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Journal articles on the topic 'Glycoprotein IIb/IIIa (GP IIb/IIIa) complex'

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Published: 3 June 2025

Last updated: 31 July 2025

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1

Royo, Teresa, Matilde Vidal, and Lina Badimon. "Purification of the Porcine Platelet GP IIb-IIIa Complex and the Propolypeptide of von Willebrand Factor." Thrombosis and Haemostasis 80, no. 08 (1998): 302–9. http://dx.doi.org/10.1055/s-0037-1615192.

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SummaryPlatelet membrane glycoproteins (GP) are involved in platelet adhesion and aggregation. The glycoprotein IIb-IIIa complex (GP IIbIIIa) is a Ca2+-dependent heterodimer that binds fibrinogen and other adhesive proteins, thereby mediating platelet aggregation and adhesion. We have purified two major glycoproteins from pig platelets by Concanavalin A-Sepharose, Heparin-Sepharose and Sephacryl S-300 HR chromatography (Fitzgerald et al. Anal Biochem, 1985): i) the GP IIb-IIIa complex, GP IIb Mr = 140,000 and GP IIIa a single chain of Mr = 95,000-100,000; and ii) a predominant glycoprotein of

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2

Parise, L. V., B. Steiner, L. Nannizzi, A. B. Criss, and D. R. Phillips. "Evidence for novel binding sites on the platelet glycoprotein IIb and IIIa subunits and immobilized fibrinogen." Biochemical Journal 289, no. 2 (1993): 445–51. http://dx.doi.org/10.1042/bj2890445.

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The present study was designed to examine the interaction of the purified platelet glycoprotein IIb-IIIa complex (GP IIb-IIIa or integrin alpha IIb beta 3) and the individual subunits of the complex with immobilized fibrinogen. Although 125I-GP IIb-IIIa binding to fibrinogen immobilized on Sepharose was specific, this interaction exhibited properties distinct from those of reversible fibrinogen binding to platelets: 125I-GP IIb-IIIa binding appeared irreversible, but non-covalent, Ca(2+)-independent, and was inhibited only weakly, or not at all, by the anti-(GP IIb-IIIa) monoclonal antibodies

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3

Meyer, M., C. M. Kirchmaier, A. Schirmer, P. Spangenberg, Ch Ströhl, and K. Breddin. "Acquired Disorder of Platelet Function Associated with Autoantibodies against Membrane Glycoprotein IIb-IIIa Complex - 1. Glycoprotein Analysis." Thrombosis and Haemostasis 65, no. 05 (1991): 491–96. http://dx.doi.org/10.1055/s-0038-1648178.

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SummaryA patient with idiopathic thrombocytopenic purpura developed after splenectomy a thrombasthenia-like severe haemor-rhagic diathesis characterized by a normal or subnormal platelet count, prolonged bleeding time, strongly reduced platelet adhesion to glass and defective platelet aggregation in response to ADP and collagen. In contrast to hereditary thrombasthenia membrane glycoproteins (GP) lib and Ilia were normally present in the patient’s platelets. Immunoelectrophoretic analysis revealed an abnormal behaviour of the patient’s GP IIb-IIIa complex. Autoantibodies against GP IIb-IIIa we

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4

Fournier, Dominique J., Arnold Kabral, Peter A. Castaldi, and Michael C. Berndt. "A Variant of Glanzmann's Thrombasthenia Characterized by Abnormal Glycoprotein IIb/IIIa Complex Formation." Thrombosis and Haemostasis 62, no. 03 (1989): 977–83. http://dx.doi.org/10.1055/s-0038-1651038.

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SummaryGlanzmann's thrombasthenia is a congenital bleeding abnormality characterized by absent platelet aggregation due to the failure of fibrinogen to bind to activated thrombasthenic platelets. In the majority of cases, this defect is caused by the absence or marked reduction of a specific fibrinogen-binding aggregation receptor, the GP IIb/IIIa complex. E.T., an 18-year-old female with a life-long history of bleeding and easy bruising, had the normal clinical features of Glanzmann's thrombasthenia. Surprisingly, sodium dodecyl sulphate-polyacrylamide gel electrophoresis of her platelets sho

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5

Hiraiwa, A., A. Matsukage, H. Shiku, T. Takahashi, K. Naito, and K. Yamada. "Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa." Blood 69, no. 2 (1987): 560–64. http://dx.doi.org/10.1182/blood.v69.2.560.560.

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Abstract The glycoprotein (GP) IIb-IIIa complex was isolated from human platelet membranes by immunoaffinity chromatography using a monoclonal antibody specific for GP IIb-IIIa. GP IIb and IIIa were further separated in the presence of sodium dodecyl sulfate (SDS) by gel filtration high- performance liquid chromatography (HPLC). Two cycles of this procedure yielded almost complete separation of homogeneous preparations of GP IIb and IIIa. Each protein was then digested with lysyl endopeptidase (Achromobacter protease I), which cleaves at the carboxyl side of lysine residues, and the resulting

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6

Hiraiwa, A., A. Matsukage, H. Shiku, T. Takahashi, K. Naito, and K. Yamada. "Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa." Blood 69, no. 2 (1987): 560–64. http://dx.doi.org/10.1182/blood.v69.2.560.bloodjournal692560.

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The glycoprotein (GP) IIb-IIIa complex was isolated from human platelet membranes by immunoaffinity chromatography using a monoclonal antibody specific for GP IIb-IIIa. GP IIb and IIIa were further separated in the presence of sodium dodecyl sulfate (SDS) by gel filtration high- performance liquid chromatography (HPLC). Two cycles of this procedure yielded almost complete separation of homogeneous preparations of GP IIb and IIIa. Each protein was then digested with lysyl endopeptidase (Achromobacter protease I), which cleaves at the carboxyl side of lysine residues, and the resulting oligopept

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7

Levene, RB, and EM Rabellino. "Platelet glycoproteins IIb and IIIa associated with blood monocytes are derived from platelets." Blood 67, no. 1 (1986): 207–13. http://dx.doi.org/10.1182/blood.v67.1.207.207.

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Abstract Platelet glycoprotein IIb/IIIa (GP IIb/IIIa), the receptor complex for fibrinogen, has been regarded as a megakaryocyte/platelet lineage- restricted antigen. Recently, however, it has been reported that GP IIb/IIIa is expressed in blood monocytes. Studies were performed to establish the origin and immunological characteristics of monocyte- associated glycoproteins IIb and IIIa (GPs IIb and IIIa). Preparations of blood monocytes containing varying platelet-monocyte ratios were metabolically labeled with [35S]methionine with the expectation that any newly synthesized GPs IIb and IIIa wo

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8

Levene, RB, and EM Rabellino. "Platelet glycoproteins IIb and IIIa associated with blood monocytes are derived from platelets." Blood 67, no. 1 (1986): 207–13. http://dx.doi.org/10.1182/blood.v67.1.207.bloodjournal671207.

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Platelet glycoprotein IIb/IIIa (GP IIb/IIIa), the receptor complex for fibrinogen, has been regarded as a megakaryocyte/platelet lineage- restricted antigen. Recently, however, it has been reported that GP IIb/IIIa is expressed in blood monocytes. Studies were performed to establish the origin and immunological characteristics of monocyte- associated glycoproteins IIb and IIIa (GPs IIb and IIIa). Preparations of blood monocytes containing varying platelet-monocyte ratios were metabolically labeled with [35S]methionine with the expectation that any newly synthesized GPs IIb and IIIa would be mo

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9

Parise, LV, AB Criss, L. Nannizzi, and MR Wardell. "Glycoprotein IIIa is phosphorylated in intact human platelets." Blood 75, no. 12 (1990): 2363–68. http://dx.doi.org/10.1182/blood.v75.12.2363.2363.

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Abstract The glycoprotein IIb-IIIa complex (GP IIb-IIIa) is a multifunctional transmembrane protein on platelets. Its most completely described function is as a fibrinogen receptor that mediates platelet aggregation, but it is also involved in clot retraction, signal transduction, calcium transport, and other events. However, the mechanisms that regulate the functions of GP IIb-IIIa during platelet activation are largely unknown. One possible mechanism is phosphorylation, since several other receptors are regulated by this process. We found that GP IIIa, but not GP IIb, was phosphorylated in 3

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10

Parise, LV, AB Criss, L. Nannizzi, and MR Wardell. "Glycoprotein IIIa is phosphorylated in intact human platelets." Blood 75, no. 12 (1990): 2363–68. http://dx.doi.org/10.1182/blood.v75.12.2363.bloodjournal75122363.

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The glycoprotein IIb-IIIa complex (GP IIb-IIIa) is a multifunctional transmembrane protein on platelets. Its most completely described function is as a fibrinogen receptor that mediates platelet aggregation, but it is also involved in clot retraction, signal transduction, calcium transport, and other events. However, the mechanisms that regulate the functions of GP IIb-IIIa during platelet activation are largely unknown. One possible mechanism is phosphorylation, since several other receptors are regulated by this process. We found that GP IIIa, but not GP IIb, was phosphorylated in 32P-labele

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11

Pidard, D., D. Didry, TJ Kunicki, and AT Nurden. "Temperature-dependent effects of EDTA on the membrane glycoprotein IIb- IIIa complex and platelet aggregability." Blood 67, no. 3 (1986): 604–11. http://dx.doi.org/10.1182/blood.v67.3.604.604.

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Abstract In agreement with previous studies, we observed that incubation of washed human platelets with EDTA at 37 degrees C for short periods caused an irreversible loss of their aggregation response to adenosine diphosphate and markedly diminished their capacity to bind fibrinogen. AP-2 is a monoclonal antibody that reacts with a determinant specific to the glycoprotein (GP) IIb-IIIa complex. We now report that in a direct binding assay, the number of sites for AP-2 on platelets incubated with EDTA at 37 degrees C fell to approximately 30% of those present on control platelets. This effect o

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12

Pidard, D., D. Didry, TJ Kunicki, and AT Nurden. "Temperature-dependent effects of EDTA on the membrane glycoprotein IIb- IIIa complex and platelet aggregability." Blood 67, no. 3 (1986): 604–11. http://dx.doi.org/10.1182/blood.v67.3.604.bloodjournal673604.

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In agreement with previous studies, we observed that incubation of washed human platelets with EDTA at 37 degrees C for short periods caused an irreversible loss of their aggregation response to adenosine diphosphate and markedly diminished their capacity to bind fibrinogen. AP-2 is a monoclonal antibody that reacts with a determinant specific to the glycoprotein (GP) IIb-IIIa complex. We now report that in a direct binding assay, the number of sites for AP-2 on platelets incubated with EDTA at 37 degrees C fell to approximately 30% of those present on control platelets. This effect of EDTA wa

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13

Hamamoto, Kenjiro, Shosaku Nomura, Masahiko Suzuki, Shigetoshi Ohga, and Shirou Fukuhara. "Internalization of an Anti-Glycoprotein IIb/IIIa Antibody by HEL Cells." Thrombosis and Haemostasis 73, no. 02 (1995): 291–96. http://dx.doi.org/10.1055/s-0038-1653767.

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SummaryPlatelets are known to internalize monoclonal antibodies directed against the glycoprotein (GP) IIb/IIIa complex. We investigated whether an antibody directed against this complex (NNKY 2-11) was transported from the surface membrane to the intracellular pool in HEL cells. Flow cytometry showed that the percent binding of NNKY 2-11 to the surface membrane of HEL cells was decreased after incubation for 24 h compared with 1 h, while the binding of an anti-GPIb antibody (NNKY 5-5) did not change. It did not seem likely that the GP Ilb/IIIa complex antibody was shed from the surface membra

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14

Powling, MJ, and RM Hardisty. "Glycoprotein IIb-IIIa complex and Ca2+ influx into stimulated platelets." Blood 66, no. 3 (1985): 731–34. http://dx.doi.org/10.1182/blood.v66.3.731.731.

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Abstract Changes in intracellular Ca2+ concentrations [( Ca2+]i) in platelets stimulated with aggregating agents were measured with the fluorescent indicator dye quin 2. Ca2+ influx, but not intracellular mobilization, in response to adenosine diphosphate (ADP), platelet aggregating factor (PAF-acether), and sodium arachidonate was significantly inhibited by monoclonal antibodies against the glycoprotein (GP) IIb-IIIa complex; inhibition of thrombin-stimulated influx was inhibited to a lesser extent and reached statistical significance only at thrombin concentrations of 0.1 U/mL and below. Ant

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15

Powling, MJ, and RM Hardisty. "Glycoprotein IIb-IIIa complex and Ca2+ influx into stimulated platelets." Blood 66, no. 3 (1985): 731–34. http://dx.doi.org/10.1182/blood.v66.3.731.bloodjournal663731.

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Changes in intracellular Ca2+ concentrations [( Ca2+]i) in platelets stimulated with aggregating agents were measured with the fluorescent indicator dye quin 2. Ca2+ influx, but not intracellular mobilization, in response to adenosine diphosphate (ADP), platelet aggregating factor (PAF-acether), and sodium arachidonate was significantly inhibited by monoclonal antibodies against the glycoprotein (GP) IIb-IIIa complex; inhibition of thrombin-stimulated influx was inhibited to a lesser extent and reached statistical significance only at thrombin concentrations of 0.1 U/mL and below. Anti-GP Ib a

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16

Kieffer, N., JL Wautier, L. Coulombel, et al. "Uncoupling in the expression of platelet GP IIb/IIIa in human endothelial cells and K562 cells: absence of immunologic crossreactivity between platelet GP IIb and the vitronectin receptor alpha chain [see comments]." Blood 72, no. 4 (1988): 1209–15. http://dx.doi.org/10.1182/blood.v72.4.1209.1209.

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Abstract Platelet glycoproteins (GP) IIb and IIIa exist as noncovalently associated Ca++-dependent heterodimer complexes within the platelet membrane and express the major platelet alloantigens Leka (Baka) and PIA1 (Zwa), which are genetic markers of GP IIb and GP IIIa, respectively. Since heterodimers immunologically related to platelet GP IIb/IIIa have been identified in a number of nucleated cell types, we tested anti-Leka and anti-PIA1 antiserum, polyclonal anti-platelet GP IIb/IIIa IgG, as well as a panel of 28 monoclonal anti-GP IIb, GP IIIa, or complex dependent anti-GP IIb/IIIa antibod

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17

Kieffer, N., JL Wautier, L. Coulombel, et al. "Uncoupling in the expression of platelet GP IIb/IIIa in human endothelial cells and K562 cells: absence of immunologic crossreactivity between platelet GP IIb and the vitronectin receptor alpha chain [see comments]." Blood 72, no. 4 (1988): 1209–15. http://dx.doi.org/10.1182/blood.v72.4.1209.bloodjournal7241209.

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Platelet glycoproteins (GP) IIb and IIIa exist as noncovalently associated Ca++-dependent heterodimer complexes within the platelet membrane and express the major platelet alloantigens Leka (Baka) and PIA1 (Zwa), which are genetic markers of GP IIb and GP IIIa, respectively. Since heterodimers immunologically related to platelet GP IIb/IIIa have been identified in a number of nucleated cell types, we tested anti-Leka and anti-PIA1 antiserum, polyclonal anti-platelet GP IIb/IIIa IgG, as well as a panel of 28 monoclonal anti-GP IIb, GP IIIa, or complex dependent anti-GP IIb/IIIa antibodies on en

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18

Boukerche, H., O. Berthier-Vergnes, M. Bailly, JF Dore, LL Leung, and JL McGregor. "A monoclonal antibody (LYP18) directed against the blood platelet glycoprotein IIb/IIIa complex inhibits human melanoma growth in vivo." Blood 74, no. 3 (1989): 909–12. http://dx.doi.org/10.1182/blood.v74.3.909.909.

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Abstract A monoclonal antibody (MoAb) (LYP18), generated against human platelet glycoprotein IIb/IIIa (GPIIb/IIIa), immuno-precipitated a IIb/IIIa-like GP complex from a highly tumorigenic human melanoma cell line (M3Dau). The M3Dau melanoma cells specifically bound 125I-labeled LYP18. To study the biologic role of these IIb/IIIa-like glycoproteins, M3Dau melanoma cells were incubated with LYP18 or a control MoAb directed against another melanoma cell-surface antigen and implanted subcutaneously (SC) in nude mice. LYP18 dramatically inhibited the growth of tumor in vivo. LYP18 was not directly

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19

Boukerche, H., O. Berthier-Vergnes, M. Bailly, JF Dore, LL Leung, and JL McGregor. "A monoclonal antibody (LYP18) directed against the blood platelet glycoprotein IIb/IIIa complex inhibits human melanoma growth in vivo." Blood 74, no. 3 (1989): 909–12. http://dx.doi.org/10.1182/blood.v74.3.909.bloodjournal743909.

