Immobilized Arg-Gly-Asp (RGD) peptides of varying lengths as structural probes of the platelet glycoprotein IIb/IIIa receptor - PubMed (original) (raw)
. 1992 Jan 1;79(1):117-28.
Affiliations
- PMID: 1728303
Free article
Immobilized Arg-Gly-Asp (RGD) peptides of varying lengths as structural probes of the platelet glycoprotein IIb/IIIa receptor
J H Beer et al. Blood. 1992.
Free article
Abstract
The interactions between ligands containing the recognition sequence arginine-glycine-aspartic acid (RGD) and integrin receptors are important in many cell-cell and cell-protein interactions. The platelet contains five integrin receptors and they contribute significantly to platelet adhesion and aggregation. To investigate the RGD binding domains on platelet integrins, we immobilized a series of RGD peptides containing variable numbers of glycine residues [(G)n-RGDF] on polyacrylonitrile beads and evaluated the ability of the beads to interact with platelets. With native platelets, virtually no interaction occurred with G1-RGDF beads, but the interactions increased as the number of glycine residues increased, plateauing with the G9-RGDF and G11-RGDF beads. ADP pretreatment enhanced the interactions with all of the beads, whereas prostaglandin E1 pretreatment eliminated the interactions with the shortest peptide beads, but only partially inhibited interactions with the longer peptide beads. Monoclonal antibodies to glycoprotein (GP) IIb/IIIa were most effective in inhibiting the interactions, but antibodies to GPIIb/IIIa with similar inhibitory effects on fibrinogen binding varied dramatically in their ability to inhibit the interaction between platelets and immobilized RGD peptides. Our data indicate that the majority of RGD binding sites on GPIIb/IIIa can be reached by peptides that extend out approximately 11 to 32 A from the surface of the bead, and these results are in accord with the dimensions of integrin receptors deduced from electron microscopy. Activation of GPIIb/IIIa facilitates the interactions, but platelet inhibition fails to eliminate the interactions with the longer peptide beads, suggesting that access to the RGD binding site on at least a fraction of the GPIIb/IIIa receptors is always possible for preferred ligands. Finally, we found that the G3-RGDF peptide beads were uniquely sensitive to the activation state of the GPIIb/IIIa receptor.
Similar articles
- The Arg-Gly-Asp (RGD) recognition site of platelet glycoprotein IIb-IIIa on nonactivated platelets is accessible to high-affinity macromolecules.
Tomiyama Y, Tsubakio T, Piotrowicz RS, Kurata Y, Loftus JC, Kunicki TJ. Tomiyama Y, et al. Blood. 1992 May 1;79(9):2303-12. Blood. 1992. PMID: 1373972 - Inhibition of integrin-mediated platelet aggregation, fibrinogen-binding, and interactions with extracellular matrix by nonpeptidic mimetics of Arg-Gly-Asp.
Varon D, Lider O, Dardik R, Shenkman B, Alon R, Hershkoviz R, Kapustina G, Savion N, Martinowitz U, Greenspoon N. Varon D, et al. Thromb Haemost. 1993 Dec 20;70(6):1030-6. Thromb Haemost. 1993. PMID: 8165596 - On the structure and function of platelet integrin alpha IIb beta 3, the fibrinogen receptor.
Calvete JJ. Calvete JJ. Proc Soc Exp Biol Med. 1995 Apr;208(4):346-60. doi: 10.3181/00379727-208-43863a. Proc Soc Exp Biol Med. 1995. PMID: 7535429 Review.
Cited by
- Determinants of cell-material crosstalk at the interface: towards engineering of cell instructive materials.
Ventre M, Causa F, Netti PA. Ventre M, et al. J R Soc Interface. 2012 Sep 7;9(74):2017-32. doi: 10.1098/rsif.2012.0308. Epub 2012 Jun 29. J R Soc Interface. 2012. PMID: 22753785 Free PMC article. Review. - Neural cell type-specific responses to glycomimetic functionalized collagen.
Masand SN, Perron IJ, Schachner M, Shreiber DI. Masand SN, et al. Biomaterials. 2012 Jan;33(3):790-7. doi: 10.1016/j.biomaterials.2011.10.013. Epub 2011 Oct 24. Biomaterials. 2012. PMID: 22027596 Free PMC article. - Hydrogels with well-defined peptide-hydrogel spacing and concentration: impact on epithelial cell behavior().
Wilson MJ, Liliensiek SJ, Murphy CJ, Murphy WL, Nealey PF. Wilson MJ, et al. Soft Matter. 2012;8(2):390-398. doi: 10.1039/C1SM06589K. Epub 2011 Oct 26. Soft Matter. 2012. PMID: 23264803 Free PMC article. - Abciximab pharmacodynamics are unaffected by antecedent therapy with other GPIIb/IIIa antagonists in non-human primates.
Nakada MT, Sassoli PM, Tam SH, Nedelman MA, Jordan RE, Kereiakes DJ. Nakada MT, et al. J Thromb Thrombolysis. 2002 Aug;14(1):15-24. doi: 10.1023/a:1022058103581. J Thromb Thrombolysis. 2002. PMID: 12652146 - Integrin beta3 regions controlling binding of murine mAb 7E3: implications for the mechanism of integrin alphaIIbbeta3 activation.
Artoni A, Li J, Mitchell B, Ruan J, Takagi J, Springer TA, French DL, Coller BS. Artoni A, et al. Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13114-20. doi: 10.1073/pnas.0404201101. Epub 2004 Jul 26. Proc Natl Acad Sci U S A. 2004. PMID: 15277669 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources