Download PDF
Thromb Haemost 1990; 64(04): 589-593
DOI: 10.1055/s-0038-1647363
Original Article
Schattauer GmbH Stuttgart

Synthetic RGDS-Containing Peptides of von Willebrand Factor Inhibit Platelet Adhesion to Collagen

Edith Fressinaud
*   Laboratoire d’Hémostase, CDTS, Angers, France
,
Jean Pierre Girma
**   INSERM U.143, Hopital Bicetre, le Kremlin-Bicêtre, France
,
J Evan Sadler
***   Howard Hughes Medical Institute, Washington University, St. Louis, MO, USA
,
Hans R Baumgartner
****   Pharma Research, Hoffmann-La Roche and Co, Basel, Switzerland
,
Dominique Meyer
**   INSERM U.143, Hopital Bicetre, le Kremlin-Bicêtre, France
› Author Affiliations
Further Information

Publication History

Received 08 August 1988

Accepted after revision14 July 1990

Publication Date:
25 July 2018 (online)

  PDF Download  Permissions and Reprints

Summary

We compared the effect of a synthetic dodecapeptide of residues 400-411 of the Γ chain of fibrinogen (Γ 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. Both types of peptides are known to inhibit the binding of adhesive proteins to platelet membrane glycoprotein Ilb/IIIa (GPIIb/IIIa). Collagen was coated onto plastic cover slips and exposed in parallel-plate perfusion chambers to reconstituted human blood at various shear rates for 5 min at 37 °C. At a shear rate of 2,600 s−1, RGDS peptides inhibited platelet adhesion to collagen in a dose-dependent manner and appeared to be more potent inhibitors than the Γ Fg 400-411 on a molar basis. No synergetic effect between RGDS and Γ Fg 400-411 peptides was observed. These results suggest that the RGDS peptides affect adhesion by inhibiting the GPIIb/IIIa-vWF interaction and confirm the involvement of this platelet receptor in vWF-mediated platelet adhesion to collagen at high shear rate.

 