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A monoclonal antibody (MoAb) (LYP18), generated against human platelet glycoprotein IIb/IIIa (GPIIb/IIIa), immuno-precipitated a IIb/IIIa-like GP complex from a highly tumorigenic human melanoma cell line (M3Dau). The M3Dau melanoma cells specifically bound 125I-labeled LYP18. To study the biologic role of these IIb/IIIa-like glycoproteins, M3Dau melanoma cells were incubated with LYP18 or a control MoAb directed against another melanoma cell-surface antigen and implanted subcutaneously (SC) in nude mice. LYP18 dramatically inhibited the growth of tumor in vivo. LYP18 was not directly cytotoxi

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20

Giltay, JC, OC Leeksma, C. Breederveld, and JA van Mourik. "Normal synthesis and expression of endothelial IIb/IIIa in Glanzmann's thrombasthenia." Blood 69, no. 3 (1987): 809–12. http://dx.doi.org/10.1182/blood.v69.3.809.809.

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Abstract Glanzmann's thrombasthenia is a bleeding disorder, inherited in an autosomal recessive way and characterized by an absence or deficiency of the platelet glycoprotein (GP) IIb/IIIa complex. Recently, we and others demonstrated that cultured human umbilical vein endothelial cells synthesized a membrane protein complex similar to the platelet GP IIb/IIIa complex. In this article, we demonstrate that endothelial cells isolated from the umbilical vein of a newborn with Glanzmann's thrombasthenia, as compared with normal endothelial cells, show no difference in their ability to synthesize a

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Giltay, JC, OC Leeksma, C. Breederveld, and JA van Mourik. "Normal synthesis and expression of endothelial IIb/IIIa in Glanzmann's thrombasthenia." Blood 69, no. 3 (1987): 809–12. http://dx.doi.org/10.1182/blood.v69.3.809.bloodjournal693809.

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Glanzmann's thrombasthenia is a bleeding disorder, inherited in an autosomal recessive way and characterized by an absence or deficiency of the platelet glycoprotein (GP) IIb/IIIa complex. Recently, we and others demonstrated that cultured human umbilical vein endothelial cells synthesized a membrane protein complex similar to the platelet GP IIb/IIIa complex. In this article, we demonstrate that endothelial cells isolated from the umbilical vein of a newborn with Glanzmann's thrombasthenia, as compared with normal endothelial cells, show no difference in their ability to synthesize and expres

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22

Boukerche, H., O. Berthier-Vergnes, E. Tabone, JF Dore, LL Leung, and JL McGregor. "Platelet-melanoma cell interaction is mediated by the glycoprotein IIb- IIIa complex." Blood 74, no. 2 (1989): 658–63. http://dx.doi.org/10.1182/blood.v74.2.658.bloodjournal742658.

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A human malignant melanoma cell line (M3Dau) was observed by electron microscopy to interact directly with human platelets and induced platelet aggregation. Fab fragments of a monoclonal antibody MoAb (LYP18), directed against the platelet glycoprotein (GP) IIb-IIIa complex, inhibited platelet-melanoma interactions and platelet-platelet aggregation. M3Dau melanoma cells bind LYP 18 and synthesize IIb-IIIa- like GPs. When the melanoma cells were preincubated with LYP 18, tumor- platelet interaction did not occur, suggesting that the interaction may be mediated by the IIb-IIIa-like GPs present o

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23

Boukerche, H., O. Berthier-Vergnes, E. Tabone, JF Dore, LL Leung, and JL McGregor. "Platelet-melanoma cell interaction is mediated by the glycoprotein IIb- IIIa complex." Blood 74, no. 2 (1989): 658–63. http://dx.doi.org/10.1182/blood.v74.2.658.658.

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Abstract A human malignant melanoma cell line (M3Dau) was observed by electron microscopy to interact directly with human platelets and induced platelet aggregation. Fab fragments of a monoclonal antibody MoAb (LYP18), directed against the platelet glycoprotein (GP) IIb-IIIa complex, inhibited platelet-melanoma interactions and platelet-platelet aggregation. M3Dau melanoma cells bind LYP 18 and synthesize IIb-IIIa- like GPs. When the melanoma cells were preincubated with LYP 18, tumor- platelet interaction did not occur, suggesting that the interaction may be mediated by the IIb-IIIa-like GPs

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24

Gachet, Christian, Anita Stierlé, Philippe Ohlmann, François Lanza, Daniel Hanau, and Jean-Pierre Cazenave. "Normal ADP-Induced Aggregation and Absence of Dissociation of the Membrane GP IIb-IIIa Complex of Intact Rat Platelets Pretreated with EDTA." Thrombosis and Haemostasis 66, no. 02 (1991): 246–53. http://dx.doi.org/10.1055/s-0038-1646398.

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SummaryADP-induced platelet aggregation requires the presence of external calcium and fibrinogen. When human platelets are incubated for 30 min at 37° C with 5mM EDTA and then resuspended in a calcium containing medium, they lose their ability to bind fibrinogen and to aggregate in response to ADP stimulation. Under these conditions, the effect of EDTA is irreversible and accompanied by dissociation of the glycoprotein (GP) IIb-IIIa complex into its free subunits, GP IIb and GP IIIa. We studied the effect of incubation of intact rat platelets with 5 mM EDTA at 37° C from 30 to 120 min. EDTA tr

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25

Ware, J. A., M. T. Decenzo, M. Smith, and M. Saitoh. "Calcium mobilization and glycoprotein IIb-IIIa complex ligands in epinephrine-stimulated platelets." American Journal of Physiology-Heart and Circulatory Physiology 260, no. 5 (1991): H1619—H1624. http://dx.doi.org/10.1152/ajpheart.1991.260.5.h1619.

