Disease relevance of Arginyl-glycyl-aspartyl-serine

• Fibronectin tetrapeptide is target for syphilis spirochete cytadherence [1].
• Previous studies have indicated that the experimental metastasis of murine melanoma cells can be inhibited by ex vivo pretreatment of cells with purified adhesion-promoting fragments of laminin or the synthetic peptide arginyl-glycyl-aspartyl-serine (RGDS) prior to tail vein injection [2].
• Platelet binding to the small cell lung cancer cells was not inhibited with anti-GP IIb-IIIa antibody or Arg-Gly-Asp-Ser peptide [3].
• A similar inhibition of aggregation to 4N1-1 was obtained in the presence of Arg-Gly-Asp-Ser in mouse platelets deficient in FcR gamma chain or SLP-76 and in patients with type I Glanzmann thrombasthenia [4].
• The peptide Arg-Gly-Asp-Ser, which binds to integrin receptors, inhibited the uptake of apoptotic cells and the subsequent enhancement of HIV-1 replication [5].

High impact information on Arginyl-glycyl-aspartyl-serine

• The data support the notion that the sequence Arg-Gly-Asp-Ser of cell surface fibronectin acts as a recognition site for attachment of the parasites [6].
• Fibronectin receptor of human macrophages recognizes the sequence Arg-Gly-Asp-Ser [7].
• The active site of the Fn molecule has been identified as a four-amino acid sequence, arg-gly-asp-ser (RGDS), located on each monomer of the cell-binding domain [1].
• The activation of C3 receptors by Fn was mediated by a receptor that recognizes a sequence, Arg-Gly-Asp-Ser (RGDS), present in the cell-binding domain of Fn [7].
• Binding was inhibited by the tetrapeptide Arg-Gly-Asp-Ser and by monoclonal and polyclonal antibodies to GPIIb/IIIa [8].

Chemical compound and disease context of Arginyl-glycyl-aspartyl-serine

• This fragment promotes melanoma adhesion and spreading in an arginyl-glycyl-aspartyl-serine (RGDS) independent manner, suggesting that cell adhesion to this region of fibronectin is independent of the typical RGD/integrin-mediated binding [9].
• Heparin, the D3 peptide, or Arg-Gly-Asp-Ser (RGDS) containing peptides did not inhibit binding of fibronectin to the hemagglutinin, indicating that the binding site is different from that of Staphylococcus aureus or Treponema pallidum [10].

Biological context of Arginyl-glycyl-aspartyl-serine

• Fibronectin is thought to participate in the attachment, and in this study the region of fibronectin that interacts with the surface receptors of T. cruzi trypomastigotes was investigated by testing the binding of the amino acid sequence Arg-Gly-Asp-Ser, corresponding to the cell attachment site of fibronectin to T. cruzi trypomastigotes [6].
• By comparison, the tetrapeptide Arg-Gly-Asp-Ser (RGDS) inhibited resorption by rat or chicken osteoclasts with an IC50 of 0.1 mM while ala24-echistatin was inactive [11].
• (i) Two peptides that inhibit the binding of fibrinogen and other ligands to gpIIb-IIIa, Arg-Gly-Asp-Ser and His-His-Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val, also inhibited the thrombin-induced tyrosine phosphorylation of this subset of proteins [12].
• Arg-Gly-Asp-Ser-selective adhesion and the stabilization of long-term potentiation: pharmacological studies and the characterization of a candidate matrix receptor [13].
• In addition, Arg-Gly-Asp-Ser-containing peptides inhibited the rate and extent of thrombin-induced platelet aggregation [14].

