Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18
Neutrophil inhibitory factor (NIF) is a hookworm-derived glycoprotein ligand of the integrin CD11b/CD18 that inhibits human neutrophil function (Moyle, M., Foster, D. L., McGrath, D. E., Brown, S. M., Laroche, Y., De Meutter, J., Stanssens, P., Bogowitz, C. A., Fried, V. A., Ely, J. A., Soule, H. R....
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| Veröffentlicht in: | The Journal of biological chemistry 1994-10, Vol.269 (42), p.26419-26423 |
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| creator | Muchowski, P J Zhang, L Chang, E R Soule, H R Plow, E F Moyle, M |
| description | Neutrophil inhibitory factor (NIF) is a hookworm-derived glycoprotein ligand of the integrin CD11b/CD18 that inhibits human
neutrophil function (Moyle, M., Foster, D. L., McGrath, D. E., Brown, S. M., Laroche, Y., De Meutter, J., Stanssens, P., Bogowitz,
C. A., Fried, V. A., Ely, J. A., Soule, H. R., and Vlasuk, G. P. (1994) J. Biol. Chem. 269, 1008-10015). Here, we present
evidence that recombinant NIF (rNIF) associates with the approximately 200-amino acid residue I domain of CD11b/CD18 and that
this interaction is essential for inhibition of neutrophil function by NIF. First, radiolabeled rNIF binds to a recombinant
glutathione S-transferase fusion protein that contains the CD11b I domain. This high affinity interaction has a partial dependence
on divalent cations. The association of rNIF with the CD11b I domain is specific because 125I-rNIF does not bind either a
glutathione S-transferase fusion protein that contains the I domain of the integrin CD11a/CD18 or recombinant glutathione
S-transferase without the I domain. Second, the CD11b I domain fusion protein effectively competes with CD11b/CD18 on human
neutrophils for 125I-rNIF binding. Third, the CD11b I domain fusion protein blocks the inhibition of certain neutrophil functions
by rNIF, including adhesion of neutrophils to human endothelial cell monolayers and adhesion-dependent release of hydrogen
peroxide from neutrophils. Specificity is demonstrated by the inability of the CD11a I domain fusion protein to block either
rNIF binding to neutrophils or rNIF activity. Fourth, rNIF blocks the interaction between neutrophils and fibrinogen, a CD11b/CD18
ligand that is also thought to bind the I domain of CD11b. In contrast, rNIF does not appear to block the binding of factor
X to CD11b/CD18 on neutrophils. These results suggest that CD11b/CD18 has multiple distinct binding sites for its cognate
ligands, including, but not limited to, the I domain. NIF interferes with the binding of a subset of these CD11b/CD18 ligands
in a highly selective manner. |
| doi_str_mv | 10.1016/S0021-9258(18)47210-9 |
| format | Article |
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neutrophil function (Moyle, M., Foster, D. L., McGrath, D. E., Brown, S. M., Laroche, Y., De Meutter, J., Stanssens, P., Bogowitz,
C. A., Fried, V. A., Ely, J. A., Soule, H. R., and Vlasuk, G. P. (1994) J. Biol. Chem. 269, 1008-10015). Here, we present
evidence that recombinant NIF (rNIF) associates with the approximately 200-amino acid residue I domain of CD11b/CD18 and that
this interaction is essential for inhibition of neutrophil function by NIF. First, radiolabeled rNIF binds to a recombinant
glutathione S-transferase fusion protein that contains the CD11b I domain. This high affinity interaction has a partial dependence
on divalent cations. The association of rNIF with the CD11b I domain is specific because 125I-rNIF does not bind either a
glutathione S-transferase fusion protein that contains the I domain of the integrin CD11a/CD18 or recombinant glutathione
S-transferase without the I domain. Second, the CD11b I domain fusion protein effectively competes with CD11b/CD18 on human
neutrophils for 125I-rNIF binding. Third, the CD11b I domain fusion protein blocks the inhibition of certain neutrophil functions
by rNIF, including adhesion of neutrophils to human endothelial cell monolayers and adhesion-dependent release of hydrogen
peroxide from neutrophils. Specificity is demonstrated by the inability of the CD11a I domain fusion protein to block either
rNIF binding to neutrophils or rNIF activity. Fourth, rNIF blocks the interaction between neutrophils and fibrinogen, a CD11b/CD18
ligand that is also thought to bind the I domain of CD11b. In contrast, rNIF does not appear to block the binding of factor
X to CD11b/CD18 on neutrophils. These results suggest that CD11b/CD18 has multiple distinct binding sites for its cognate
ligands, including, but not limited to, the I domain. NIF interferes with the binding of a subset of these CD11b/CD18 ligands
