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Cathepsin L derived from skeletal muscle cells transfected with bFGF promotes endothelial cell migration

DC Field Value Language
dc.contributor.author김수혁-
dc.contributor.author이경혜-
dc.contributor.author임은경-
dc.contributor.author장양수-
dc.contributor.author정지형-
dc.contributor.author진태원-
dc.contributor.author최은영-
dc.date.accessioned2014-12-20T16:44:21Z-
dc.date.available2014-12-20T16:44:21Z-
dc.date.issued2011-
dc.identifier.issn1226-3613-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/93285-
dc.description.abstractGene transfer of basic fibroblast growth factor (bFGF) has been shown to induce significant endothelial migration and angiogenesis in ischemic disease models. Here, we investigate what factors are secreted from skeletal muscle cells (SkMCs) transfected with bFGF gene and whether they participate in endothelial cell migration. We constructed replication-defective adenovirus vectors containing the human bFGF gene (Ad/bFGF) or a control LacZ gene (Ad/LacZ) and obtained conditioned media, bFGF-CM and LacZ-CM, from SkMCs infected by Ad/bFGF or Ad/LacZ, respectively. Cell migration significantly increased in HUVECs incubated with bFGF-CM compared to cells incubated with LacZ-CM. Interestingly, HUVEC migration in response to bFGF-CM was only partially blocked by the addition of bFGF-neutralizing antibody, suggesting that bFGF-CM contains other factors that stimulate endothelial cell migration. Several proteins, matrix metalloproteinase-1 (MMP-1), plasminogen activator inhibitor-1 (PAI-1), and cathepsin L, increased in bFGF-CM compared to LacZ-CM; based on 1-dimensional gel electrophoresis and mass spectrometry. Their increased mRNA and protein levels were confirmed by RT-PCR and immunoblot analysis. The recombinant human bFGF protein induced MMP-1, PAI-1, and cathepsin L expression in SkMCs. Endothelial cell migration was reduced in groups treated with bFGF-CM containing neutralizing antibodies against MMP-1 or PAI-1. In particular, HUVECs treated with bFGF-CM containing cell-impermeable cathepsin L inhibitor showed the most significant decrease in cell migration. Cathepsin L protein directly promotes endothelial cell migration through the JNK pathway. These results indicate that cathepsin L released from SkMCs transfected with the bFGF gene can promote endothelial cell migration.-
dc.description.statementOfResponsibilityopen-
dc.format.extent179~188-
dc.relation.isPartOfEXPERIMENTAL AND MOLECULAR MEDICINE-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHAntibodies, Neutralizing/immunology-
dc.subject.MESHCathepsin L/genetics-
dc.subject.MESHCathepsin L/metabolism*-
dc.subject.MESHCell Movement*-
dc.subject.MESHCells, Cultured-
dc.subject.MESHComet Assay-
dc.subject.MESHDependovirus/genetics-
dc.subject.MESHEndothelial Cells/cytology-
dc.subject.MESHEndothelial Cells/metabolism*-
dc.subject.MESHFibroblast Growth Factor 2/genetics-
dc.subject.MESHFibroblast Growth Factor 2/immunology-
dc.subject.MESHFibroblast Growth Factor 2/metabolism*-
dc.subject.MESHGene Transfer Techniques-
dc.subject.MESHHumans-
dc.subject.MESHImmunoblotting-
dc.subject.MESHJNK Mitogen-Activated Protein Kinases-
dc.subject.MESHLac Operon/genetics-
dc.subject.MESHMass Spectrometry-
dc.subject.MESHMatrix Metalloproteinase 1/biosynthesis-
dc.subject.MESHMatrix Metalloproteinase 1/genetics-
dc.subject.MESHMuscle, Skeletal/metabolism*-
dc.subject.MESHNeovascularization, Physiologic-
dc.subject.MESHPlasminogen Activator Inhibitor 1/biosynthesis-
dc.subject.MESHPlasminogen Activator Inhibitor 1/genetics-
dc.subject.MESHRNA, Messenger/biosynthesis-
dc.subject.MESHReverse Transcriptase Polymerase Chain Reaction-
dc.titleCathepsin L derived from skeletal muscle cells transfected with bFGF promotes endothelial cell migration-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentYonsei Biomedical Research Center (연세의생명연구원)-
dc.contributor.googleauthorJi Hyung Chun-
dc.contributor.googleauthorEun Kyoung Im-
dc.contributor.googleauthorTaewon Jin-
dc.contributor.googleauthorSeung-Min Lee-
dc.contributor.googleauthorSoo Hyuk Kim-
dc.contributor.googleauthorEun Young Choi-
dc.contributor.googleauthorMin-Jeong Shin-
dc.contributor.googleauthorKyung Hye Lee-
dc.contributor.googleauthorYangsoo Jang-
dc.identifier.doi10.3858/emm.2011.43.4.022-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA00640-
dc.contributor.localIdA02658-
dc.contributor.localIdA03390-
dc.contributor.localIdA03448-
dc.contributor.localIdA03739-
dc.contributor.localIdA03990-
dc.contributor.localIdA04154-
dc.relation.journalcodeJ00860-
dc.identifier.eissn2092-6413-
dc.identifier.pmid21350328-
dc.contributor.alternativeNameKim, Soo Hyuk-
dc.contributor.alternativeNameLee, Kyung Hye-
dc.contributor.alternativeNameIm, Eun Kyoung-
dc.contributor.alternativeNameJang, Yang Soo-
dc.contributor.alternativeNameChung, Ji Hyung-
dc.contributor.alternativeNameJin, Tae Won-
dc.contributor.alternativeNameChoi, Eun Young-
dc.contributor.affiliatedAuthorKim, Soo Hyuk-
dc.contributor.affiliatedAuthorLee, Kyung Hye-
dc.contributor.affiliatedAuthorIm, Eun Kyoung-
dc.contributor.affiliatedAuthorJang, Yang Soo-
dc.contributor.affiliatedAuthorChung, Ji Hyung-
dc.contributor.affiliatedAuthorJin, Tae Won-
dc.contributor.affiliatedAuthorChoi, Eun Young-
dc.rights.accessRightsfree-
dc.citation.volume43-
dc.citation.number4-
dc.citation.startPage179-
dc.citation.endPage188-
dc.identifier.bibliographicCitationEXPERIMENTAL AND MOLECULAR MEDICINE, Vol.43(4) : 179-188, 2011-
dc.identifier.rimsid27111-
dc.type.rimsART-
Appears in Collections:
1. College of Medicine (의과대학) > Research Institute (부설연구소) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Internal Medicine (내과학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > Yonsei Biomedical Research Center (연세의생명연구원) > 1. Journal Papers

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