Thromb Haemost 1991; 65(05): 581-587
DOI: 10.1055/s-0038-1648194
Original Article
Schattauer GmbH Stuttgart

Platelets Adhere to Sulfatides by von Willebrand Factor Dependent and Independent Mechanisms

Richard E Data
The Hematology Service, Clinical Pathology Department, Clinical Center, Bethesda, MD, U.S.A.
,
Sybil B Williams
The Hematology Service, Clinical Pathology Department, Clinical Center, Bethesda, MD, U.S.A.
,
David D Roberts
*   The Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, U.S.A.
,
Harvey R Gralnick
The Hematology Service, Clinical Pathology Department, Clinical Center, Bethesda, MD, U.S.A.
› Author Affiliations
Further Information

Publication History

Received 02 October 1990

Accepted after revision 09 January 1991

Publication Date:
24 July 2018 (online)

Summary

Unstimulated human platelets from normal volunteers adhere to sulfatides (galactosylceramide-I3-sulfate) as single cells but do not adhere appreciably to other lipids including gangliosides, neutral glycolipids, phospholipids or cholesterol-3-SO4. Platelet adhesion to sulfatide is saturable and dose-dependent, reaches maximal levels in 90 to 120 min, and is not divalent cation-dependent. Because sulfatides bind von Willebrand factor (vWf) with specificity and high affinity and platelet adhesion to structurally related sulfated glycolipids is approximately proportionate to their ability to bind vWf, we examined whether vWf mediates platelet adhesion to sulfatides. Platelets from a patient with severe Type I von Willebrand’s disease adhere poorly to sulfatides. However, adhesion to levels seen with normal platelets is restored by the addition of vWf. Adhesion of normal platelets can be partially inhibited by a monospecific antibody to vWf. Normal platelet adhesion to sulfatides, however, is not increased following preincubation with vWf. Both vWf binding and platelet adhesion to sulfatides can be inhibited by the sulfated polysaccharide dextran sulfate at low concentration, fucoidan at high concentrations, but not by heparin, fibrinogen, fibronectin, or the synthetic peptides Gly-Arg-Gly-Asp-Ser-Pro or Gly-Arg-Gly-Glu-Ser-Pro. Thus, adhesion to sulfatides appears to be of two types; vWf dependent (50-75%) and vWf independent (25-50%).

