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Article: Characterization of a chimeric monoclonal antibody against the insulin-like growth factor-I receptor.
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TitleCharacterization of a chimeric monoclonal antibody against the insulin-like growth factor-I receptor.
 
AuthorsZhang, MY
Feng, Y
Wang, Y
Dimitrov, DS
 
Issue Date2009
 
PublisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/mabs/
 
CitationMabs, 2009, v. 1 n. 5, p. 475-480 [How to Cite?]
 
AbstractThe insulin-like growth factors (IGFs) signaling system has been shown to play important roles in neoplasia. The IGF receptor type 1 (IGF-IR) is overexpressed in many types of solid and hematopoietic malignancies, and there is substantial experimental and clinical evidence that targeting IGF-IR is a promising therapeutic strategy against cancer. It has been previously reported that a mouse monoclonal antibody (mAb), 4G11, blocked IGF-I binding to IGF-IR and downregulated the IGF-IR in MCF-7 cells. We cloned this antibody, constructed a human-mouse chimeric antibody, designated m590, and characterized it. The chimeric IgG1 m590 bound to cell-associated IGF-IR on NWT c43 stably transfected cells and MCF-7 breast cancer cells as efficiently as the parental murine antibody. Using purified IGF-IR extracellular domains, we found that both the chimeric m590 and the parental 4G11 antibodies bind to conformational epitopes on IGF-IR. Neither of these antibodies bound to the insulin receptor (IR) ectodomain. Furthermore, IgG1 m590 blocked the binding of IGF-I and IGF-II to IGF-IR, and inhibited both IGF-I and IGF-II induced phosphorylation of IGF-IR in MCF-7 cells. These results suggest that m590 could be an useful antibody in diagnosis and treatment of cancer, as well as a research tool.
 
ISSN1942-0870
2013 SCImago Journal Rankings: 1.547
1942-0862
2013 Impact Factor: 4.726
 
PubMed Central IDPMC2759497
 
ISI Accession Number IDWOS:000271989300009
 
DC FieldValue
dc.contributor.authorZhang, MY
 
dc.contributor.authorFeng, Y
 
dc.contributor.authorWang, Y
 
dc.contributor.authorDimitrov, DS
 
dc.date.accessioned2010-09-17T10:24:11Z
 
dc.date.available2010-09-17T10:24:11Z
 
dc.date.issued2009
 
dc.description.abstractThe insulin-like growth factors (IGFs) signaling system has been shown to play important roles in neoplasia. The IGF receptor type 1 (IGF-IR) is overexpressed in many types of solid and hematopoietic malignancies, and there is substantial experimental and clinical evidence that targeting IGF-IR is a promising therapeutic strategy against cancer. It has been previously reported that a mouse monoclonal antibody (mAb), 4G11, blocked IGF-I binding to IGF-IR and downregulated the IGF-IR in MCF-7 cells. We cloned this antibody, constructed a human-mouse chimeric antibody, designated m590, and characterized it. The chimeric IgG1 m590 bound to cell-associated IGF-IR on NWT c43 stably transfected cells and MCF-7 breast cancer cells as efficiently as the parental murine antibody. Using purified IGF-IR extracellular domains, we found that both the chimeric m590 and the parental 4G11 antibodies bind to conformational epitopes on IGF-IR. Neither of these antibodies bound to the insulin receptor (IR) ectodomain. Furthermore, IgG1 m590 blocked the binding of IGF-I and IGF-II to IGF-IR, and inhibited both IGF-I and IGF-II induced phosphorylation of IGF-IR in MCF-7 cells. These results suggest that m590 could be an useful antibody in diagnosis and treatment of cancer, as well as a research tool.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationMabs, 2009, v. 1 n. 5, p. 475-480 [How to Cite?]
 
dc.identifier.epage480
 
dc.identifier.hkuros170373
 
dc.identifier.isiWOS:000271989300009
 
dc.identifier.issn1942-0870
2013 SCImago Journal Rankings: 1.547
 
dc.identifier.issn1942-0862
2013 Impact Factor: 4.726
 
dc.identifier.issue5
 
dc.identifier.openurl
 
dc.identifier.pmcidPMC2759497
 
dc.identifier.pmid20065647
 
dc.identifier.scopuseid_2-s2.0-77950358405
 
dc.identifier.scopuseid_2-s2.0-77953655319
 
dc.identifier.spage475
 
dc.identifier.urihttp://hdl.handle.net/10722/91715
 
dc.identifier.volume1
 
dc.languageeng
 
dc.publisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/mabs/
 
dc.relation.ispartofmAbs
 
dc.subject.meshAntibodies, Monoclonal - chemistry - genetics - immunology - metabolism
 
dc.subject.meshReceptor, IGF Type 1 - immunology - metabolism
 
dc.subject.meshRecombinant Proteins - chemistry - genetics - immunology - metabolism
 
dc.subject.meshAmino Acid Sequence
 
dc.subject.meshAnimals
 
dc.titleCharacterization of a chimeric monoclonal antibody against the insulin-like growth factor-I receptor.
 
dc.typeArticle
 
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<contributor.author>Wang, Y</contributor.author>
<contributor.author>Dimitrov, DS</contributor.author>
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<description.abstract>The insulin-like growth factors (IGFs) signaling system has been shown to play important roles in neoplasia. The IGF receptor type 1 (IGF-IR) is overexpressed in many types of solid and hematopoietic malignancies, and there is substantial experimental and clinical evidence that targeting IGF-IR is a promising therapeutic strategy against cancer. It has been previously reported that a mouse monoclonal antibody (mAb), 4G11, blocked IGF-I binding to IGF-IR and downregulated the IGF-IR in MCF-7 cells. We cloned this antibody, constructed a human-mouse chimeric antibody, designated m590, and characterized it. The chimeric IgG1 m590 bound to cell-associated IGF-IR on NWT c43 stably transfected cells and MCF-7 breast cancer cells as efficiently as the parental murine antibody. Using purified IGF-IR extracellular domains, we found that both the chimeric m590 and the parental 4G11 antibodies bind to conformational epitopes on IGF-IR. Neither of these antibodies bound to the insulin receptor (IR) ectodomain. Furthermore, IgG1 m590 blocked the binding of IGF-I and IGF-II to IGF-IR, and inhibited both IGF-I and IGF-II induced phosphorylation of IGF-IR in MCF-7 cells. These results suggest that m590 could be an useful antibody in diagnosis and treatment of cancer, as well as a research tool.</description.abstract>
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Author Affiliations
  1. National Cancer Institute at Frederick