, we have developed cell lines that lack an endogenous FN matrix but will form fibrils when provided with exogenous FN. Recombinant FNs (recFN) containing deletions of either the RGD cell-binding sequence (RGD-) or the first type III repeats (FNAIIII_7) including the IIIx FN binding site were generated

enrichment in gene bodies and depletion in protein binding sites and enhancers. Non-CG methylation disappeared upon induced differentiation of the embryonic stem cells, and was restored in induced pluripotent stem cells. We identified hundreds of differentially methylated regions proximal to genes involved

can be modulated through choice of cell-binding domain, and (ii) recommend the RGD sequence for applications that require rapid endothelial cell spreading and matrix adhesion.

the upstream region of genes in the same expression pattern group and look for sequence motifs. These motifs might be the regulatory signal (most likely a transcriptional protein binding site) that causes these genes to respond similarly to 2 developmental or environmental changes. Information on expressions

The completion of the Arabidopsis thaliana genome sequence allows a com-parative analysis of transcriptional regulators across the three eukaryotic king-doms. Arabidopsis dedicates over 5 % of its genome to code for more than 1500 transcription factors, about 45 % of which are from families speciÞc

PURPOSE. Fibronectin plays an important role in the migration of corneal epithelial cells in vivo. The Arg-Gly-Asp (RGD) sequence in the principal cell binding domain of fibronectin mediates the interaction of fibronectin with integrins, whereas the Pro-His-Ser-Arg-Asn (PHSRN) sequence

Abstract. Site-directed mutagenesis studies have suggested that additional peptide information in the central cell-binding domain of fibronectin besides the minimal Arg-Gly-Asp (RGD) sequence is required for its full adhesive activity. The nature of this second, synergistic site was analyzed

corresponding to a portion of the same hypervariable region but not containing the RGD sequence did not inhibit virus attachment under the same conditions. Antibody against the RGD region of VPI blocked attachment of the virus to BHK cells, and neutralizing monoclonal antibodies, which neutralize virus

repeats and fibronectin cell-binding domains. aECM-RGD contains the RGD sequence from fibronectin, and aECM-RDG contains a scrambled cell-binding domain. Covalent attachment of poly(ethylene glycol) (PEG) to protein substrates reduced nonspecific cell adhesion to aECM-RDG-PEG but did not preclude sequence

, but not on polylysine or on uncoated plastic. Integrin mediation of this effect was suggested by finding the same pattern of elevated tyrosine phosphorylation in cells plated on the cell-binding fragment of fibronectin and in ceils plated on a synthetic polymer containing multiple RGD sequences. We have identified one