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dc.contributor.authorKang, Hye-Won
dc.contributor.authorWalvick, Ronn P.
dc.contributor.authorBogdanov, Alexei A. Jr.
dc.date2022-08-11T08:10:50.000
dc.date.accessioned2022-08-23T17:21:45Z
dc.date.available2022-08-23T17:21:45Z
dc.date.issued2009-12-01
dc.date.submitted2015-01-05
dc.identifier.citationFASEB J. 2009 Dec;23(12):4126-34. doi: 10.1096/fj.08-127795. Epub 2009 Aug 19. <a href="http://dx.doi.org/10.1096/fj.08-127795">Link to article on publisher's site</a>
dc.identifier.issn0892-6638 (Linking)
dc.identifier.doi10.1096/fj.08-127795
dc.identifier.pmid19692649
dc.identifier.urihttp://hdl.handle.net/20.500.14038/48595
dc.description.abstractNoggin protein is a potent bone morphogenetic protein (BMP) antagonist capable of inhibiting vasculogenesis even in the presence of provasculogenic VEGF and FGF-2. We found that human umbilical vein endothelial cells (HUVECs) do not express Noggin in culture and used these cells for modeling of antivasculogenesis. We hypothesized that high-efficiency transduction of HUVECs with bicistronic lentiviral vector encoding Noggin and enhanced green fluorescent protein (EGFP) enables direct visualization of Noggin effects in homogenous primary cell populations in vitro and in vivo. By comparing HUVECs transduced with a control GFP and GFP/Noggin expression cassettes, we showed that constitutive and orthotopic Noggin protein expression did not influence cell proliferation, down-regulated BMP-2 expression, and showed no effect on BMP receptor transcripts. We demonstrated that in contrast to GFP-only control, Noggin expression in endothelial cells abrogated endothelial migration in response to monolayer injury, blocked endothelial transmigration, and caused abrogation of cord formation in vitro. Adding exogenous BMP-4 restored the formation of cords. Imaging experiments in vivo investigated vessel formation in Matrigel implants in athymic mice by utilizing GFP imaging or magnetic resonance imaging of perfusion in the implants. Both approaches demonstrated the lack of functional vessel formation after the adoptive transfer of GFP/Noggin-expressing human endothelial cells in mice.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=19692649&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2812039/
dc.subjectAnimals
dc.subjectBone Morphogenetic Protein 2
dc.subjectBone Morphogenetic Protein 4
dc.subjectBone Morphogenetic Protein Receptors
dc.subjectCarrier Proteins
dc.subjectCell Movement
dc.subjectCell Proliferation
dc.subjectCells, Cultured
dc.subjectEndothelial Cells
dc.subjectHumans
dc.subjectMice
dc.subjectNeovascularization, Physiologic
dc.subjectUmbilical Veins
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectCell Biology
dc.subjectCells
dc.subjectInvestigative Techniques
dc.subjectRadiology
dc.titleIn vitro and In vivo imaging of antivasculogenesis induced by Noggin protein expression in human venous endothelial cells
dc.typeJournal Article
dc.source.journaltitleFASEB journal : official publication of the Federation of American Societies for Experimental Biology
dc.source.volume23
dc.source.issue12
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/radiology_pubs/82
dc.identifier.contextkey6497736
html.description.abstract<p>Noggin protein is a potent bone morphogenetic protein (BMP) antagonist capable of inhibiting vasculogenesis even in the presence of provasculogenic VEGF and FGF-2. We found that human umbilical vein endothelial cells (HUVECs) do not express Noggin in culture and used these cells for modeling of antivasculogenesis. We hypothesized that high-efficiency transduction of HUVECs with bicistronic lentiviral vector encoding Noggin and enhanced green fluorescent protein (EGFP) enables direct visualization of Noggin effects in homogenous primary cell populations in vitro and in vivo. By comparing HUVECs transduced with a control GFP and GFP/Noggin expression cassettes, we showed that constitutive and orthotopic Noggin protein expression did not influence cell proliferation, down-regulated BMP-2 expression, and showed no effect on BMP receptor transcripts. We demonstrated that in contrast to GFP-only control, Noggin expression in endothelial cells abrogated endothelial migration in response to monolayer injury, blocked endothelial transmigration, and caused abrogation of cord formation in vitro. Adding exogenous BMP-4 restored the formation of cords. Imaging experiments in vivo investigated vessel formation in Matrigel implants in athymic mice by utilizing GFP imaging or magnetic resonance imaging of perfusion in the implants. Both approaches demonstrated the lack of functional vessel formation after the adoptive transfer of GFP/Noggin-expressing human endothelial cells in mice.</p>
dc.identifier.submissionpathradiology_pubs/82
dc.contributor.departmentDepartment of Radiology
dc.source.pages4126-34


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