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In the presence of extracellular Ca2+, epinephrine induces a rise in cytoplasmic Ca2+ ([Ca2+]i) that is associated with fibrinogen binding to the platelet surface, platelet aggregation, and enhancement of the thrombin-stimulated [Ca2+]i rise and protein phosphorylation. Whether the [Ca2+]i rise induced by epinephrine results from Ca2+ entry associated with fibrinogen binding to its receptor on the platelet surface, the glycoprotein (gp) IIb-IIIa complex, is unknown. To determine the importance of the occupancy of the gp IIb-IIIa receptor on platelet function after epinephrine administration, w

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26

Kieffer, N., L. A. Fitzgerald, D. Wolf, D. A. Cheresh, and D. R. Phillips. "Adhesive properties of the beta 3 integrins: comparison of GP IIb-IIIa and the vitronectin receptor individually expressed in human melanoma cells." Journal of Cell Biology 113, no. 2 (1991): 451–61. http://dx.doi.org/10.1083/jcb.113.2.451.

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Glycoprotein IIb-IIIa (alpha IIb beta 3) and the vitronectin receptor (alpha v beta 3), two integrins that share the common beta 3 subunit, have been reported to function as promiscuous receptors for the RGD-containing adhesive proteins fibrinogen, vitronectin, fibronectin, von Willebrand factor, and thrombospondin. The present study was designed to establish a cell system for the expression of either GP IIb-IIIa or the vitronectin receptor in an otherwise identical cellular environment and to compare the adhesive properties of these two integrins with those of native GP IIb-IIIa and the vitro

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27

Leeksma, OC, J. Zandbergen-Spaargaren, JC Giltay, and JA van Mourik. "Cultured human endothelial cells synthesize a plasma membrane protein complex immunologically related to the platelet glycoprotein IIb/IIIa complex." Blood 67, no. 4 (1986): 1176–80. http://dx.doi.org/10.1182/blood.v67.4.1176.1176.

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Abstract We have previously demonstrated that endothelial cells synthesize a plasma membrane protein indistinguishable from platelet glycoprotein (GP) IIa. The present study provides evidence for a further analogy between the platelet and the endothelial cell membrane by showing that cultured endothelial cells also synthesize a membrane protein complex immunologically related to the platelet GP IIb/GP IIIa complex. This evidence is based on the following observations: (1) C17, a murine monoclonal antiplatelet GP IIIa antibody, consistently precipitates two proteins, apparent molecular weights,

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Leeksma, OC, J. Zandbergen-Spaargaren, JC Giltay, and JA van Mourik. "Cultured human endothelial cells synthesize a plasma membrane protein complex immunologically related to the platelet glycoprotein IIb/IIIa complex." Blood 67, no. 4 (1986): 1176–80. http://dx.doi.org/10.1182/blood.v67.4.1176.bloodjournal6741176.

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We have previously demonstrated that endothelial cells synthesize a plasma membrane protein indistinguishable from platelet glycoprotein (GP) IIa. The present study provides evidence for a further analogy between the platelet and the endothelial cell membrane by showing that cultured endothelial cells also synthesize a membrane protein complex immunologically related to the platelet GP IIb/GP IIIa complex. This evidence is based on the following observations: (1) C17, a murine monoclonal antiplatelet GP IIIa antibody, consistently precipitates two proteins, apparent molecular weights, respecti

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29

Annamol, Joseph* Rinto Paul Raju Alen Joe Francy L.Britto Duraisingh Haja Sherief S. T. Sivakumar. "A CASE REPORT ON GLANZMANN'S THROMBASTHENIA." Indo American Journal of Pharmaceutical Sciences 04, no. 12 (2017): 4729–32. https://doi.org/10.5281/zenodo.1087450.

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Glanzmann’s thrombasthenia (GT) is a rare autosomal recessive disorder in which the platelet glycoprotein IIb/IIIa (GP IIb/IIIa) complex is either deficient or, dysfunctional. The incidence is about 1 in 1,000,000. It is more common in populations where marriage between blood relatives is common. The signs of GT occur early in life and include easy bruising, epistaxis and prolonged bleeding from minor injuries. Epistaxis, menorrhagia, postpartum bleeding and surgical bleeding can be life-threatening. Here we are presenting a case of 4 year old female child with recurrent epistaxis and gi

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30

Golden, A., J. S. Brugge, and S. J. Shattil. "Role of platelet membrane glycoprotein IIb-IIIa in agonist-induced tyrosine phosphorylation of platelet proteins." Journal of Cell Biology 111, no. 6 (1990): 3117–27. http://dx.doi.org/10.1083/jcb.111.6.3117.

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Treatment of platelets with thrombin was shown previously to induce rapid changes in tyrosine phosphorylation of several platelet proteins. In this report, we demonstrate that a variety of agonists which induce platelet aggregation also stimulate tyrosine phosphorylation of three proteins with apparent molecular masses of 84, 95, and 97 kD. Since platelet aggregation requires the agonist-induced activation of an integrin receptor (GP IIb-IIIa) as well as the binding of fibrinogen to this receptor, we examined the relationship between tyrosine phosphorylation and the function of GP IIb-IIIa. Wh

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Coller, BS, DA Cheresh, E. Asch, and U. Seligsohn. "Platelet vitronectin receptor expression differentiates Iraqi-Jewish from Arab patients with Glanzmann thrombasthenia in Israel." Blood 77, no. 1 (1991): 75–83. http://dx.doi.org/10.1182/blood.v77.1.75.75.

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Abstract Glanzmann thrombasthenia is a rare, inherited disorder of the platelet glycoprotein IIb/IIIa (GP IIb/IIIa) complex. We previously identified two distinct populations with this disorder in Israel, Iraqi-Jews and Arabs. The groups are indistinguishable in hemorrhagic symptoms and platelet GP IIB/IIIa receptor deficiency, but they differ in their platelet immunodetectable GP IIIa (beta 3), with the Iraqi-Jewish population expressing no detectable GP IIIa and the Arab population expressing small amounts. We have now examined the platelets of these two populations as well as normal platele

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Coller, BS, DA Cheresh, E. Asch, and U. Seligsohn. "Platelet vitronectin receptor expression differentiates Iraqi-Jewish from Arab patients with Glanzmann thrombasthenia in Israel." Blood 77, no. 1 (1991): 75–83. http://dx.doi.org/10.1182/blood.v77.1.75.bloodjournal77175.

