Interaction of Platelet Membrane Receptors with von Willebrand Factor, Ristocetin, and the Fc Region of Immunoglobulin G

Moore, A. Ulric; Ross, Gordon D.; Nachman, Ralph L.

doi:10.1172/jci109210

Cited by 67 publications

(26 citation statements)

References 25 publications

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“…Binding ofimmune complexes to GP 210 may therefore sterically hinder interaction of GP lb with ristocetin or F VIII:vWF and block aggregation. This mechanism would explain the findings of Moore et al (1). Although Nachman et al (22) suggested a structural similarity between GP 210 and GP lb based on tryptic peptide mapping, the exact nature ofGP 210 and its relationship to GP lb remains unknown.…”

Section: Resultsmentioning

confidence: 87%

“…Previous studies have suggested that platelet glycoprotein lb (GP lb)' functions as an Fc receptor (1,2). GP lb is a 170,000-molwt glycoprotein that binds von Willebrand factor (F VIII: vWF) when platelets are exposed to ristocetin (1).…”

Section: Introductionmentioning

confidence: 99%

“…GP lb is a 170,000-molwt glycoprotein that binds von Willebrand factor (F VIII: vWF) when platelets are exposed to ristocetin (1). In the Bernard-Soulier syndrome, platelets are deficient in GP lb and lack the ability to respond to ristocetin.…”

Section: Introductionmentioning

confidence: 99%

“…Moore et al. (1) showed that binding ofaggregated IgG to platelets inhibits ristocetin-induced platelet agglutination, and suggested that the IgG complex interferes with ristocetin-induced binding ofF VIII:vWF to GP lb. Also, binding of keyhole limpet hemocyanin (KLH)-anti-KLH immune complex to platelets is blocked by prior platelet exposure to ristocetin and F VIII: vWF (2).…”

Section: Introductionmentioning

confidence: 99%

“…This finding suggests that the Fc receptor may be distinct from GP lb. Moreover, 1. Abbreviations used in this paper: FITC, fluorescein isothiocyanate; F VIII: vWF, von Willebrand factor; GP, glycoprotein; KLH, keyhole limpet hemocyanin; NP-40, Nonidet P40; OA, ovalbumin; TBS, Tris-buffered saline.…”

Section: Introductionmentioning

confidence: 99%

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Evidence that a 210,000-molecular-weight glycoprotein (GP 210) serves as a platelet Fc receptor.

Stricker¹,

Reyes²,

Corash³

et al. 1987

J. Clin. Invest.

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Section: Resultsmentioning

confidence: 87%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Evidence that a 210,000-molecular-weight glycoprotein (GP 210) serves as a platelet Fc receptor.

Stricker¹,

Reyes²,

Corash³

et al. 1987

J. Clin. Invest.

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Evidence that circulating immune complexes remove transfused platelets from the circulation

et al. 1981

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Fifteen recently diagnosed patients with acute leukemias admitted for induction chemotherapy were selected for study. When thrombocytopenic (venous platelet count less than 20 X 10(9)/l) these patients received prophylactic platelet transfusions. A total of 67 platelet transfusion therapies were administered and evaluated. Using the Raji cell radioimmunoassay, the serum concentrations of circulating immune complexes (CIC) were measured immediately before and 10-12 hr after each platelet transfusion. In 36 instances, elevated values of CIC were present in the recipient's pretransfusion samples. The corresponding posttransfusion values being significantly lower (P less than 0.05). Furthermore, in those 36 instances the mean percentage for the posttransfusion platelet increment was significantly lower (P less than 0.001) than in the remaining 31 instances in which normal pretransfusion values of CIC were measured. We conclude that CIC were an important factor in rapidly removing transfused platelets from the circulation, thereby, adversely affecting the benefit of platelet transfusions.

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Platelet IgG Fc receptor

et al. 1987

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The glycoprotein localization of the platelet binding site for the Fc IgG has been the subject of debate. We attempted to resolve this issue by relating the binding of radiolabeled IgG immune complexes composed of heat-aggregated IgG to platelets from healthy individuals; an individual with Bernard-Soulier syndrome lacking glycoproteins IIb and IX; and a patient with Glanzmann's thrombasthenia lacking glycoproteins IIb and IIIa. The binding of IgG complexes to platelets was determined by measuring the specific binding of radiolabeled heat-aggregated IgG to washed platelets in a plasma-free mileu. 125I aggregated IgG bound to normal platelets in a saturable and concentration-dependent fashion. Specific binding could be inhibited by a 50-fold excess of purified Fc, but not by F(ab')2. Identical binding curves were obtained by using platelets from a patient with Glanzmann's thrombasthenia and a patient with Bernard-Soulier syndrome, indicating that the platelet Fc receptor is not carried on glycoproteins Ib, IIb, IIIa, or IX. We then measured the binding of radiolabeled detergent-solubilized platelets to IgG fixed to a solid matrix. A 40-kD platelet fragment bound to the immobilized IgG following passage across a density gradient. Confirmation of the Fc specificity of the interaction was shown by inhibition of platelet glycoprotein binding by excess IgG or purified Fc but not F(ab')2. The electrophoretic mobility decreased slightly after reduction, which indicated the existence of at least one intrachain disulfide bond. Treatment with high salt solutions or urea did not solubilize the receptor, which indicated that it was an integral protein. Enzyme studies showed that the platelet Fc receptor was not digested by neuraminidase, but neuraminidase treatment altered mobility by about 3%. In addition, treatment of platelets with trypsin or pronase did not affect its function as measured by the binding of 125I-IgG aggregates to enzyme-treated platelets, but did prevent its detection when using radioimmunoprecipitation studies. The platelet Fc receptor is a 40-kD, integral protein without interchain disulfide bonds.

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Interaction of Platelet Membrane Receptors with von Willebrand Factor, Ristocetin, and the Fc Region of Immunoglobulin G

Abstract: A B S T R A C T The agglutination of human platelets by

Cited by 67 publications

References 25 publications

Evidence that a 210,000-molecular-weight glycoprotein (GP 210) serves as a platelet Fc receptor.

Evidence that a 210,000-molecular-weight glycoprotein (GP 210) serves as a platelet Fc receptor.

Evidence that circulating immune complexes remove transfused platelets from the circulation

Platelet IgG Fc receptor

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