Advertisement
Paper| Volume 26, ISSUE 6, P431-441, June 15, 1982

Effects of galactose-binding lectins on human blood platelets: Identity of the peanut agglutinin receptor with the von Willebrand factor receptor

DOI:https://doi.org/10.1016/0049-3848(82)90315-2
Effects of galactose-binding lectins on human blood platelets: Identity of the peanut agglutinin receptor with the von Willebrand factor receptor
Previous ArticlePlatelet activation during exercise-induced myocardial ischaemia
Next ArticleThe loss of sialic acid and its prevention in stored human platelets
      This paper is only available as a PDF. To read, Please Download here.

      Abstract

      Platelets washed in the presence of EDTA were treated with neuraminidase and resuspended in platelet-poor plasma, source of human von Willebrand factor (vWF) [denoted desialo-platelets]. Peanut agglutinin (PNA), soybean agglutinin (SBA) and Math Eq agglutinin (RCAI) induced agglutination of desialo-platelets down to concentrations of 25 μg/ml. Agglutination of platelets by ristocetin/vWF was not affected by removal of the terminal sialic acid. In subagglutinating concentrations, PNA inhibited the ristocetin-induced agglutination of desialo-platelets whereas SBA and RCAI were without effect. When platelets incubated in Ca2+-containing medium were desialylated and resuspended in platelet-poor plasma [denoted desialo-platelets preincubated with Ca2+], their agglutination with PNA and ristocetin was greatly impaired, SBA and RCAI reacted normally. These results indicate that PNA and ristocetin/vWF compete in binding to the same receptor. Since asialoglycoprotein Ib was shown earlier to be the only glycoprotein on desialo-platelets to bind to a PNA-Sepharose affinity column these results provide further evidence that glycoprotein Ib is the vWF receptor on human platelets and that the carbohydrate-rich outer part of glycoprotein Ib is an essential part of the receptor structure. Lectin-induced platelet agglutination can be mediated by structures other than glycoprotein Ib but lectins which interact with glycoprotein Ib induce strong platelet responses including secretion.

      Keywords

      To read this article in full you will need to make a payment

      Purchase one-time access:

      Academic & Personal: 24 hour online accessCorporate R&D Professionals: 24 hour online access
      One-time access price info
      • For academic or personal research use, select 'Academic and Personal'
      • For corporate R&D use, select 'Corporate R&D Professionals'

      Subscribe:

      Subscribe to Thrombosis Research
      Already a print subscriber? Claim online access
      Already an online subscriber? Sign in
      Register: Create an account
      Institutional Access: Sign in to ScienceDirect

