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Article: Production and characterization of a humanized single-chain antibody against human integrin αvβ3 protein

TitleProduction and characterization of a humanized single-chain antibody against human integrin αvβ3 protein
Authors
Issue Date2011
Citation
Journal of Biological Chemistry, 2011, v. 286, n. 27, p. 24500-24507 How to Cite?
AbstractAnti-angiogenesis therapy is an emerging strategy for cancer treatment. This therapy has many advantages over existing treatments, such as fewer side effects, fewer resistance problems, and a broader tumor type spectrum. Integrin αvβ3 is a heterodimeric transmembrane glycoprotein that has been demonstrated to play a key role in tumor angiogenesis and metastasis. Wehave used a phage antibody display to humanize a mouse monoclonal antibody (mAb E10) against human integrin αvβ3 with a predetermined CDR3 gene. Three human phage antibodies were developed. Analysis of the humanized phage antibodies by phage ELISA revealed that the antibodies retained high antigen-binding activity and detected the same epitope as the parent mAb E10. A humanized single chain Fv (scFv) antibody was expressed in Escherichia coli in a soluble form. Analysis of the purified scFv indicated that it has the same specificity and affinity as the original mAb. Cell viability assays and xenograft model results suggested that the humanized scFv possesses anti-tumor growth activity in vitro and in vivo. This successful production of a humanized scFv with the ability to inhibit αvβ3-mediated cancer cell growth may provide a novel candidate for integrin αvβ3-targeted therapy. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/297320
ISSN
2020 Impact Factor: 5.157
2023 SCImago Journal Rankings: 1.766
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLiu, Dabin-
dc.contributor.authorWang, Chen-
dc.contributor.authorLi, Cun-
dc.contributor.authorZhang, Xin-
dc.contributor.authorZhang, Baozhong-
dc.contributor.authorMi, Zhiqiang-
dc.contributor.authorAn, Xiaoping-
dc.contributor.authorTong, Yigang-
dc.date.accessioned2021-03-15T07:33:31Z-
dc.date.available2021-03-15T07:33:31Z-
dc.date.issued2011-
dc.identifier.citationJournal of Biological Chemistry, 2011, v. 286, n. 27, p. 24500-24507-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10722/297320-
dc.description.abstractAnti-angiogenesis therapy is an emerging strategy for cancer treatment. This therapy has many advantages over existing treatments, such as fewer side effects, fewer resistance problems, and a broader tumor type spectrum. Integrin αvβ3 is a heterodimeric transmembrane glycoprotein that has been demonstrated to play a key role in tumor angiogenesis and metastasis. Wehave used a phage antibody display to humanize a mouse monoclonal antibody (mAb E10) against human integrin αvβ3 with a predetermined CDR3 gene. Three human phage antibodies were developed. Analysis of the humanized phage antibodies by phage ELISA revealed that the antibodies retained high antigen-binding activity and detected the same epitope as the parent mAb E10. A humanized single chain Fv (scFv) antibody was expressed in Escherichia coli in a soluble form. Analysis of the purified scFv indicated that it has the same specificity and affinity as the original mAb. Cell viability assays and xenograft model results suggested that the humanized scFv possesses anti-tumor growth activity in vitro and in vivo. This successful production of a humanized scFv with the ability to inhibit αvβ3-mediated cancer cell growth may provide a novel candidate for integrin αvβ3-targeted therapy. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.-
dc.languageeng-
dc.relation.ispartofJournal of Biological Chemistry-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleProduction and characterization of a humanized single-chain antibody against human integrin αvβ3 protein-
dc.typeArticle-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1074/jbc.M110.211847-
dc.identifier.pmid21606501-
dc.identifier.pmcidPMC3129229-
dc.identifier.scopuseid_2-s2.0-79959907602-
dc.identifier.volume286-
dc.identifier.issue27-
dc.identifier.spage24500-
dc.identifier.epage24507-
dc.identifier.eissn1083-351X-
dc.identifier.isiWOS:000292294900090-
dc.identifier.issnl0021-9258-

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