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Glanzmann thrombasthenia is a rare, inherited disorder of the platelet glycoprotein IIb/IIIa (GP IIb/IIIa) complex. We previously identified two distinct populations with this disorder in Israel, Iraqi-Jews and Arabs. The groups are indistinguishable in hemorrhagic symptoms and platelet GP IIB/IIIa receptor deficiency, but they differ in their platelet immunodetectable GP IIIa (beta 3), with the Iraqi-Jewish population expressing no detectable GP IIIa and the Arab population expressing small amounts. We have now examined the platelets of these two populations as well as normal platelets for th

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Suldan, Z., and LF Brass. "Role of the glycoprotein IIb-IIIa complex in plasma membrane Ca2+ transport: a comparison of results obtained with platelets and human erythroleukemia cells." Blood 78, no. 11 (1991): 2887–93. http://dx.doi.org/10.1182/blood.v78.11.2887.2887.

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Abstract Several studies have suggested that the glycoprotein (GP) IIb-IIIa complex, which serves as the platelet fibrinogen receptor, also plays a role in the regulation of Ca2+ influx across the platelet plasma membrane. To examine this possibility further, we have compared Ca2+ transport in platelets and human erythroleukemia (HEL) cells, a megakaryoblastic cell line which synthesizes GP IIb-IIIa complexes that appear to be identical to those found on platelets. As with platelets, the results show the presence in unstimulated HEL cells of a rapidly exchangeable cytosolic Ca2+ pool that is i

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34

Suldan, Z., and LF Brass. "Role of the glycoprotein IIb-IIIa complex in plasma membrane Ca2+ transport: a comparison of results obtained with platelets and human erythroleukemia cells." Blood 78, no. 11 (1991): 2887–93. http://dx.doi.org/10.1182/blood.v78.11.2887.bloodjournal78112887.

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Several studies have suggested that the glycoprotein (GP) IIb-IIIa complex, which serves as the platelet fibrinogen receptor, also plays a role in the regulation of Ca2+ influx across the platelet plasma membrane. To examine this possibility further, we have compared Ca2+ transport in platelets and human erythroleukemia (HEL) cells, a megakaryoblastic cell line which synthesizes GP IIb-IIIa complexes that appear to be identical to those found on platelets. As with platelets, the results show the presence in unstimulated HEL cells of a rapidly exchangeable cytosolic Ca2+ pool that is in equilib

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35

Simsek, S., H. Heyboer, LG de Bruijne-Admiraal, R. Goldschmeding, HT Cuijpers, and AE von dem Borne. "Glanzmann's thrombasthenia caused by homozygosity for a splice defect that leads to deletion of the first coding exon of the glycoprotein IIIa mRNA." Blood 81, no. 8 (1993): 2044–49. http://dx.doi.org/10.1182/blood.v81.8.2044.2044.

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Abstract Glanzmann's thrombasthenia (GT) is the result of the absence or of an altered and dysfunctional expression on the platelet membrane of the fibrinogen receptor (glycoprotein [GP] IIb/IIIa complex). Various molecular genetic mechanisms have been found to be responsible for this inherited disease. In a patient with a severe type of GT, we have found a splice variant in the GP IIIa gene that leads to premature chain termination. Immunoprecipitation experiments, using monoclonal antibodies specific for GP IIb/IIIa, showed that GP IIb/IIIa was not detectable on the platelet membrane. Amplif

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36

Simsek, S., H. Heyboer, LG de Bruijne-Admiraal, R. Goldschmeding, HT Cuijpers, and AE von dem Borne. "Glanzmann's thrombasthenia caused by homozygosity for a splice defect that leads to deletion of the first coding exon of the glycoprotein IIIa mRNA." Blood 81, no. 8 (1993): 2044–49. http://dx.doi.org/10.1182/blood.v81.8.2044.bloodjournal8182044.

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Glanzmann's thrombasthenia (GT) is the result of the absence or of an altered and dysfunctional expression on the platelet membrane of the fibrinogen receptor (glycoprotein [GP] IIb/IIIa complex). Various molecular genetic mechanisms have been found to be responsible for this inherited disease. In a patient with a severe type of GT, we have found a splice variant in the GP IIIa gene that leads to premature chain termination. Immunoprecipitation experiments, using monoclonal antibodies specific for GP IIb/IIIa, showed that GP IIb/IIIa was not detectable on the platelet membrane. Amplification o

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37

Molino, M., M. Di Lallo, N. Martelli, G. de Gaetano, and C. Cerletti. "Effects of leukocyte-derived cathepsin G on platelet membrane glycoprotein Ib-IX and IIb-IIIa complexes: a comparison with thrombin." Blood 82, no. 8 (1993): 2442–51. http://dx.doi.org/10.1182/blood.v82.8.2442.2442.

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Abstract Cathepsin G is a serine, chymotrypsin-like protease released by activated polymorphonuclear leukocytes (PMN) that may act as a platelet agonist. The effect of this enzyme on platelet surface glycoproteins (Gp) Ib and IIb-IIIa was evaluated by means of a cytofluorimetric assay, using fluorescein isothiocyanate-labeled monoclonal antibodies (MoAbs) directed at the alpha chain of Gp Ib (SZ2), at Gp IX or at the complex Gp IIb-IIIa (P2), and the fibrinogen-receptor-specific MoAb PAC- 1. In human washed platelets, cathepsin G increased the binding of P2 and PAC-1, decreased the binding of

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38

Molino, M., M. Di Lallo, N. Martelli, G. de Gaetano, and C. Cerletti. "Effects of leukocyte-derived cathepsin G on platelet membrane glycoprotein Ib-IX and IIb-IIIa complexes: a comparison with thrombin." Blood 82, no. 8 (1993): 2442–51. http://dx.doi.org/10.1182/blood.v82.8.2442.bloodjournal8282442.

