like form of mouse E-selectin as an affinity probe
4,5
. Here we report the isolation of a mouse complementary DNA for this E-selectin ligand (ESL-1). The predicted amino-acid sequence of ESL-1 is 94% identical (over 1,078 amino acids) to the recently identified chicken cysteine-rich fibroblast growth-factor receptor
6
, except for a unique 70-amino-acid amino-terminal domain of mature ESL-1. Fucosylation of ESL-1 is imperative for affinity isolation with E-selectin-IgG. A fucosylated, recombinant antibody-like form of ESL-1, but not of L-selectin, supports adhesion of E-selectin-transfected Chinese hamster ovary cells. Antibodies against ESL-1 block the binding of mouse myeloid cells to E-selectin. ESL-1, with a structure essentially identical to that of a receptor, thus functions as a cell adhesion ligand of E-selectin.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/373615a0</identifier><identifier>PMID: 7531823</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Adhesion ; Amino Acid Sequence ; Amino acids ; Animals ; Base Sequence ; Cell Adhesion Molecules - metabolism ; Chickens ; CHO Cells ; Cloning, Molecular ; Cricetinae ; Deoxyribonucleic acid ; DNA ; DNA, Complementary ; E-Selectin ; Fucose - metabolism ; Glycoproteins - chemistry ; Glycoproteins - genetics ; Glycoproteins - isolation & purification ; Glycoproteins - metabolism ; Humanities and Social Sciences ; Humans ; Immunoglobulin G - genetics ; Immunoglobulin G - metabolism ; letter ; Ligands ; Membrane Glycoproteins - genetics ; Membrane Glycoproteins - isolation & purification ; Membrane Glycoproteins - metabolism ; Mice ; Molecular Sequence Data ; Molecules ; multidisciplinary ; Neutrophils - metabolism ; Precipitin Tests ; Protein Binding ; Receptors, Fibroblast Growth Factor - chemistry ; Receptors, Fibroblast Growth Factor - genetics ; Receptors, Fibroblast Growth Factor - isolation & purification ; Receptors, Fibroblast Growth Factor - metabolism ; Receptors, Immunologic - genetics ; Receptors, Immunologic - isolation & purification ; Receptors, Immunologic - metabolism ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Rodents ; Science ; Science (multidisciplinary) ; Sequence Homology, Amino Acid ; Sialoglycoproteins ; Transfection</subject><ispartof>Nature (London), 1995-02, Vol.373 (6515), p.615-620</ispartof><rights>Springer Nature Limited 1995</rights><rights>Copyright Macmillan Journals Ltd. Feb 16, 1995</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c468t-a29fcbbedebd343c7224b48272acbb5ad0415c954028ead5fb5430f06b0130993</citedby><cites>FETCH-LOGICAL-c468t-a29fcbbedebd343c7224b48272acbb5ad0415c954028ead5fb5430f06b0130993</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/373615a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/373615a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7531823$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Steegmaler, Martin</creatorcontrib><creatorcontrib>Levinovitz, Agneta</creatorcontrib><creatorcontrib>Isenmann, Sandra</creatorcontrib><creatorcontrib>Borges, Eric</creatorcontrib><creatorcontrib>Lenter, Martin</creatorcontrib><creatorcontrib>Kocher, Hans P.</creatorcontrib><creatorcontrib>Kleuser, Beate</creatorcontrib><creatorcontrib>Vestweber, Dletmar</creatorcontrib><title>The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast growth factor</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>E-SELECTIN is an inducible cell-adhesion molecule on endothelial cells, which mediates the binding of neutrophils and functions as a Ca
2+
-dependent lectin
1–3
. We have recently identified a 150K glycoprotein as the major ligand for E-selectin on myeloid cells, using a recombinant antibody-like form of mouse E-selectin as an affinity probe
4,5
. Here we report the isolation of a mouse complementary DNA for this E-selectin ligand (ESL-1). The predicted amino-acid sequence of ESL-1 is 94% identical (over 1,078 amino acids) to the recently identified chicken cysteine-rich fibroblast growth-factor receptor
6
