Interaction of lectins with human platelets Effects of platelet stimulation by thrombin and ristocetin

Ganguly, P.; Gould, N. L.; Sidhu, P.

doi:10.1016/0304-4165(79)90048-5

Cited by 30 publications

(1 citation statement)

References 24 publications

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“…These observations demonstrate that GPIb is a platelet-binding site (receptor) of vWF in the presence of ristocetin. It is known that wheat germ agglutinin which shows specificity for N-acetylglucosamine, N-acetylgalactosamine and sialic acid (24)(25)(26) preferentially binds to GPIb (27,28). There fore, complete inhibition of ristocetin (plus vWF)-induced agglutination of fixed patient platelets by wheat germ agglutinin (Fig.…”

Section: Agglutination O F Fixed Patient Platelets By Ristocetin and mentioning

confidence: 99%

Agglutination of Formalin-Fixed, Platelet-Type von Willebrand’s Disease Platelets by Human von Willebrand Factor

Takahashi

Shibata

1984

Thromb Haemost

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SummaryThe interaction of platelets and von Willebrand factor (vWF) in platelet-type von Willebrand’s disease (vWD) was characterized using formalin-fixed platelets from the patients. Formalin-fixed patient platelets were agglutinated directly by human vWF in normal plasma and type IIB vWD plasma, but not in type IIA vWD plasma. In the presence of a small amount of normal vWF, ristocetin-induced agglutination of patient platelets was enhanced with low concentrations of ristocetin. Wheat germ agglutinin and EDTA inhibited vWF-induced agglutination, although EDTA had no effect on ristocetin (plus vWF)-induced agglutination. These results demonstrate that vWF-induced agglutination of platelet-type vWD platelets is independent of active platelet metabolism but requires divalent cations, and suggest that platelet membrane glycoprotein I (GPI) would be involved in this agglutination.

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Section: Agglutination O F Fixed Patient Platelets By Ristocetin and mentioning

confidence: 99%

Agglutination of Formalin-Fixed, Platelet-Type von Willebrand’s Disease Platelets by Human von Willebrand Factor

Takahashi

Shibata

1984

Thromb Haemost

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Wheat germ agglutinin inhibits thrombin‐induced rises in cytosolic free calcium and prostacyclin synthesis by human umbilical vein endothelial cells

Grulich‐Henn

Weksler

Watanabe

et al. 1988

Journal Cellular Physiology

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To characterize the endothelial cell surface membrane glycoproteins that mediate thrombin stimulation of PGI2 synthesis by human umbilical vein endothelial cells (HUVEC), HUVEC were stimulated with thrombin in the presence or absence of different lectins. Of the lectins tested, only wheat germ agglutinin (WGA) inhibited thrombin-induced rises in cytosolic free calcium [( Ca2+]i), measured using Quin 2-loaded HUVEC and PGI2 production measured by radioimmunoassay. However, WGA by itself had no influence on baseline [Ca2+]i or PGI2 production and did not inhibit histamine-induced rises in [Ca2+]i. The inhibition of thrombin-induced rises in [Ca2+]i and PGI2 production by WGA was dose dependent, with half-maximal inhibition occurring at 2 micrograms/ml. WGA also inhibited thrombin-induced release of 3H-arachidonic acid. These effects of WGA were reversed by N-acetyl-glucosamine (GlcNAc) and N-acetyl-neuraminic acid, which bind specifically to WGA, but not by unrelated sugars. Succinylated WGA (succ-WGA), a chemically modified derivative of WGA that binds to GlcNAc but, unlike native WGA, not to sialoglycoproteins, did not inhibit thrombin-induced rises in [Ca2+]i and PGI2 production. These results suggest that thrombin induces rises in [Ca2+]i and PGI2 production by interacting with an endothelial surface membrane sialoglycoprotein.

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Detection of anomalies in cell-surface carbohydrates on thrombasthenic platelets using 125I-labeled lectins

Manso

Dios

Alberca

et al. 1986

Blut

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The composition of carbohydrates on the surface of platelets from a patient with Glanzmann's thrombasthenia and from seven normal donors were determined and compared. To this end, binding studies were performed using nine different purified 125I-labeled lectins; Concanavalin A, P-Phytohaemagglutinin, Wheat Germ Agglutinin, Dolichos biflorus, Pisum sativum, Ricinus communis II Agglutinin, Tetragonolobus purpureus, Lens culinaris and Soybean Agglutinin. These studies show that thrombasthenic platelets bear significantly decreased numbers of receptors for Concanavalin A and Lens culinaris, both with a specificity for D-mannose, and Ricinus communis II, with specificity for D-galactose. There were no detectable differences in the numbers of other lectin receptors. These results provide further evidence of molecular defects in thrombasthenic platelets. Moreover, the use of 125I-labeled lectins, as shown here, provides a fast and reliable technique for identifying abnormalities in the carbohydrate composition on the surface of platelets in various thrombopathies.

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Interaction of lectins with human platelets Effects of platelet stimulation by thrombin and ristocetin

Cited by 30 publications

References 24 publications

Agglutination of Formalin-Fixed, Platelet-Type von Willebrand’s Disease Platelets by Human von Willebrand Factor

Agglutination of Formalin-Fixed, Platelet-Type von Willebrand’s Disease Platelets by Human von Willebrand Factor

Wheat germ agglutinin inhibits thrombin‐induced rises in cytosolic free calcium and prostacyclin synthesis by human umbilical vein endothelial cells

Detection of anomalies in cell-surface carbohydrates on thrombasthenic platelets using 125I-labeled lectins

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