The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

Gdrgdsp     (2S)-1-[(2R)-2-[[(2S)-2-[2- [[(2S)-2-(2...

Synonyms: Grgdsp, AR-1J1309, AC1L3GZ2, AC1Q5R4D, Gly-arg-gly-asp-ser-pro, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of Grgdsp

  • A 140 kd protein was bound by the affinity matrix from octylglucoside extracts of MG-63 human osteosarcoma cells and specifically eluted with the synthetic peptide Gly-Arg-Gly-Asp-Ser-Pro [1].
  • In a dose-dependent manner, the GRGDSP hexapeptide appeared to inhibit the adhesion of the E. coli JM109[pmrkABCD(V3)F] to HCT-8, an ileocecal epithelial cell line [2].
  • The purified GST-Rho coated on culture plates facilitated the attachment of human hepatoma cells, which was inhibitable by co-incubation with a synthetic hexapeptide GRGDSP but not with a related peptide of GRGESP, suggesting that the E. coli-expressed Rho-fusion protein was properly folded and biologically functional [3].
  • As a synthetic RGD-containing peptide GRGDSP blocked the spreading of glioma cells on fibrin monomer concentration-dependently, the spreading was thought to be mediated by their cell surface receptors [4].
 

High impact information on Grgdsp

  • Antibodies, as well as GRGDSP, abolished adhesion of N1 and N7 clones to FN and VN, revealing a similar implication of integrins in the adhesion of these clones to the ECM proteins [5].
  • The synthetic peptide, Gly-Arg-Gly-Asp-Ser-Pro, that contains the Arg-Gly-Asp (RGD) integrin recognition site, reversibly inhibited entactin-mediated blastocyst outgrowth in a dose-dependent manner, but had no effect on laminin-mediated outgrowth [6].
  • Cell adhesion mediated by this fragment was completely inhibited by the synthetic peptide GRGDSP [7].
  • To further investigate this, we made use of GRGDSP, a peptide which inhibits binding of integrins to vitronectin and fibronectin [8].
  • Furthermore, adhesion was partially inhibited by a synthetic peptide containing the perlecan domain III sequence LPASFRGDKVTSY (c-RGD) as well as by GRGDSP, but not by GRGESP [9].
 

Chemical compound and disease context of Grgdsp

 

Biological context of Grgdsp

  • Both receptor complexes bound to and were specifically eluted from a column containing the cell adhesion peptide GRGDSP [11].
  • Preincubation of intact platelets with 7E3, a monoclonal antibody that blocks the fibrinogen binding site, or GRGDSP peptide inhibited FXIIIa binding by about 95% when measured by flow cytometry; FXIIIa binding to purified GPIIb-IIIa was also inhibited by 7E3 [12].
  • A synthetic peptide (GRGDSP) and monoclonal anti-GPIIb-IIIa antibody (2G12) that block platelet aggregation also blocked aggregation of these cells [13].
  • The inhibitory effect of tenascin on monocyte or PMN chemotaxis through these matrices was reversed by Abs directed against alpha5beta1 integrins or by a peptide (GRGDSP) that binds to beta1 integrins [14].
  • Soluble fibronectin (IC50 = 0.2 microM) or Gly-Arg-Gly-Asp-Ser-Pro, but not laminin, competitively inhibited fibronectin binding activity [15].
 

Anatomical context of Grgdsp

  • Treatment of XTC fibroblasts with the phorbol ester 12-o-tetradecanoylphorbol-13-acetate reduced cell spreading and accelerated cell rounding in response to GRGDSP, which is essentially opposite to the effect exerted by non-hydrolyzable GTP analogs [8].
  • The effect of SPARC on endothelial cells appeared to be independent of the rounding phenomenon produced by the peptide GRGDSP [16].
  • Cultured oligodendrocytes did not become sensitive to inhibition of sulfolipid synthesis by GRGDSP until a period immediately preceding the peak in sulfolipid biosynthesis [17].
  • The morphological characteristics of individual cells cultured with 0.1 mg/ml GRGDSP were similar to untreated cultures; small rounded cell bodies radiating numerous fine processes [17].
  • Trophoblast attachment and limited outgrowth also could be obtained on dishes to which the hexapeptide Gly-Arg-Gly-Asp-Ser-Pro was coupled [18].
 

Associations of Grgdsp with other chemical compounds

 

Gene context of Grgdsp

  • SAA-induced adhesion was inhibited by antibodies against the integrin receptor alphaIIbbeta3, by the peptide GRGDSP and by SAA-derived peptide containing YIGSR-like and RGD-like adhesion motifs (amino acids 29 to 42) [23].
  • Furthermore, alpha 8 beta 1 binds to both fibronectin- and vitronectin-Sepharose and can be specifically eluted from either matrix protein by the arginine-glycine-aspartic acid (RGD)-containing peptide, GRGDSP [24].
  • Infusion of the integrin-antagonizing hexapeptide GRGDSP or the Src inhibitor PP-2 prevented activation of Src and p38(MAPK) and, consequently, proteolysis inhibition by insulin [25].
  • METHODS: Chondrocytes extracted from macroscopically and microscopically normal and OA cartilage were mechanically stimulated in the presence or absence of GRGDSP or GRADSP oligopeptides, neutralizing interleukin-4 (IL-4) antibodies, gadolinium, or apamin [22].
  • The platelet fibrinogen receptor alpha(IIb)beta(3) (platelet GPIIb-IIIa) in a high affinity state following GRGDSP peptide activation was identified for the first time as the receptor for RBC ICAM-4 [26].
 

