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Antibody neutralization of cell-surface gC1qR/HABP1/SF2-p32 prevents lamellipodia formation and tumorigenesis

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dc.contributor.authorKim, Beom-Chan-
dc.contributor.authorHwang, Hyun-Jung-
dc.contributor.authorAn, Hyoung-Tae-
dc.contributor.authorLee, Hyun-
dc.contributor.authorPark, Jun-Sub-
dc.contributor.authorHong, Jin-
dc.contributor.authorKo, Jesang-
dc.contributor.authorKim, Chungho-
dc.contributor.authorLee, Jae-Seon-
dc.contributor.authorKo, Young-Gyu-
dc.date.accessioned2021-09-03T21:12:43Z-
dc.date.available2021-09-03T21:12:43Z-
dc.date.created2021-06-18-
dc.date.issued2016-08-02-
dc.identifier.issn1949-2553-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/87838-
dc.description.abstractWe previously demonstrated that cell-surface gC1qR is a key regulator of lamellipodia formation and cancer metastasis. Here, we screened a monoclonal mouse antibody against gC1qR to prevent cell migration by neutralizing cell-surface gC1qR. The anti-gC1qR antibody prevented growth factor-stimulated lamellipodia formation, cell migration and focal adhesion kinase activation by inactivating receptor tyrosine kinases (RTKs) in various cancer cells such as A549, MDA-MB-231, MCF7 and HeLa cells. The antibody neutralization of cell-surface gC1qR also inhibited angiogenesis because the anti-gC1qR antibody prevented growth factor-stimulated RTK activation, lamellipodia formation, cell migration and tube formation in HUVEC. In addition, we found that A549 tumorigenesis was reduced in a xenograft mouse model by following the administration of the anti-gC1qR antibody. With these data, we can conclude that the antibody neutralization of cell-surface gC1qR could be a good therapeutic strategy for cancer treatment.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherIMPACT JOURNALS LLC-
dc.subjectBINDING PROTEIN-1 HABP1/P32/GC1QR-
dc.subjectGROWTH-FACTOR-BETA-
dc.subjectFUNCTIONAL EXPRESSION-
dc.subjectENDOTHELIAL-CELLS-
dc.subjectGLOBULAR HEADS-
dc.subjectTUMOR-CELLS-
dc.subjectMIGRATION-
dc.subjectRECEPTOR-
dc.subjectCANCER-
dc.subjectINVASION-
dc.titleAntibody neutralization of cell-surface gC1qR/HABP1/SF2-p32 prevents lamellipodia formation and tumorigenesis-
dc.typeArticle-
dc.contributor.affiliatedAuthorKo, Jesang-
dc.contributor.affiliatedAuthorKim, Chungho-
dc.contributor.affiliatedAuthorKo, Young-Gyu-
dc.identifier.doi10.18632/oncotarget.10267-
dc.identifier.scopusid2-s2.0-84981303304-
dc.identifier.wosid000385422000091-
dc.identifier.bibliographicCitationONCOTARGET, v.7, no.31, pp.49972 - 49985-
dc.relation.isPartOfONCOTARGET-
dc.citation.titleONCOTARGET-
dc.citation.volume7-
dc.citation.number31-
dc.citation.startPage49972-
dc.citation.endPage49985-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaOncology-
dc.relation.journalResearchAreaCell Biology-
dc.relation.journalWebOfScienceCategoryOncology-
dc.relation.journalWebOfScienceCategoryCell Biology-
dc.subject.keywordPlusBINDING PROTEIN-1 HABP1/P32/GC1QR-
dc.subject.keywordPlusGROWTH-FACTOR-BETA-
dc.subject.keywordPlusFUNCTIONAL EXPRESSION-
dc.subject.keywordPlusENDOTHELIAL-CELLS-
dc.subject.keywordPlusGLOBULAR HEADS-
dc.subject.keywordPlusTUMOR-CELLS-
dc.subject.keywordPlusMIGRATION-
dc.subject.keywordPlusRECEPTOR-
dc.subject.keywordPlusCANCER-
dc.subject.keywordPlusINVASION-
dc.subject.keywordAuthorgC1qR-
dc.subject.keywordAuthorlamellipodia-
dc.subject.keywordAuthorcell migration-
dc.subject.keywordAuthorantibody-
dc.subject.keywordAuthorcancer-
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