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Human apolipoprotein(a) kringle V inhibits angiogenesis in vitro and in vivo by interfering with the activation of focal adhesion kinases

DC FieldValueLanguage
dc.contributor.author홍순원-
dc.date.accessioned2020-09-04T02:06:07Z-
dc.date.available2020-09-04T02:06:07Z-
dc.date.issued2004-01-
dc.identifier.issn0006-291X-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/178805-
dc.description.abstractApolipoprotein(a) [apo(a)] contains the largest numbers of kringle domains identified to date. Of these, apo(a) kringle V shows significant sequence homology with plasminogen kringle 5, which is reported to be a potent angiogenesis inhibitor. To determine the effects of apo(a) kringle V on angiogenesis, it was expressed as a soluble protein (termed rhLK8) in Pichia pastoris and its in vitro and in vivo anti-angiogenic properties were examined. rhLK8 inhibited the migration of human umbilical vein endothelial cells in vitro in a dose-dependent manner. This function was associated with the down-regulation of the activation of focal adhesion kinase and the inhibition of the consequent formation of actin stress fibers/focal adhesions. rhLK8 also inhibited new capillary formation in vivo, as assessed by the chick chorioallantoic membrane assay and the Matrigel plug assay. These results indicate that rhLK8 may be an effective angiogenesis inhibitor both in vitro and in vivo.-
dc.description.statementOfResponsibilityrestriction-
dc.languageEnglish-
dc.publisherElsevier-
dc.relation.isPartOfBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.subject.MESHActins / metabolism-
dc.subject.MESHAmino Acid Sequence-
dc.subject.MESHAnimals-
dc.subject.MESHApolipoproteins / chemistry*-
dc.subject.MESHApoprotein(a)-
dc.subject.MESHBlotting, Western-
dc.subject.MESHCell Movement-
dc.subject.MESHCells, Cultured-
dc.subject.MESHChick Embryo-
dc.subject.MESHChorion / metabolism-
dc.subject.MESHCollagen / pharmacology-
dc.subject.MESHDNA, Complementary / metabolism-
dc.subject.MESHDose-Response Relationship, Drug-
dc.subject.MESHDrug Combinations-
dc.subject.MESHElectrophoresis, Polyacrylamide Gel-
dc.subject.MESHEndothelium, Vascular / cytology-
dc.subject.MESHEndothelium, Vascular / pathology-
dc.subject.MESHFocal Adhesion Kinase 1-
dc.subject.MESHFocal Adhesion Protein-Tyrosine Kinases-
dc.subject.MESHGenetic Vectors-
dc.subject.MESHHumans-
dc.subject.MESHKringles-
dc.subject.MESHLaminin / pharmacology-
dc.subject.MESHLipoprotein(a) / chemistry*-
dc.subject.MESHMitogen-Activated Protein Kinase 1 / metabolism-
dc.subject.MESHMitogen-Activated Protein Kinase 3-
dc.subject.MESHMitogen-Activated Protein Kinases / metabolism-
dc.subject.MESHMolecular Sequence Data-
dc.subject.MESHNeovascularization, Pathologic-
dc.subject.MESHPhosphorylation-
dc.subject.MESHProtein Structure, Tertiary-
dc.subject.MESHProtein-Tyrosine Kinases / chemistry*-
dc.subject.MESHProtein-Tyrosine Kinases / metabolism-
dc.subject.MESHProteoglycans / pharmacology-
dc.subject.MESHRecombinant Proteins / metabolism-
dc.subject.MESHTime Factors-
dc.subject.MESHTyrosine / metabolism-
dc.subject.MESHUmbilical Veins / cytology-
dc.subject.MESHWound Healing-
dc.titleHuman apolipoprotein(a) kringle V inhibits angiogenesis in vitro and in vivo by interfering with the activation of focal adhesion kinases-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Pathology (병리학교실)-
dc.contributor.googleauthorJang-Seong Kim-
dc.contributor.googleauthorHyun-Kyung Yu-
dc.contributor.googleauthorJin-Hyung Ahn-
dc.contributor.googleauthorHo-Jeong Lee-
dc.contributor.googleauthorSoon-Won Hong-
dc.contributor.googleauthorKyung-Hwan Jung-
dc.contributor.googleauthorSoo-Ik Chang-
dc.contributor.googleauthorYong-Kil Hong-
dc.contributor.googleauthorYoung-Ae Joe-
dc.contributor.googleauthorSi-Myung Byun-
dc.contributor.googleauthorSuk-Keun Lee-
dc.contributor.googleauthorSoo-Il Chung-
dc.contributor.googleauthorYeup Yoon-
dc.identifier.doi10.1016/j.bbrc.2003.11.148-
dc.contributor.localIdA04411-
dc.relation.journalcodeJ00281-
dc.identifier.eissn1090-2104-
dc.identifier.pmid14697222-
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S0006291X03025488-
dc.contributor.alternativeNameHong, Soon Won-
dc.contributor.affiliatedAuthor홍순원-
dc.citation.volume313-
dc.citation.number3-
dc.citation.startPage534-
dc.citation.endPage540-
dc.identifier.bibliographicCitationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol.313(3) : 534-540, 2004-01-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Pathology (병리학교실) > 1. Journal Papers

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