, except for a unique 70-amino-acid amino-terminal domain of mature ESL-1. Fucosylation of ESL-1 is imperative for affinity isolation with E-selectin-IgG. A fucosylated, recombinant antibody-like form of ESL-1, but not of L-selectin, supports adhesion of E-selectin-transfected Chinese hamster ovary cells. Antibodies against ESL-1 block the binding of mouse myeloid cells to E-selectin. ESL-1, with a structure essentially identical to that of a receptor, thus functions as a cell adhesion ligand of E-selectin.</description><subject>Adhesion</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Chickens</subject><subject>CHO Cells</subject><subject>Cloning, Molecular</subject><subject>Cricetinae</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA, Complementary</subject><subject>E-Selectin</subject><subject>Fucose - metabolism</subject><subject>Glycoproteins - chemistry</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - isolation & purification</subject><subject>Glycoproteins - metabolism</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Immunoglobulin G - genetics</subject><subject>Immunoglobulin G - metabolism</subject><subject>letter</subject><subject>Ligands</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - isolation & purification</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Molecules</subject><subject>multidisciplinary</subject><subject>Neutrophils - metabolism</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>Receptors, Fibroblast Growth Factor - chemistry</subject><subject>Receptors, Fibroblast Growth Factor - genetics</subject><subject>Receptors, Fibroblast Growth Factor - isolation & purification</subject><subject>Receptors, Fibroblast Growth Factor - metabolism</subject><subject>Receptors, Immunologic - genetics</subject><subject>Receptors, Immunologic - isolation & purification</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Rodents</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sialoglycoproteins</subject><subject>Transfection</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkUtLAzEUhYMotVbBPyAEFz4WozfvmaWU-oCCi9b1kGQy7ch0piZTxX9vSquCgi7CJTkf5-beg9AxgSsCLL1mikkiNOygPuFKJlymahf1AWiaQMrkPjoI4RkABFG8h3pKMJJS1keT6dzhURJc7WxXNUldzXRT4NFknBBcBazxq_aVbjrclvHinXXLrvW4XJ_K-NbUOnR45tu3bo5LbaN4iPZKXQd3tK0D9HQ7mg7vk_Hj3cPwZpzY-L0u0TQrrTGucKZgnFlFKTc8pYrq-Cx0AZwImwkeh3C6EKURnEEJ0gBhkGVsgM42vkvfvqxc6PJFFayra924dhVypda7SEUEz_8GORMUJIN_LYmUIKhUETz9AT63K9_EcXMKnKecwxq62EDWtyF4V-ZLXy20f88J5Ovc8s_cInqy9VuZhSu-wG1QUb_c6CEqzcz5736_vD4ARm-crw</recordid><startdate>19950216</startdate><enddate>19950216</enddate><creator>Steegmaler, Martin</creator><creator>Levinovitz, 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E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast growth factor</title><author>Steegmaler, Martin ; Levinovitz, Agneta ; Isenmann, Sandra ; Borges, Eric ; Lenter, Martin ; Kocher, Hans P. ; Kleuser, Beate ; Vestweber, Dletmar</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c468t-a29fcbbedebd343c7224b48272acbb5ad0415c954028ead5fb5430f06b0130993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adhesion</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Chickens</topic><topic>CHO Cells</topic><topic>Cloning, Molecular</topic><topic>Cricetinae</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA, Complementary</topic><topic>E-Selectin</topic><topic>Fucose - metabolism</topic><topic>Glycoproteins - chemistry</topic><topic>Glycoproteins - genetics</topic><topic>Glycoproteins - isolation & purification</topic><topic>Glycoproteins - metabolism</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Immunoglobulin G - genetics</topic><topic>Immunoglobulin G - metabolism</topic><topic>letter</topic><topic>Ligands</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane Glycoproteins - isolation & purification</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Molecules</topic><topic>multidisciplinary</topic><topic>Neutrophils - metabolism</topic><topic>Precipitin Tests</topic><topic>Protein Binding</topic><topic>Receptors, Fibroblast Growth Factor - chemistry</topic><topic>Receptors, Fibroblast Growth Factor - genetics</topic><topic>Receptors, Fibroblast Growth Factor - isolation & purification</topic><topic>Receptors, Fibroblast Growth Factor - metabolism</topic><topic>Receptors, Immunologic - genetics</topic><topic>Receptors, Immunologic - isolation & purification</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Rodents</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sialoglycoproteins</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Steegmaler, Martin</creatorcontrib><creatorcontrib>Levinovitz, Agneta</creatorcontrib><creatorcontrib>Isenmann, Sandra</creatorcontrib><creatorcontrib>Borges, Eric</creatorcontrib><creatorcontrib>Lenter, Martin</creatorcontrib><creatorcontrib>Kocher, Hans P.