  • References

  • 1 Tschopp TB, Weiss HJ, Baumgartner HR. Decreased adhesion of platelets to subendothelium in von Willebrand’s disease. J Lab Clin Med 1974; 83: 296-305
    PubMedGoogle Scholar
  • 2 Hawiger J, Parkinson S, Timmons S. Prostacyclin inhibits mobilisation of fibrinogen binding sites on human ADP- and thrombin-treated platelets. Nature 1980; 283: 195-197
    CrossrefPubMedGoogle Scholar
  • 3 Plow EF, Ginsberg M. Specific and saturable binding of plasma fibronectin to thrombin-stimulated human platelets. J Biol Chem 1981; 256: 9477-9482
    PubMedGoogle Scholar
  • 4 Ruggeri ZM, De Marco L, Gatti L, Bader R, Montgomery R. Platelets have more than one binding site for von Willebrand factor. J Clin Invest 1983; 72: 1-12
    CrossrefPubMedGoogle Scholar
  • 5 Ruggeri ZM, Bader R, De Marco L. Glanzmann thrombasthenia: Deficient binding of von Willebrand factor to thrombin-stimulated platelets. Proc Natl Acad Sci USA 1982; 79: 6038-6041
    CrossrefPubMedGoogle Scholar
  • 6 Bennett JS, Hoxie JA, Leitman SF, Vilaire G, Cines DB. Inhibition of fibrinogen binding to stimulated human platelets by a monoclonal antibody. Proc Natl Acad Sci USA 1983; 80: 2417-2421
    CrossrefPubMedGoogle Scholar
  • 7 Coller BS, Peerschke EI, Scudder LE, Sullivan CA. A murine monoclonal antibody that completely blocks the binding of fibrinogen to platelets produces a thrombasthenic-like state in normal platelets and binds to glycoproteins lib and/or Ilia. J Clin Invest 1983; 72: 325-338
    CrossrefPubMedGoogle Scholar
  • 8 Pietu G, Cherel G, Marguerie GA, Meyer D. Inhibition of von Willebrand factor-platelet interaction by fibrinogen. Nature 1984; 308: 648-649
    CrossrefPubMedGoogle Scholar
  • 9 Plow EF, Pierschbacher MD, Ruoslahti E, Marguerie GA, Ginsberg MH. The effect of arg-gly-asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets. Proc Natl Acad Sci USA 1985; 82: 8057-8061
    CrossrefPubMedGoogle Scholar
  • 10 Titani K, Kumar S, Takio K, Ericsson LH, Wade RD, Ashida K, Walsh KA, Chopek MW, Sadler JE, Fujikawa K. Amino acid sequence of human von Willebrand factor. Biochemistry 1986; 25: 3171-3184
    CrossrefPubMedGoogle Scholar
  • 11 Kloczewiak M, Timmons S, Lukas T, Hawiger J. Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the y chain. Biochemistry 1984; 23: 1767-1774
    CrossrefPubMedGoogle Scholar
  • 12 Marguerie GA, Thomas-Maison N, Ginsberg MH, Plow EE. The platelet-fibrinogen interaction. Evidence for proximity of A a chain of fibrinogen to platelet membrane glycoproteins Ilb/IIIa. Eur J Biochem 1984; 139: 5-11
    CrossrefPubMedGoogle Scholar
  • 13 Plow EF, Srouji AH, Meyer D, Marguerie G, Ginsberg MH. Evidence that three adhesive proteins interact with a common recognition site on activated platelets. J Biol Chem 1984; 259: 5388-5391
    PubMedGoogle Scholar
  • 14 Miller EF, Rhodes RK. Preparation and characterization of the different types of collagen. Methods Enzymol 1982; 82: 32-41
    PubMedGoogle Scholar
  • 15 Bruns RR, Gross J. High resolution analysis of the quarter stagger model of the collagen fibril. Biopolymers 1977; 13: 931-941
    PubMedGoogle Scholar
  • 16 Woessner JF. The determination of hydroxyproline in tissue and protein samples containing small proportions of this amino acid. Arch Biochem Biophys 1961; 93: 440-447
    CrossrefPubMedGoogle Scholar
  • 17 Cohen SA, Bidlingmeyer BA, Tarvin TL. PITC derivatives in amino acid analysis. Nature (London) 1986; 320: 769-770
    CrossrefPubMedGoogle Scholar
  • 18 Hunkapiller MW, Hood LE. Analysis of phenylthiohydantoins by ultrasensitive gradient high performance liquid chromatography. Methods Enzymol 1983; 91: 486-493
    PubMedGoogle Scholar
  • 19 Hunkapiller MW, Hewick RM, Dreyer WJ, Hood LE. High-sensitivity sequency with a gas-phase sequenator. Methods Enzymol 1983; 91: 399-413
    PubMedGoogle Scholar