in a highly selective manner.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)47210-9</identifier><identifier>PMID: 7929363</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Base Sequence ; Binding Sites ; CD11 Antigens - metabolism ; CHO Cells ; Cricetinae ; Glycoproteins - metabolism ; Glycoproteins - pharmacology ; Helminth Proteins - metabolism ; Helminth Proteins - pharmacology ; Integrins - antagonists & inhibitors ; Macrophage-1 Antigen - metabolism ; Membrane Proteins ; Molecular Sequence Data ; Neutrophils - drug effects ; Recombinant Proteins - metabolism</subject><ispartof>The Journal of biological chemistry, 1994-10, Vol.269 (42), p.26419-26423</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c380t-2e734e373ab66415494ed1020c9f36af2ef3c2c815f64241bd10a6e6f5c1aa3a3</citedby><cites>FETCH-LOGICAL-c380t-2e734e373ab66415494ed1020c9f36af2ef3c2c815f64241bd10a6e6f5c1aa3a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7929363$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Muchowski, P J</creatorcontrib><creatorcontrib>Zhang, L</creatorcontrib><creatorcontrib>Chang, E R</creatorcontrib><creatorcontrib>Soule, H R</creatorcontrib><creatorcontrib>Plow, E F</creatorcontrib><creatorcontrib>Moyle, M</creatorcontrib><title>Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Neutrophil inhibitory factor (NIF) is a hookworm-derived glycoprotein ligand of the integrin CD11b/CD18 that inhibits human
neutrophil function (Moyle, M., Foster, D. L., McGrath, D. E., Brown, S. M., Laroche, Y., De Meutter, J., Stanssens, P., Bogowitz,
C. A., Fried, V. A., Ely, J. A., Soule, H. R., and Vlasuk, G. P. (1994) J. Biol. Chem. 269, 1008-10015). Here, we present
evidence that recombinant NIF (rNIF) associates with the approximately 200-amino acid residue I domain of CD11b/CD18 and that
this interaction is essential for inhibition of neutrophil function by NIF. First, radiolabeled rNIF binds to a recombinant
glutathione S-transferase fusion protein that contains the CD11b I domain. This high affinity interaction has a partial dependence
on divalent cations. The association of rNIF with the CD11b I domain is specific because 125I-rNIF does not bind either a
glutathione S-transferase fusion protein that contains the I domain of the integrin CD11a/CD18 or recombinant glutathione
S-transferase without the I domain. Second, the CD11b I domain fusion protein effectively competes with CD11b/CD18 on human
neutrophils for 125I-rNIF binding. Third, the CD11b I domain fusion protein blocks the inhibition of certain neutrophil functions
by rNIF, including adhesion of neutrophils to human endothelial cell monolayers and adhesion-dependent release of hydrogen
peroxide from neutrophils. Specificity is demonstrated by the inability of the CD11a I domain fusion protein to block either
rNIF binding to neutrophils or rNIF activity. Fourth, rNIF blocks the interaction between neutrophils and fibrinogen, a CD11b/CD18
ligand that is also thought to bind the I domain of CD11b. In contrast, rNIF does not appear to block the binding of factor
X to CD11b/CD18 on neutrophils. These results suggest that CD11b/CD18 has multiple distinct binding sites for its cognate
ligands, including, but not limited to, the I domain. NIF interferes with the binding of a subset of these CD11b/CD18 ligands
in a highly selective manner.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>CD11 Antigens - metabolism</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Glycoproteins - metabolism</subject><subject>Glycoproteins - pharmacology</subject><subject>Helminth Proteins - metabolism</subject><subject>Helminth Proteins - pharmacology</subject><subject>Integrins - antagonists & inhibitors</subject><subject>Macrophage-1 Antigen - metabolism</subject><subject>Membrane Proteins</subject><subject>Molecular Sequence Data</subject><subject>Neutrophils - drug effects</subject><subject>Recombinant Proteins - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kF1rHCEUhqW0pNs0PyEwF6W0F9N41HHGy7JpPiCQi7SQO3HcMzuWHd2qQ8i_rzu7xAsP-r6PwkPIJdAfQEFePVHKoFas6b5B9120DGit3pEV0I7XvIHn92T1VvlIPqX0l5YlFJyRs1YxxSVfkXgze5td8GZXOZ8xmuVU9ZhfEH2VR1zut9H5yvhstsG7lCuPc45hP7oDNrre5RBfq6HQIZbeZgHvq02YTAHDUK2vAfqrsnefyYfB7BJenOY5-XPz6_f6rn54vL1f_3yoLe9orhm2XCBvuemlFNAIJXADlFGrBi7NwHDgltkOmkEKJqAvoZEoh8aCMdzwc_L1-O4-hn8zpqwnlyzudsZjmJNuZdsUH6IUm2PRxpBSxEHvo5tMfNVA9cG1Xlzrg0gNnV5ca1W4y9MHcz_h5o06yS35l2M-uu344iLq3gU74qSZVFqwMgQo_h_X-IZ8</recordid><startdate>19941021</startdate><enddate>19941021</enddate><creator>Muchowski, P J</creator><creator>Zhang, L</creator><creator>Chang, E R</creator><creator>Soule, H