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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
- Stimulation of fibroblasts and neuroblasts on a biomimetic extracellular matrix consisting of tandem repeats of the elastic VGVPG domain and RGD motif
- 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
- Journal of Biomedical Materials Research Part A, 97A(2), 152-157
- Article Type
- Adhesion; Adhesion-Mediated Spreading; Amino Acid Sequence; Animal Cell Culture; Antibodies; Arginine; Artificial Extracellular Matrix; Artificial Extracellular Matrixes; Aspartic Acid; Biocompatibility; Bioinformatics; Biomechanics; Biomimetic Material; Biomimetics; Biosynthesis; Cell Adhesion; Cell Culture; Cell Line; Cell Proliferation; Cell Stimulation; Cell Structure; Cell Survival; Computer Simulation; Controlled Study; DNA Synthesis; Elasticity; Elastin; Elastin-Like Protein (ELP); Extracellular Matrix; Fibroblast; Fibroblasts; Fibronectin; Fibronectin-Integrin Signaling; Fibronectins; Genes; Genetic Engineering; Glycine; Glycoproteins; Heat Sensitivity; Human; Human Cell; Humans; Integrin; Mammals; Matrix Algebra; Mechanical Properties; Neuroblast; Neurons; Nucleic Acids; Oligopeptides; Pentapeptide; Proliferation; Protein Binding; Protein Domain; Protein Motif; Protein Structure, Tertiary; Scleroprotein; Signal Transduction; Signaling; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tandem Repeat; Temperature; Thermally Induced; Thermally Induced Inverse Transition; Tissue
- 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.
- Wiley Blackwell
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- Companion Diagnostics and Medical Technology Research Group1. Journal Articles
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