  • 20 Fressinaud E, Baruch D, Girma JP, Sakariassen KS, Baumgartner HR, Meyer D. von Willebrand factor-mediated platelet adhesion to collagen involves platelet membrane glycoprotein Ilb/IIIa as well as glycoprotein lb. J Lab Clin Med 1988; 112: 58-67
    PubMedGoogle Scholar
  • 21 Sakariassen KS, Aarts PA, de Groot PG, Houdijk WP, Sixma JJ. A perfusion chamber developed to investigate platelet interaction in flowing blood with human vessel wall cells, their extra-cellular matrix and purified components. J Lab Clin Med 1983; 102: 522-535
    PubMedGoogle Scholar
  • 22 Sakariassen KS, Muggli SR, Baumgartner HR. Measurements of platelet interaction with components of the vessel wall in flowing blood. In: Platelets. Methods Enzymol 1989; 169: 37-70
    PubMedGoogle Scholar
  • 23 Baumgartner HR, Muggli R. Adhesion and aggregation: Morphological demonstration and quantitation in vivo and in vitro. In: Platelets in Biology and Pathology Gordon JL. (ed). Elsevier, North-Holland, Biomedical Press; New York: 1976: 23-60
  • 24 Hynes RO. Integrins: a family of cell surface receptors. Cell 1987; 48: 549-554
    CrossrefPubMedGoogle Scholar
  • 25 Sakariassen KS, Fressinaud E, Girma JP, Meyer D, Baumgartner HR. Role of platelet membrane glycoproteins and von Willebrand factor in adhesion of platelets to subendothelium and collagen. NY Acad Sci USA 1987; 516: 52-65
    PubMedGoogle Scholar
  • 26 Weiss HJ, Hawiger J, Ruggeri ZM, Turitto VT, Thiagarajan P, Hoffmann T. Fibrinogen-independent platelet adhesion and thrombus formation on subendothelium mediated by glycoprotein Ilb-IIIa complex at high shear rate. J Clin Invest 1989; 83: 288-297
    CrossrefPubMedGoogle Scholar
  • 27 Williams S, Gralnick H. Inhibition of von Willebrand factor binding to platelets by two recognition site peptides: the pentadecapeptide of the carboxy terminus of the fibrinogen gamma chain and the tetrapeptide arg-gly-asp-ser. Thromb Res 1987; 46: 457-471
    CrossrefPubMedGoogle Scholar
  • 28 Nievelstein PF E M, Ottenhof-Rovers M, Pierschbacher MD, Sixma JJ. The arg-gly-asp (ser) sequence of fibronectin and the glycoprotein Ilb-IIIa complex are not involved in fibronectin dependent platelet adhesion in flow. Thromb Haemostas 1987; 58: 791
    PubMedGoogle Scholar
  • 29 Weiss HJ, Turitto VT, Baumgartner HR. Platelet adhesion and thrombus formation on subendothelium in platelets deficient in glycoproteins Ilb-IIIa, lb, and storage granules. Blood 1986; 68: 322-330
    PubMedGoogle Scholar
  • 30 Lombardo VT, Hodson E, Roberts JR, Kunicki TJ, Zimmerman TS, Ruggeri ZM. Independent modulation of von Willebrand factor and fibrinogen binding to the platelet membrane glycoprotein Ilb/IIIa complex as demonstrated by monoclonal antibody. J Clin Invest 1985; 76: 1950-1958
    CrossrefPubMedGoogle Scholar
  • 31 Meyer D, Fressinaud E, Sakariassen KS, Baumgartner HR, Girma JP. Role of von Willebrand factor in platelet-vessel wall interactions. Ann NY Acad Sci USA 1987; 509: 118-130
    CrossrefPubMedGoogle Scholar
  • 32 Girma JP, Kalafatis M, Pietu G, Lavergne JM, Chopek MA, Edgington TS, Meyer D. Mapping of distinct von Willebrand factor domains interacting with platelet GPIb and GPIIb/IIIa and with collagen using monoclonal antibodies. Blood 1986; 67: 1356-1366
    PubMedGoogle Scholar
  • 33 Sakariassen KS, Bolhuis PA, Sixma JJ. Human blood platelet adhesion to artery subendothelium is mediated by factor VHI-von Willebrand factor bound to the subendothelium. Nature 1979; 279: 636-638
    CrossrefPubMedGoogle Scholar
  • 34 Fressinaud E, Baruch D, Rothschild C, Baumgartner HR, Meyer D. Platelet von Willebrand factor: evidence for its involvement in platelet adhesion to collagen. Blood 1987; 70: 1214-1217
    PubMedGoogle Scholar
  • 35 Parker RI, Gralnick HR. Inhibition of platelet-von Willebrand factor binding to platelets by adhesion site peptides. Blood 1989; 74: 1226-1230
    PubMedGoogle Scholar