      References

        • Shattil S.J.
        • Bennett J.S.
        Platelets and their membranes in hemostasis: Physiology and pathophysiology.
        Ann. Intern. Med. 1981; 94: 108-118
        • Berndt M.C.
        • Phillips D.R.
        Platelet membrane proteins: Composition and receptor function.
        in: Platelets in Biology and Pathology. 2. Elsevier/North Holland Biomedical Press, 1981: 43-76
        • Phillips D.R.
        An evaluation of membrane glycoproteins in platelet adhesion and aggregation.
        in: Progress in Hemostasis and Thrombosis. 5. Grune and Stratton, New York1980: 81-109
        • Nurden A.T.
        • Caen J.P.
        Specific roles for platelet surface glycoproteins in platelet function.
        Nature (London). 1975; 255: 720-722
        • Jenkins C.S.P.
        • Phillips D.R.
        • Clemetson K.J.
        • Meyer D.
        • Larrieu M.-J.
        • Lüscher E.F.
        Platelet membrane glycoproteins implicated in ristocetin-induced aggregation.
        J. Clin. Invest. 1976; 57: 112-124
        • Cooper H.A.
        • Clemetson K.J.
        • Lüscher E.F.
        Human platelet membrane receptor for bovine von Willebrand factor (platelet aggregating factor): An integral membrane glycoprotein.
        in: Proc. Natl. Acad. Sci, USA. 76. 1979: 1069-1073
        • Howard M.A.
        • Firkin B.G.
        Ristocetin - A new tool in the investigation of platelet aggregation.
        Thromb. Diath. Haemorrh. 1971; 26: 362-369
        • Kirby E.P.
        Factor VIII-associated platelet aggregation.
        Thromb. Haemost. (Stuttg.). 1977; 38: 1054-1072
        • Ischopp T.B.
        • Weiss H.J.
        • Baumgartner H.R.
        Decreased adhesion of platelets to subendothelium in von Willebrand's disease.
        J. Lab. Clin. Med. 1974; 83: 296-300
        • Sharon N.
        • Lis H.
        Lectins: Cell-agglutinating and sugar-specific proteins.
        Science. 1972; 177: 949-959
        • Hughes R.C.
        Membrane Glycoproteins.
        Butterworths, London-Boston1976
        • Ganguly P.
        • Gould N.L.
        • Sidhu P.
        Interaction of lectins with human platelets.
        Biochim. Biophys. Acta. 1979; 586: 574-583
        • Clemetson K.J.
        • Pfueller S.L.
        • Lüscher E.F.
        • Jenkins C.S.P.
        Isolation of the membrane glycoproteins of human blood platelets by lectin affinity chromatography.
        Biochim. Biophys. Acta. 1977; 464: 493-508
        • Greenberg J.
        • Packham M.A.
        • Cazenave J.-P.
        • Reimers H.-J.
        • Mustard J.F.
        Effects on platelet function of removal of platelet sialic acid by neuraminidase.
        Lab. Invest. 1975; 32: 476-484
        • Patscheke H.
        • Brossmer R.
        • Wörner P.
        D-galactose-binding lectins induce a differential response on blood platelets.
        Biochem. Biophys. Res. Commun. 1977; 75: 200-206
        • Patscheke H.
        • Wörner P.
        Common activation of aggregation and release reaction of platelets.
        Thromb. Res. 1977; 11: 391-402
        • Greenberg J.H.
        • Jamieson G.A.
        The effects of various lectins on platelet aggregation and release.
        Biochim. Biophys. Acta. 1974; 345: 231-242
        • Pereira M.E.A.
        • Kabat E.A.
        • Lotan R.
        • Sharon N.
        Immunochemical studies on the specificity of the peanut (Math Eq) agglutinin.
        Carbohyd. Res. 1976; 51: 107-118
        • Pereira M.E.A.
        • Kabat E.A.
        • Sharon N.
        Immunochemical studies on specificity of soybean agglutinin.
        Carbohyd. Res. 1974; 37: 89-102
        • Debray H.
        • Decout D.
        • Strecker G.
        • Spik G.
        • Montreuil J.
        Speicificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins.
        Eur. J. Biochem. 1981; 117: 41-55
        • Baenziger J.U.
        • Fiete D.
        Structural determinants of Math Eq aggltuinin and toxin specificity for oligosaccharides.
        J. Biol. Chem. 1979; 254: 9795-9799
        • Judson P.A.
        • Anstee D.
        Characterization of membrane glycoproteins of human platelets.
        in: Peeters H. Proc. of the 27th Meeting, Protides of the Biological Fluids. Pergamon, Oxford, New York1980: 871-874
        • Clemetson K.J.
        • Naim H.Y.
        • Lüscher E.F.
        Relationship tetween glycocalicin and glycoprotein Ib of human platelets.
        in: Proc. Natl. Acad. Sci. USA. 78. 1981: 2712-2716
        • Bettex-Galland M.
        • Lüscher E.F.
        Studies on the metabolism of human blood platelets in relation to clot retraction.
        Thromb. Diath. Haemorrh. 1960; 4: 178-195
        • Massini P.
        • Lüscher E.F.
        Some effects of ionophores for divalent cations on blood platelets.
        Biochim. Biophys. Acta. 1974; 372: 109-121
        • Aminoff D.
        Methods for the quantitative estimation of N-acetyneuraminic acid and their application to hydrolysates of sialomucoids.
        Biochem. J. 1961; 81: 384-392
        • Nicolson G.L.
        • Blaustein J.
        • Etzler M.E.
        Characterization of two plant lectins from Math Eq and their quantitative interaction with a murine lymphoma.
        Biochemistry. 1974; 13: 196-204
        • McGregor J.L.
        • Clemetson K.J.
        • James E.
        • Capitanio A.
        • Greenland T.
        • Luscher E.F.
        • Dechavanne M.
        Glycoproteins of platelet membranes from Glanzmann's thrombasthenia.
        Eur. J. Biochem. 1981; 116: 379-388
        • Solum N.O.
        • Hagen I.
        • Fillion-Myklebust C.
        • Stabaek T.
        Platelet glycocalicin.
        in: Its membrane association and solubilization in aqueous media. Biochim. Biophys. Acta. 597. 1980: 235-246
        • Phillips D.R.
        • Jakabova M.
        Calcium-dependent protease in human platelets.
        J. Biol. Chem. 1977; 252: 5602-5605
        • Solum N.O.
        • Hagen I.
        • Sletbakk T.
        Further evidence for glycocalicin being derived from a larger amphiphilic platelet membrane glycoprotein.
        Thromb. Res. 1980; 18: 773-785

      Article info

      Publication history

      Received in revised form: March 30, 1982
      Received: December 11, 1981

      Identification

      DOI: https://doi.org/10.1016/0049-3848(82)90315-2

      Copyright

      © 1982 Published by Elsevier Inc.

      ScienceDirect

      Access this article on ScienceDirect

      The content on this site is intended for healthcare professionals.


      We use cookies to help provide and enhance our service and tailor content. To update your cookie settings, please visit the Cookie Preference Center for this site.
      Copyright © 2023 Elsevier Inc. except certain content provided by third parties.


      RELX