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Article: Expression of an extracellular domain of soluble leukocyte integrin beta-2 subunit (sCD18) and its functional implication

TitleExpression of an extracellular domain of soluble leukocyte integrin beta-2 subunit (sCD18) and its functional implication
Authors
Issue Date1996
PublisherFederation of American Societies for Experimental Biology. The Journal's web site is located at http://www.fasebj.org/
Citation
Faseb Journal, 1996, v. 10 n. 6, p. A1226 How to Cite?
AbstractLeukocyte beta-2 integrins are heterodimeric glycoproteins, composed of a common beta chain (CD18) noncovalently associated with three distinct alpha-chain subnnits (CDlla, CDllb, CDllc). We have successfully truncated the extracellular domain of human integrin beta-2 chain by site-directed mut agenesis, and expressed the soluble CD18 subunit without the association of integrin alpha chain. Transfection of COS cells with the truncated beta 2cDNA construct produced in culture supernatant, but not on the cell surface, a secretory protein with an apparent M.W. ∼80kD as revealed by SDS-PAGE. Production of the sCDlS protein in a CHO cell expression system gave milligram quantities, and the average yield in bulk culture was approximately 5-10 mg-/L as estimated by a sandwich ELISA assay. The sCDlS protein was purified by affinity chromatography using an anti-CD18 mAb. Eight anti-CD18 mAbs were used in an ELISA to assess the structural integrity of the soluble beta chain - three mAbs bound equally well to the sCDlS and the wild-type CDllc/CDl8, whereas four other mAbs bound stronger to the native form. Interestingly, one mAb reacted strongly with the recombinant sCDlS. These binding data suggested that the isolated sCDlS subunit is structurally similar to the native heterodimeric form, but its epitope pattern was somehow modified. Furthermore, the sCDlS protein was shown to be able to partially inhibit the PMA-induced neutrophil aggregation.
Persistent Identifierhttp://hdl.handle.net/10722/172857
ISSN
2015 Impact Factor: 5.299
2015 SCImago Journal Rankings: 2.775

 

DC FieldValueLanguage
dc.contributor.authorLuk, JMen_US
dc.contributor.authorSpringer, TAen_US
dc.date.accessioned2012-10-30T06:25:21Z-
dc.date.available2012-10-30T06:25:21Z-
dc.date.issued1996en_US
dc.identifier.citationFaseb Journal, 1996, v. 10 n. 6, p. A1226en_US
dc.identifier.issn0892-6638en_US
dc.identifier.urihttp://hdl.handle.net/10722/172857-
dc.description.abstractLeukocyte beta-2 integrins are heterodimeric glycoproteins, composed of a common beta chain (CD18) noncovalently associated with three distinct alpha-chain subnnits (CDlla, CDllb, CDllc). We have successfully truncated the extracellular domain of human integrin beta-2 chain by site-directed mut agenesis, and expressed the soluble CD18 subunit without the association of integrin alpha chain. Transfection of COS cells with the truncated beta 2cDNA construct produced in culture supernatant, but not on the cell surface, a secretory protein with an apparent M.W. ∼80kD as revealed by SDS-PAGE. Production of the sCDlS protein in a CHO cell expression system gave milligram quantities, and the average yield in bulk culture was approximately 5-10 mg-/L as estimated by a sandwich ELISA assay. The sCDlS protein was purified by affinity chromatography using an anti-CD18 mAb. Eight anti-CD18 mAbs were used in an ELISA to assess the structural integrity of the soluble beta chain - three mAbs bound equally well to the sCDlS and the wild-type CDllc/CDl8, whereas four other mAbs bound stronger to the native form. Interestingly, one mAb reacted strongly with the recombinant sCDlS. These binding data suggested that the isolated sCDlS subunit is structurally similar to the native heterodimeric form, but its epitope pattern was somehow modified. Furthermore, the sCDlS protein was shown to be able to partially inhibit the PMA-induced neutrophil aggregation.en_US
dc.languageengen_US
dc.publisherFederation of American Societies for Experimental Biology. The Journal's web site is located at http://www.fasebj.org/en_US
dc.relation.ispartofFASEB Journalen_US
dc.titleExpression of an extracellular domain of soluble leukocyte integrin beta-2 subunit (sCD18) and its functional implicationen_US
dc.typeArticleen_US
dc.identifier.emailLuk, JM: jmluk@hkucc.hku.hken_US
dc.identifier.authorityLuk, JM=rp00349en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-12644305351en_US
dc.identifier.volume10en_US
dc.identifier.issue6en_US
dc.identifier.spageA1226en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLuk, JM=7006777791en_US
dc.identifier.scopusauthoridSpringer, TA=35450639400en_US

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