Anatomical context of Arginyl-glycyl-aspartyl-serine

• A synthetic peptide containing the Arg-Gly-Asp-Ser (RGDS) sequence also inhibited monocyte adherence to fibronectin. cDNA hybridization experiments revealed the presence of mRNA for both the alpha and beta subunits of the fibroblast fibronectin receptor in human monocytes [15].
• The cytoadhesive tetrapeptide portion of fibronectin, Arg-Gly-Asp-Ser (250-1,000 micrograms/ml), released 1.94 +/- 0.10 micrograms/ml of elastase from 10(7) neutrophils, in contrast to the lack of release by the control hexapeptide, Arg-Gly-Tyr-Ser-Leu-Gly [16].
• Aortic endothelial cell adhesion to type IV collagen was not inhibited by high levels (10(-3) M) of arginyl-glycyl-aspartyl-serine [17].
• Neurite outgrowth was also maximal on f110, and half of these neurites were also resistant to soluble RGDS peptide [18].
• The fibronectin cell attachment sequence Arg-Gly-Asp-Ser promotes focal contact formation during early fibroblast attachment and spreading [19].

Associations of Arginyl-glycyl-aspartyl-serine with other chemical compounds

• Neither control antibodies nor heparin, fibronectin, fibrinogen, nor the fibronectin adhesion tetrapeptide Arg-Gly-Asp-Ser inhibited rosetting [20].
• Cell adhesion to fibronectin can be mediated by the interaction of an integrin (alpha 5 beta 1) with the Arg-Gly-Asp-Ser (RGDS)-containing cell adhesion region of fibronectin [21].
• We compared the effect of RGDS (Arg-Gly-Asp-Ser) and four disintegrins (echistatin, flavoridin, albolabrin, and bitistatin) on platelet behavior in a membrane oxygenator [22].
• FN bound appreciably to this column and was eluted much more efficiently by a solution of Arg-Gly-Asp-Ser-containing peptide than by a solution of related but inactive Arg-Gly-Glu-Ser-containing peptide [23].
• 125I-fibrinogen was not recovered with platelet cytoskeletons if binding was inhibited by the RGDS peptide, excess unlabeled fibrinogen, or disruption of the glycoprotein (GP) IIb-IIIa complex by EDTA-treatment [24].

Gene context of Arginyl-glycyl-aspartyl-serine

• In contrast, neither RGDS peptide nor MoAb 7E3, both known to block alphaIIbbeta3 engagement, had any effect on SIPA and pp125FAK [25].
• Both the vitronectin-induced MMP-2 production and vitronectin-enhanced invasion were blocked by the peptide ligand Arg-Gly-Asp-Ser (RGDS) [26].
• Neither control monoclonal antibodies nor the cell attachment peptide Arg-Gly-Asp-Ser inhibited tumor cell attachment to TSP, alone or in the presence of heparin [27].
• In HEK-293 human embryonic kidney cells, LPA and thrombin receptor-mediated Erk 1/2 activation is partially sensitive to both the RGDS peptide and tyrphostin AG1478, suggesting that both focal adhesion and receptor tyrosine kinase scaffolds are employed in these cells [28].
• We compared the effect of a synthetic dodecapeptide of residues 400-411 of the gamma chain of fibrinogen (gamma Fg 400-411) and of three synthetic peptides (15 to 18 aminoacids), of human von Willebrand Factor (vWF), containing the 1744-1747 Arg-Gly-Asp-Ser (RGDS) sequence, upon platelet adhesion to collagen in flowing blood [29].

Analytical, diagnostic and therapeutic context of Arginyl-glycyl-aspartyl-serine

• The sequence recognized by L2B does not resemble known GPllb-llla binding site peptide sequences [Arg-Gly-Asp-Ser (RGDS) or gamma 50 400-411] as determined by competitive inhibition ELISA comparing these binding site synthetic peptides with gamma 57.5 408-416 [30].
• Selective inactivation of the Arg-Gly-Asp-Ser (RGDS) binding site in von Willebrand factor by site-directed mutagenesis [31].
• Indirect immunofluorescence study demonstrates that Xyk is exclusively localized to the cortex of Xenopus eggs, indicating that Xyk can function in close proximity to the sperm-egg or RGDS peptide-egg interaction site [32].
• Activation of human neutrophils by Arg-Gly-Asp-Ser immobilized on microspheres [33].
• Immunoblotting using polyclonal antibodies (pAb) raised against an FR-1 receptor (FR-1R), a 57 kDa Arg-Gly-Asp-Ser (RGDS)-binding protein, of the sand dollar Clypeaster japonicus showed that the pAb monospecifically bound to the protein [34].

References