 
  • References

  • 1 Buchanan MR, Richardson M, Haas TA, Hirsh J, Madri JA. The basement membrane underlying the vascular endothelium is not thrombogenic: In vivo and in vitro studies with rabbit and human tissue. Thromb Haemostas 1987; 58: 698-704
  • 2 Ill CR, Engvall E, Ruoslahti E. Adhesion of platelets to laminin in the absence of activation. J Cell Biol 1984; 99: 2140-2145
  • 3 Pierschbacher M, Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature (London) 1984; 309: 30-33
  • 4 Lahav J, Schwartz MA, Hynes RO. Analysis of platelet adhesion with a radioactive chemical crosslinking reagent: Interaction of thrombo-spondin with fibronectin and collagen. Cell 1982; 31: 253-262
  • 5 Girma JP, Meyer D, Verweij DL, Pannekoek J, Sixma JJ. Structure-function relationship of human von Willebrand factor. Blood 1987; 70: 605-611
  • 6 Parker RI, Gralnick HR. Identification of platelet glycoprotein IIb/ IIIa as the major binding site for released platelet von Willebrand factor. Blood 1986; 66: 732-736
  • 7 Sakariassen KS, Nievelstein PFEM, Coller BS, Sixma JJ. The role of platelet membrane glycoprotein Ib and IIb-IIIa in platelet adherence to human artery subendothelium. Br J Haematol 1986; 63: 681-691
  • 8 Houdijk WPM, Sakariassen KS, Nievelstein PFEM, Sixma JJ. Role of factor VIII-von Willebrand factor and fibronectin in the interaction of platelets in flowing blood with monomeric and fibrillar human collagen types I and III. J Clin Invest 75: 531-540
  • 9 Wagner DD, Urban-Pickering M, Marder V. von Willebrand protein binds to extracellular matrices independently of collagen. Proc Natl Acad Sci USA 1984; 81: 471-475
  • 10 Santoro SA. Identification of a 160,000 dalton platelet membrane protein that mediates the initial divalent cation-dependent adhesion of platelets to collagen. Cell 1986; 46: 913-920
  • 11 Nieuwenhuis HK, Akkerman JWN, Houdijk WPM, Sixma JJ. Human blood platelets showing no response to collagen fail to express surface glycoprotein 1a. Nature 1985; 318: 470-472
  • 12 Fujimura Y, Titani K, Holland LZ, Roberts JR, Kostel P, Ruggeri ZM, Zimmerman TS. A heparin-binding domain of human von Willebrand factor. Characterization and localization to a tryptic fragment extending from amino acid residue val 449 to lys-728. Biol Chem 1987; 262: 1734-1739
  • 13 Roberts DD, Williams SB, Gralnick HR, Ginsburg V. von Willebrand factor binds specifically to sulfated glycolipids. J Biol Chem 1986; 261: 3306-3309
  • 14 Roberts DD. Sulfatide-binding proteins. Chem Phys Lipids 1986; 42: 173-183
  • 15 Roberts DD, Wewer UM, Liotta LA, Ginsburg V. Laminin-depen-dent and laminin-independent adhesion of melanoma cells to sul-fatides. Cancer Res 1988; 48: 3367-3373
  • 16 Roberts DD, Rao C, Liotta LA, Gralnick HR, Ginsburg V. Comparison of the specificities of laminin, thrombospondin and von Willebrand factor for binding to sulfated glycolipids. J Biol Chem 1986; 261: 6872-6877
  • 17 Ishizuka I, Suzuki M, Yamakawa T. Isolation and characterization of a novel sulfoglycolipid, “Seminolipid”, from boar testis and per-matozoa. J Biochem 1973; 73: 77-87
  • 18 Rauvala H. Gangliosides of human kidney. J Biol Chem 1976; 251: 7511-7520
  • 19 Schwarzmann G. A simple and novel method for tritium labeling of gangliosides and other sphingolipids. Biochim Biophys Acta 1978; 529: 106-114
  • 20 Gralnick HR. Factor VIII/von Willebrand factor protein. Galactose, a cryptic determinant of von Willebrand activity. J Clin Invest 1978; 62: 496-499
  • 21 Gralnick HR, Coller BS, Sultan Y. Studies of the human factor VIII/ von Willebrand factor protein III. Qualitative defects in von Wille-brand’s disease. J Clin Invest 1975; 56: 814-827
  • 22 David GS. Solid state lactoperoxidase: a highly stable enzyme for simple, gentle iodination of proteins. Biochem Biophys Res Commun 1972; 48: 464-471
  • 23 David GS, Reisfeld RA. Protein iodination with solid state lactoperoxidase. Biochemistry 1974; 13: 1014-1021
  • 24 Hoyer LW, Shainoff JR. Factor VUI-related protein circulates in normal human plasma as high molecular weight multimers. Blood 1980; 60: 790-794
  • 25 Roberts DD, Havenstick DM, Dixit VM, Frazier WA, Santoro SA, Ginsburg V. The platelet glycoprotein thrombospondin binds specifically to sulfated glycolipids. J Biol Chem 1985; 260: 9405-9411
  • 26 Haverstick DM, Dixit VM, Grant GA, Frazier WA, Santoro SA. Localization of the hemagglutinating activity to platelet thrombospondin to a 140,000 dalton thermolytic fragment. Biochemistry 1984; 23: 5597-5603
  • 27 Coller BS. Interaction of normal, thrombasthénie and Bemard-Soulier platelets with immobilized fibrinogen: defective platelet-fibrinogen interaction in thrombasthenia. Blood 1980; 55: 169-178
  • 28 Hoyer LW. Immunologic studies of antihemophilic factor (AHF, factor VIII). V. Radioimmunoassay of AHF antigen. J Lab Clin Med 1972; 80: 822-833
  • 29 Timmons S, Hawiger J. Separation of human platelets from plasma proteins including factor VUI-vWf by a combined albumin gradientgel filtration method using Hepes buffer. Thromb Res 1978; 12: 297-306
  • 30 Hawker RJ, Hawker LM, Wilkinson AR. Indium (111In)-labeled platelets: optimal method. Clin Sci 1980; 58: 243-248
  • 31 Silverstein RL, Nachman RL. Thrombospondin binds to monocytes-macrophages and mediates platelet-monocyte adhesion. J Clin Invest 1987; 79: 867-874
  • 32 Plow EF, Pierschbacher E, Ruoslahti E, Marguerie G, Ginsburg 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
  • 33 Ginsberg M, Pierschbacher MD, Ruoslahti E, Marguerie G, Plow E. Inhibition of fibronectin binding to platelets by proteolytic fragments and synthetic peptides which support fibroblast adhesion. J Biol Chem 1985; 260: 3931-3936
  • 34 Haverstick DM, Cowan JP, Yamada KM, Santoro SA. Inhibition of platelet adhesion to fibronectin, fibrinogen and von Willebrand factor substrates by a synthetic tetrapeptide derived from the cell-binding domain of fibronectin. Blood 1985; 66: 946-952