Analytical, diagnostic and therapeutic context of Grgdsp

  • In contrast, GRGDSP, a peptide that interacts better with alphavbeta3, was unable to induce sustained constrictions [27].
  • Affinity chromatography of octylglucoside extracts of 125I surface-labeled cells on GRGDSPK-Sepharose columns resulted in the specific binding and elution with GRGDSP of three radiolabeled polypeptides with relative molecular masses of 135, 115, and 90 kD when analyzed by SDS-PAGE under nonreducing conditions [28].
  • In vitro immunohistochemistry indicated that the binding of exogenous FN to the PMC surface was inhibited by the peptides RGDSPASSKP and PASS, but not by RGDS, GRGDSP, PA, or PAS [29].
  • GRGDSP may also suppress the myocyte hypertrophic response in the co-culture [30].
  • Fibronectin receptor in several cell lysates was bound to a column of C279-immobilized Sepharose HP and obtained in a highly purified form by elution with a synthetic peptide, GRGDSP. alpha 5 beta 1-Integrin was detected in the GRGDSP-eluted fraction by immunoblotting [31].

References

  1. Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor. Pytela, R., Pierschbacher, M.D., Ruoslahti, E. Cell (1985) [Pubmed]
  2. Characterization of the type 3 fimbriae with different MrkD adhesins: Possible role of the MrkD containing an RGD motif. Huang, Y.J., Wu, C.C., Chen, M.C., Fung, C.P., Peng, H.L. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  3. Rhodostomin, an RGD-containing peptide expressed from a synthetic gene in Escherichia coli, facilitates the attachment of human hepatoma cells. Chang, H.H., Hu, S.T., Huang, T.F., Chen, S.H., Lee, Y.H., Lo, S.J. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  4. Two-step spreading mode of human glioma cells on fibrin monomer: interaction of alpha(v)beta3 with the substratum followed by interaction of alpha5beta1 with endogenous cellular fibronectin secreted in the extracellular matrix. Yang, W., Asakura, S., Sakai, T., Nakamura, M., Fujimura, K., Matsuda, M. Thromb. Res. (1999) [Pubmed]
  5. Integrin-mediated neurite outgrowth in neuroblastoma cells depends on the activation of potassium channels. Arcangeli, A., Becchetti, A., Mannini, A., Mugnai, G., De Filippi, P., Tarone, G., Del Bene, M.R., Barletta, E., Wanke, E., Olivotto, M. J. Cell Biol. (1993) [Pubmed]
  6. Recombinant entactin promotes mouse primary trophoblast cell adhesion and migration through the Arg-Gly-Asp (RGD) recognition sequence. Yelian, F.D., Edgeworth, N.A., Dong, L.J., Chung, A.E., Armant, D.R. J. Cell Biol. (1993) [Pubmed]
  7. Thrombin adhesive properties: induction by plasmin and heparan sulfate. Bar-Shavit, R., Eskohjido, Y., Fenton, J.W., Esko, J.D., Vlodavsky, I. J. Cell Biol. (1993) [Pubmed]
  8. A GTPase controls cell-substrate adhesion in Xenopus XTC fibroblasts. Symons, M.H., Mitchison, T.J. J. Cell Biol. (1992) [Pubmed]
  9. Endothelial cells interact with the core protein of basement membrane perlecan through beta 1 and beta 3 integrins: an adhesion modulated by glycosaminoglycan. Hayashi, K., Madri, J.A., Yurchenco, P.D. J. Cell Biol. (1992) [Pubmed]
  10. A 125/115-kDa cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fibronectin. Pytela, R., Pierschbacher, M.D., Ruoslahti, E. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  11. A novel integrin beta subunit is associated with the vitronectin receptor alpha subunit (alpha v) in a human osteosarcoma cell line and is a substrate for protein kinase C. Freed, E., Gailit, J., van der Geer, P., Ruoslahti, E., Hunter, T. EMBO J. (1989) [Pubmed]
  12. Factor XIIIa binding to activated platelets is mediated through activation of glycoprotein IIb-IIIa. Cox, A.D., Devine, D.V. Blood (1994) [Pubmed]
  13. Platelet glycoprotein IIb-IIIa (alpha IIb beta 3 integrin) confers fibrinogen- and activation-dependent aggregation on heterologous cells. Frojmovic, M.M., O'Toole, T.E., Plow, E.F., Loftus, J.C., Ginsberg, M.H. Blood (1991) [Pubmed]
  14. Blockade of alpha 5 beta 1 integrins reverses the inhibitory effect of tenascin on chemotaxis of human monocytes and polymorphonuclear leukocytes through three-dimensional gels of extracellular matrix proteins. Loike, J.D., Cao, L., Budhu, S., Hoffman, S., Silverstein, S.C. J. Immunol. (2001) [Pubmed]