R</creator><creator>Plow, E F</creator><creator>Moyle, M</creator><general>American Society for Biochemistry and Molecular Biology</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>7X8</scope></search><sort><creationdate>19941021</creationdate><title>Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18</title><author>Muchowski, P J ; Zhang, L ; Chang, E R ; Soule, H R ; Plow, E F ; Moyle, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c380t-2e734e373ab66415494ed1020c9f36af2ef3c2c815f64241bd10a6e6f5c1aa3a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>CD11 Antigens - metabolism</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Glycoproteins - metabolism</topic><topic>Glycoproteins - pharmacology</topic><topic>Helminth Proteins - metabolism</topic><topic>Helminth Proteins - pharmacology</topic><topic>Integrins - antagonists & inhibitors</topic><topic>Macrophage-1 Antigen - metabolism</topic><topic>Membrane Proteins</topic><topic>Molecular Sequence Data</topic><topic>Neutrophils - drug effects</topic><topic>Recombinant Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Muchowski, P J</creatorcontrib><creatorcontrib>Zhang, L</creatorcontrib><creatorcontrib>Chang, E R</creatorcontrib><creatorcontrib>Soule, H R</creatorcontrib><creatorcontrib>Plow, E F</creatorcontrib><creatorcontrib>Moyle, M</creatorcontrib><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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Muchowski, P J</au><au>Zhang, L</au><au>Chang, E R</au><au>Soule, H R</au><au>Plow, E F</au><au>Moyle, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-10-21</date><risdate>1994</risdate><volume>269</volume><issue>42</issue><spage>26419</spage><epage>26423</epage><pages>26419-26423</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Neutrophil inhibitory factor (NIF) is a hookworm-derived glycoprotein ligand of the integrin CD11b/CD18 that inhibits human
neutrophil function (Moyle, M., Foster, D. L., McGrath, D. E., Brown, S. M., Laroche, Y., De Meutter, J., Stanssens, P., Bogowitz,
C. A., Fried, V. A., Ely, J. A., Soule, H. R., and Vlasuk, G. P. (1994) J. Biol. Chem. 269, 1008-10015). Here, we present
evidence that recombinant NIF (rNIF) associates with the approximately 200-amino acid residue I domain of CD11b/CD18 and that
this interaction is essential for inhibition of neutrophil function by NIF. First, radiolabeled rNIF binds to a recombinant
glutathione S-transferase fusion protein that contains the CD11b I domain. This high affinity interaction has a partial dependence
on divalent cations. The association of rNIF with the CD11b I domain is specific because 125I-rNIF does not bind either a
glutathione S-transferase fusion protein that contains the I domain of the integrin CD11a/CD18 or recombinant glutathione
S-transferase without the I domain. Second, the CD11b I domain fusion protein effectively competes with CD11b/CD18 on human
neutrophils for 125I-rNIF binding. Third, the CD11b I domain fusion protein blocks the inhibition of certain neutrophil functions
by rNIF, including adhesion of neutrophils to human endothelial cell monolayers and adhesion-dependent release of hydrogen
peroxide from neutrophils. Specificity is demonstrated by the inability of the CD11a I domain fusion protein to block either
rNIF binding to neutrophils or rNIF activity. Fourth, rNIF blocks the interaction between neutrophils and fibrinogen, a CD11b/CD18
ligand that is also thought to bind the I domain of CD11b. In contrast, rNIF does not appear to block the binding of factor
X to CD11b/CD18 on neutrophils. These results suggest that CD11b/CD18 has multiple distinct binding sites for its cognate
ligands, including, but not limited to, the I domain. NIF interferes with the binding of a subset of these CD11b/CD18 ligands
in a highly selective manner.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7929363</pmid><doi>10.1016/S0021-9258(18)47210-9</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | The Journal of biological chemistry, 1994-10, Vol.269 (42), p.26419-26423 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76750044 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Base Sequence Binding Sites CD11 Antigens - metabolism CHO Cells Cricetinae Glycoproteins - metabolism Glycoproteins - pharmacology Helminth Proteins - metabolism Helminth Proteins - pharmacology Integrins - antagonists & inhibitors Macrophage-1 Antigen - metabolism Membrane Proteins Molecular Sequence Data Neutrophils - drug effects Recombinant Proteins - metabolism |
| title | Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18 |
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