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Cathepsin G is a serine, chymotrypsin-like protease released by activated polymorphonuclear leukocytes (PMN) that may act as a platelet agonist. The effect of this enzyme on platelet surface glycoproteins (Gp) Ib and IIb-IIIa was evaluated by means of a cytofluorimetric assay, using fluorescein isothiocyanate-labeled monoclonal antibodies (MoAbs) directed at the alpha chain of Gp Ib (SZ2), at Gp IX or at the complex Gp IIb-IIIa (P2), and the fibrinogen-receptor-specific MoAb PAC- 1. In human washed platelets, cathepsin G increased the binding of P2 and PAC-1, decreased the binding of SZ2, but

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Mazzucato, Mario, Luigi De Marco, Paola Pradella, Adriana Masotti, and Francesco I. Pareti. "Porcine von Willebrand Factor Binding to Human Platelet GPIb Induces Transmembrane Calcium Influx." Thrombosis and Haemostasis 75, no. 04 (1996): 655–60. http://dx.doi.org/10.1055/s-0038-1650338.

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SummaryPorcine von Willebrand factor (P-vWF) binds to human platelet glycoprotein (GP) lb and, upon stirring (1500 rpm/min) at 37° C, induces, in a dose-dependent manner, a transmembrane flux of Ca2+ ions and platelet aggregation with an increase in their intracellular concentration. The inhibition of P-vWF binding to GP lb, obtained with anti GP lb monoclonal antibody (LJ-Ib1), inhibits the increase of intracellular Ca2+ concentration ([Ca2+]i) and platelet aggregation. This effect is not observed with LJ-Ib10, an anti GP lb monoclonal antibody which does not inhibit the vWF binding to GP lb.

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40

Niiya, K., E. Hodson, R. Bader, et al. "Increased surface expression of the membrane glycoprotein IIb/IIIa complex induced by platelet activation. Relationship to the binding of fibrinogen and platelet aggregation." Blood 70, no. 2 (1987): 475–83. http://dx.doi.org/10.1182/blood.v70.2.475.475.

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Abstract Platelet activation altered the binding of three monoclonal antibodies (monovalent Fab' fragment) directed against the glycoprotein (GP) IIb/IIIa complex. An increased binding of two- to threefold occurred after stimulation with thrombin or phorbol myristate acetate (PMA), with slight but significant increase in the dissociation constants (Kd) of two antibodies (LJ-CP8 and LJ-P9). In contrast, no statistically significant changes were observed with ADP-stimulated platelets. The increased binding of LJ-CP3, but not of the other two antibodies, to activated platelets decreased by 30% to

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41

Niiya, K., E. Hodson, R. Bader, et al. "Increased surface expression of the membrane glycoprotein IIb/IIIa complex induced by platelet activation. Relationship to the binding of fibrinogen and platelet aggregation." Blood 70, no. 2 (1987): 475–83. http://dx.doi.org/10.1182/blood.v70.2.475.bloodjournal702475.

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Platelet activation altered the binding of three monoclonal antibodies (monovalent Fab' fragment) directed against the glycoprotein (GP) IIb/IIIa complex. An increased binding of two- to threefold occurred after stimulation with thrombin or phorbol myristate acetate (PMA), with slight but significant increase in the dissociation constants (Kd) of two antibodies (LJ-CP8 and LJ-P9). In contrast, no statistically significant changes were observed with ADP-stimulated platelets. The increased binding of LJ-CP3, but not of the other two antibodies, to activated platelets decreased by 30% to 40% in t

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42

Bird, Christopher, Marion Callus, Lynne Trickett, and Robin Thorpe. "Immunochemical characterization of a new platelet specific monoclonal antibody and its use to demonstrate the cytoskeletal association of the platelet glycoprotein IIb-IIIa complex." Bioscience Reports 6, no. 3 (1986): 323–33. http://dx.doi.org/10.1007/bf01115162.

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We describe the production and characterization of a monoclonal antibody specific for platelets. This antibody reacts strongly with human and primate platelets, but does not recognise human monocytes, polymorphonuclear leucocytes, lymphocytes, erythrocytes, leukaemic nor fibroblast cell lines, nor rodent platelets. Immunoprecipitation studies using radiolabelled platelet membrane proteins showed that the monoclonal antibody binds to the platelet membrane glycoprotein IIb-IIIa complex. Affinity chromatography using immobilized monoclonal antibody allows purification of the antigen, but also co-

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Abrams, C. S., Z. M. Ruggeri, R. Taub, et al. "Anti-idiotypic antibodies against an antibody to the platelet glycoprotein (GP) IIb-IIIa complex mimic GP IIb-IIIa by recognizing fibrinogen." Journal of Biological Chemistry 267, no. 4 (1992): 2775–85. http://dx.doi.org/10.1016/s0021-9258(18)45946-7.

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Satoh, T., W. C. Kouns, Y. Yamashita, T. Kamiyama, and B. Steiner. "Tetrafibricin, a novel non-peptide fibrinogen receptor antagonist, induces conformational changes in glycoprotein IIb/IIIa." Biochemical Journal 301, no. 3 (1994): 785–91. http://dx.doi.org/10.1042/bj3010785.

