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Stimulation of fibroblasts and neuroblasts on a biomimetic extracellular matrix consisting of tandem repeats of the elastic VGVPG domain and RGD motif

Title
Stimulation of fibroblasts and neuroblasts on a biomimetic extracellular matrix consisting of tandem repeats of the elastic VGVPG domain and RGD motif
Authors
Jeon, WB[Jeon, Won Bae]Park, BH[Park, Bo Hyung]Wei, J[Wei, Junjun]Park, RW[Park, Rang-Woon]
DGIST Authors
Jeon, WB[Jeon, Won Bae]; Park, BH[Park, Bo Hyung]
Issue Date
2011-05
Citation
Journal of Biomedical Materials Research Part A, 97A(2), 152-157
Type
Article
Article Type
Article
Keywords
AdhesionAdhesion-Mediated SpreadingAmino Acid SequenceAnimal Cell CultureAntibodiesArginineArtificial Extracellular MatrixArtificial Extracellular MatrixesAspartic AcidBiocompatibilityBioinformaticsBiomechanicsBiomimetic MaterialBiomimeticsBiosynthesisCell AdhesionCell CultureCell LineCell ProliferationCell StimulationCell StructureCell SurvivalComputer SimulationControlled StudyDNA SynthesisElasticityElastinElastin-Like Protein (ELP)Extracellular MatrixFibroblastFibroblastsFibronectinFibronectin-Integrin SignalingFibronectinsGenesGenetic EngineeringGlycineGlycoproteinsHeat SensitivityHumanHuman CellHumansIntegrinMammalsMatrix AlgebraMechanical PropertiesNeuroblastNeuronsNucleic AcidsOligopeptidesPentapeptideProliferationProtein BindingProtein DomainProtein MotifProtein Structure, TertiaryScleroproteinSignal TransductionSignalingSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem RepeatTemperatureThermally InducedThermally Induced Inverse TransitionTissue
ISSN
1549-3296
Abstract
Elastin-like proteins (ELPs) modeled after tropoelastin are favored in the development of biomimetic matrices due to their biocompatibility and the possibility to precisely control their environmental responsiveness, mechanical properties, and fate within the cells by recombinant DNA technology-mediated design at the gene level. However, a basic prerequisite in the use of ELPs as cell culture matrices is the presence of a biofunctionality that can induce adhesion-mediated signaling pathways. To activate fibronectin-integrin signaling events from a cell-matrix interface and direct cell survival and proliferation, we biosynthesized a modular ELP, represented as TGPG[VGRGD(VGVPG) 6]20WPC, consisting of alternating elastic (VGVPG) 6 structural domains and cell-binding VGRGD motifs that are intended to emulate various aspects of extracellular matrix proteins. The inverse transition curves of [VGRGD(VGVPG)6]20 and (VGVPG) 140 overlapped with each other, indicating that one VGRGD sequence fused with six elastic pentapeptides did not disturb the thermal sensitivity of [VGRGD(VGVPG)6]20. The cell adhesion activity of [VGRGD(VGVPG)6]20 toward HEK293 fibroblasts and N2A neuroblasts was similar to that of native fibronectin. Upon contact with [VGRGD(VGVPG)6]20, the fibroblasts exhibited a flattened polygonal morphology, and the neuroblasts synthesized new DNA and proliferated. On the basis of these physiological changes, we concluded that RGD-functionalized ELP triggers the activation of signaling cascades within cells and can be used as an elastin-like matrix for mammalian cell culture. © 2011 Wiley Periodicals, Inc.
URI
http://hdl.handle.net/20.500.11750/2486
DOI
10.1002/jbm.a.33041
Publisher
Wiley Blackwell
Related Researcher
Files:
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Collection:
ETC1. Journal Articles
Companion Diagnostics and Medical Technology Research Group1. Journal Articles


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