</creatorcontrib><creatorcontrib>Kleuser, Beate</creatorcontrib><creatorcontrib>Vestweber, 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(London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1995-02-16</date><risdate>1995</risdate><volume>373</volume><issue>6515</issue><spage>615</spage><epage>620</epage><pages>615-620</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>E-SELECTIN is an inducible cell-adhesion molecule on endothelial cells, which mediates the binding of neutrophils and functions as a Ca
2+
-dependent lectin
1–3
. We have recently identified a 150K glycoprotein as the major ligand for E-selectin on myeloid cells, using a recombinant antibody-like form of mouse E-selectin as an affinity probe
4,5
. Here we report the isolation of a mouse complementary DNA for this E-selectin ligand (ESL-1). The predicted amino-acid sequence of ESL-1 is 94% identical (over 1,078 amino acids) to the recently identified chicken cysteine-rich fibroblast growth-factor receptor
6
, except for a unique 70-amino-acid amino-terminal domain of mature ESL-1. Fucosylation of ESL-1 is imperative for affinity isolation with E-selectin-IgG. A fucosylated, recombinant antibody-like form of ESL-1, but not of L-selectin, supports adhesion of E-selectin-transfected Chinese hamster ovary cells. Antibodies against ESL-1 block the binding of mouse myeloid cells to E-selectin. ESL-1, with a structure essentially identical to that of a receptor, thus functions as a cell adhesion ligand of E-selectin.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>7531823</pmid><doi>10.1038/373615a0</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1995-02, Vol.373 (6515), p.615-620 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77147685 |
| source | MEDLINE; SpringerLink Journals (MCLS); Nature Journals Online |
| subjects | Adhesion Amino Acid Sequence Amino acids Animals Base Sequence Cell Adhesion Molecules - metabolism Chickens CHO Cells Cloning, Molecular Cricetinae Deoxyribonucleic acid DNA DNA, Complementary E-Selectin Fucose - metabolism Glycoproteins - chemistry Glycoproteins - genetics Glycoproteins - isolation & purification Glycoproteins - metabolism Humanities and Social Sciences Humans Immunoglobulin G - genetics Immunoglobulin G - metabolism letter Ligands Membrane Glycoproteins - genetics Membrane Glycoproteins - isolation & purification Membrane Glycoproteins - metabolism Mice Molecular Sequence Data Molecules multidisciplinary Neutrophils - metabolism Precipitin Tests Protein Binding Receptors, Fibroblast Growth Factor - chemistry Receptors, Fibroblast Growth Factor - genetics Receptors, Fibroblast Growth Factor - isolation & purification Receptors, Fibroblast Growth Factor - metabolism Receptors, Immunologic - genetics Receptors, Immunologic - isolation & purification Receptors, Immunologic - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Rodents Science Science (multidisciplinary) Sequence Homology, Amino Acid Sialoglycoproteins Transfection |
| title | The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast growth factor |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-31T23%3A16%3A07IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20E-selectin-ligand%20ESL-1%20is%20a%20variant%20of%20a%20receptor%20for%20fibroblast%20growth%20factor&rft.jtitle=Nature%20(London)&rft.au=Steegmaler,%20Martin&rft.date=1995-02-16&rft.volume=373&rft.issue=6515&rft.spage=615&rft.epage=620&rft.pages=615-620&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/373615a0&rft_dat=%3Cproquest_cross%3E743520630%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=204484407&rft_id=info:pmid/7531823&rfr_iscdi=true |