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Arg-Gly-Asp (RGD) is an amino acid sequence in fibrinogen recognized by platelet glycoprotein (GP) IIb/IIIa. Recently, it was found that RGD peptide binding to GPIIb/IIIa leads to conformational changes in the complex that are associated with the acquisition of high-affinity fibrinogen-binding function. In this study, we found that tetrafibricin, a novel non-peptidic GPIIb/IIIa antagonist, induced similar conformational changes in GPIIb/IIIa as did RGD peptides. Tetrafibricin increased the binding of purified inactive GPIIb/IIIa to immobilized pl-80, a monoclonal antibody that preferentially r

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45

Meyer, M., and F. H. Herrmann. "Diversity of Glycoprotein Deficiencies in Glanzmann’s Thrombasthenia." Thrombosis and Haemostasis 54, no. 03 (1985): 626–29. http://dx.doi.org/10.1055/s-0038-1660085.

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SummaryThe platelet proteins of 9 thrombasthenic patients from 7 families were analysed by high resolution two-dimensional gel electrophoresis (HR-2DE) and crossed immunoelectrophoresis (CIE). In 7 patients both glycoproteins (GPs) IIb and Ilia were absent or reduced to roughly the same extent. In two related patients only a trace of GP Ilb-IIIa complex was detected in CIE, but HR-2DE revealed a glycopeptide in the position of GP Ilia in an amount comparable to type II thrombasthenia. This GP Ilia-like component was neither recognized normally by anti-GP Ilb-IIIa antibodies nor labeled by surf

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46

Piotrowicz, R. S., R. P. Orchekowski, D. J. Nugent, K. Y. Yamada, and T. J. Kunicki. "Glycoprotein Ic-IIa functions as an activation-independent fibronectin receptor on human platelets." Journal of Cell Biology 106, no. 4 (1988): 1359–64. http://dx.doi.org/10.1083/jcb.106.4.1359.

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Soluble fibronectin binds specifically to glycoprotein (GP) IIb-IIIa on thrombin-activated platelets, and this binding is not observed with platelets of patients with Glanzmann's thrombasthenia (GT) which lack GPIIb-IIIa. Here we report that GT platelets retain the ability to interact with fibronectin-coated surfaces. Adhesion to fibronectin does not require platelet activation and is inhibited by soluble fibronectin, antibodies specific for fibronectin, peptides containing the sequence Arg-Gly-Asp and polyclonal antibodies specific for band 3 of the chicken embryo fibroblast fibronectin recep

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47

Fujimoto, Tetsuro, Kingo Fujimura, and Atsushi Kuramoto. "Functional Ca2+ Channel Produced by Purified Platelet Membrane Glycoprotein IIb-IIIa Complex Incorporated into Planar Phospholipid Bilayer." Thrombosis and Haemostasis 66, no. 05 (1991): 598–603. http://dx.doi.org/10.1055/s-0038-1646466.

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SummaryThe ability of the platelet membrane glycoprotein (GP) IIb-IIIa complex to function as a Ca2+ channel was investigated by electrophysiological methods. The GPIIb-IIIa complex was purified with an electrically silent detergent, CHAPS, and reconstituted into liposomes. After incorporation of these liposomes to a planar phospholipid bilayer, Ba2+-permeable channel currents were detected. Since neither residual detergent nor dissociated GPIIb and IIIa produced any currents, the observed channel currents were attributed to the GPIIb-IIIa complex. These channel currents showed similar electri

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48

Ali, Abbas, Sayani Raza, Muhammad Mustahsan Syed, and Saeed Anwar. "Glanzmann's Thrombasthenia: Role of Angioembolization and factor VII in recurrent bleeding from ulcerated duodenum." International Journal of Endorsing Health Science Research 4, no. 2 (2016): 17–21. https://doi.org/10.29052/IJEHSR.v4.i2.2016.17-21.

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Abstract <strong>Introduction:</strong> Glanzmann’s thrombasthenia (GT) is a rare, genetically inherited, functional disorder of platelets. The pathology is deficient or dysfunctional platelet glycoprotein IIb/IIIa (GP IIb/IIIa) complex resulting in bleeding diathesis. <strong>Case Report:</strong> Here in, we report the effectivity of angioembolization with factor VII in a patient with Glanzmann’s thrombasthenia (GT), who presented with recurrent bleeding from duodenal ulcer. <strong>Conclusion:</strong> Angioembolization with added infusion of factor VII,

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Jallu, Vincent, Marc Meunier, Maryline Brément, and Cécile Kaplan. "A new platelet polymorphism Duva+, localized within the RGD binding domain of glycoprotein IIIa, is associated with neonatal thrombocytopenia." Blood 99, no. 12 (2002): 4449–56. http://dx.doi.org/10.1182/blood.v99.12.4449.

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We report here the identification and characterization of a new platelet alloantigen, Duva+, implicated in a case of neonatal thrombocytopenia. Immunochemical studies demonstrated that the epitope was localized on glycoprotein (GP) IIIa. Sequencing of the exons 2 to 15 of GP IIIa gene polymerase chain reaction products from both parents revealed a single base substitution 517C&gt;T (complementary DNA) present in a heterozygous state in DNA from the father leading to amino acid substitution Thr140Ile (ACC&gt;ATC) within the Arg-Gly-Asp binding domain of GP IIIa. Flow cytometry and immun

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Visentin, GP, PJ Newman, and RH Aster. "Characteristics of quinine- and quinidine-induced antibodies specific for platelet glycoproteins IIb and IIIa." Blood 77, no. 12 (1991): 2668–76. http://dx.doi.org/10.1182/blood.v77.12.2668.2668.

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Abstract Recent studies have shown that antibodies characteristic of quinine- and quinidine-induced thrombocytopenia sometimes recognize the platelet membrane glycoprotein (GP) complex IIb/IIIa in addition to their well known target, GPIb/IX. We have investigated the frequency with which drug-induced antibodies bind to GPIIb/IIIa and the nature of their target epitopes. In studies of sera from 13 patients sensitive to quinidine or quinine, we found that 10 contained IgG antibodies specific for both GPIb/IX and GPIIb/IIIa, two reacted with GPIb/IX alone, and one reacted with GPIIb/IIIa alone. I

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