  15. Beta 1- and beta 3-class integrins mediate fibronectin binding activity at the surface of developing mouse peri-implantation blastocysts. Regulation by ligand-induced mobilization of stored receptor. Schultz, J.F., Armant, D.R. J. Biol. Chem. (1995) [Pubmed]
  16. SPARC, a secreted protein associated with cellular proliferation, inhibits cell spreading in vitro and exhibits Ca+2-dependent binding to the extracellular matrix. Sage, H., Vernon, R.B., Funk, S.E., Everitt, E.A., Angello, J. J. Cell Biol. (1989) [Pubmed]
  17. RGD-containing peptides inhibit the synthesis of myelin-like membrane by cultured oligodendrocytes. Cardwell, M.C., Rome, L.H. J. Cell Biol. (1988) [Pubmed]
  18. The effect of hexapeptides on attachment and outgrowth of mouse blastocysts cultured in vitro: evidence for the involvement of the cell recognition tripeptide Arg-Gly-Asp. Armant, D.R., Kaplan, H.A., Mover, H., Lennarz, W.J. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  19. Vitronectin receptor (alpha(v)beta3) mediates platelet adhesion to the luminal aspect of endothelial cells: implications for reperfusion in acute myocardial infarction. Gawaz, M., Neumann, F.J., Dickfeld, T., Reininger, A., Adelsberger, H., Gebhardt, A., Schömig, A. Circulation (1997) [Pubmed]
  20. Two integrin-binding peptides abrogate T cell-mediated immune responses in vivo. Ferguson, T.A., Mizutani, H., Kupper, T.S. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  21. Integrin Ligands Mobilize Ca2+ from Ryanodine Receptor-gated Stores and Lysosome-related Acidic Organelles in Pulmonary Arterial Smooth Muscle Cells. Umesh, A., Thompson, M.A., Chini, E.N., Yip, K.P., Sham, J.S. J. Biol. Chem. (2006) [Pubmed]
  22. Mechanotransduction via integrins and interleukin-4 results in altered aggrecan and matrix metalloproteinase 3 gene expression in normal, but not osteoarthritic, human articular chondrocytes. Millward-Sadler, S.J., Wright, M.O., Davies, L.W., Nuki, G., Salter, D.M. Arthritis Rheum. (2000) [Pubmed]
  23. Adhesion of human platelets to serum amyloid A. Urieli-Shoval, S., Shubinsky, G., Linke, R.P., Fridkin, M., Tabi, I., Matzner, Y. Blood (2002) [Pubmed]
  24. The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin. Schnapp, L.M., Hatch, N., Ramos, D.M., Klimanskaya, I.V., Sheppard, D., Pytela, R. J. Biol. Chem. (1995) [Pubmed]
  25. Involvement of integrins and Src in insulin signaling toward autophagic proteolysis in rat liver. Schliess, F., Reissmann, R., Reinehr, R., vom Dahl, S., Häussinger, D. J. Biol. Chem. (2004) [Pubmed]
  26. Red cell ICAM-4 is a novel ligand for platelet-activated alpha IIbbeta 3 integrin. Hermand, P., Gane, P., Huet, M., Jallu, V., Kaplan, C., Sonneborn, H.H., Cartron, J.P., Bailly, P. J. Biol. Chem. (2003) [Pubmed]
  27. RGDN peptide interaction with endothelial alpha5beta1 integrin causes sustained endothelin-dependent vasoconstriction of rat skeletal muscle arterioles. Mogford, J.E., Davis, G.E., Meininger, G.A. J. Clin. Invest. (1997) [Pubmed]
  28. Isolation of a novel integrin receptor mediating Arg-Gly-Asp-directed cell adhesion to fibronectin and type I collagen from human neuroblastoma cells. Association of a novel beta 1-related subunit with alpha v. Dedhar, S., Gray, V. J. Cell Biol. (1990) [Pubmed]
  29. A fibronectin-related synthetic peptide, Pro-Ala-Ser-Ser, inhibits fibronectin binding to the cell surface, fibronectin-promoted cell migration in vitro, and cell migration in vivo. Katow, H., Yazawa, S., Sofuku, S. Exp. Cell Res. (1990) [Pubmed]
  30. Outside-in signalling of fibronectin stimulates cardiomyocyte hypertrophy in cultured neonatal rat ventricular myocytes. Ogawa, E., Saito, Y., Harada, M., Kamitani, S., Kuwahara, K., Miyamoto, Y., Ishikawa, M., Hamanaka, I., Kajiyama, N., Takahashi, N., Nakagawa, O., Masuda, I., Kishimoto, I., Nakao, K. J. Mol. Cell. Cardiol. (2000) [Pubmed]
  31. A 31-kDa recombinant fibronectin cell-binding domain fragment: its binding to receptor, cell adhesive activity, and fusion proteins. Hashino, K., Uemori, Y., Kimizuka, F., Kato, I., Titani, K. J. Biochem. (1996) [Pubmed]
 
WikiGenes - Universities