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  • Fujita, Shigeru  (4)
  • 1995-1999  (4)
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  • 1995-1999  (4)
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Subjects(RVK)
  • 1
    Online Resource
    Online Resource
    A Novel Mechanism for Exposure of Fibrinogen Binding Sites on GPIIb-IIIa by a Monoclonal Antibody
    Georg Thieme Verlag KG ; 1995
    In:  Thrombosis and Haemostasis Vol. 73, No. 01 ( 1995), p. 138-143
    Details
    In: Thrombosis and Haemostasis, Georg Thieme Verlag KG, Vol. 73, No. 01 ( 1995), p. 138-143
    Abstract: Conformational changes in platelet membrane glycoprotein (GP) IIb-IIIa, whose nature is not defined, lead to exposure of fibrinogen binding sites. We have reported previously that F(ab’)2fragments of a monoclonal antibody, PMA4, directed against the GPIIb-IIIa complex- specific domain, induced binding of fibrinogen to platelets without causing intracellular activation, whereas Fab did not. In this study, we examined the mechanism responsible for the difference in the ability of PMA4 F(ab’)2and Fab to expose fibrinogen binding sites. PMA4 Fab had affinity for GPIIb-IIIa similar to that of PMA4 F(ab’)2. Addition of F(ab’)2goat anti-mouse Fab antibody to cross-link PMA4 Fab-bound GPIIb-IIIa molecules induced fibrinogen binding. There was a direct correlation between the number of molecules of PMA4 F(ab’)2and the amount of fibrinogen bound. PMA4 did not recognize ligand-induced binding sites (LIBS). These results suggest that the cross-linking of special sites on the GPIIb-IIIa complex-specific domain by bivalent antibody alters the conformation of GPIIb-IIIa to a state competent to bind soluble fibrinogen and that conformational changes in non-LIBS are involved in the mechanism for exposing fibrinogen binding sites on GPIIb-IIIa.
    Type of Medium: Online Resource
    ISSN: 0340-6245 , 2567-689X
    URL: Article
    DOI: 10.1055/s-0038-1653739
    Language: English
    Publisher: Georg Thieme Verlag KG
    Publication Date: 1995
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    Online Resource
  • 2
    Online Resource
    Online Resource
    Differential Inhibition of Fibrinogen Binding to Agonist-and RGDS Peptide-activated States of GPIIb-IIIa by an anti-GPIIIa Monoclonal Antibody, PMA5
    Georg Thieme Verlag KG ; 1996
    In:  Thrombosis and Haemostasis Vol. 76, No. 06 ( 1996), p. 1030-1037
    Details
    In: Thrombosis and Haemostasis, Georg Thieme Verlag KG, Vol. 76, No. 06 ( 1996), p. 1030-1037
    Abstract: Platelet agonists and RGD-containing peptides can convert platelet membrane glycoprotein (GP) Ilb-IIIa from its resting state to an activated state competent to bind soluble fibrinogen. We examined the effects of two anti-GPIIb-IIIa monoclonal antibodies, PMA1 and PMA5, on fibrinogen binding to agonist- and RGD-activated GPIIb-IIIa. PMA1 abolished aggregation of both agonist- and RGDS peptide-activated fixed platelets, and inhibited the binding of 125I-fibrinogen to these platelets almost completely. PMA5 had the same effects on agonist-activated platelets, but had little effect on the aggregation of RGDS-activated fixed platelets, and inhibited fibrinogen binding to RGDS-activated fixed platelets by only 44%. PMA5 bound to agonist- and RGDS-activated platelets equally. Immunoblot analysis showed that PMA5 bound to intact GPIIIa, but not to a 66 kDa fragment of GPIIIa digested by chymotrypsin. Although PMA5 inhibited platelet adhesion to immobilized fibrinogen by 94%, 44% of the remaining adherent platelets were spread. In contrast, no platelet spreading was observed in the presence of PMA1. These findings indicate that PMA5 is a novel anti-GPIIIa monoclonal antibody with the ability to inhibit fibrinogen binding to agonist- and RGD-activated states of GPIIb-IIIa differentially, and suggest that binding of immobilized fibrinogen to RGD-activated GPIIb-IIIa is necessary for platelet spreading.
    Type of Medium: Online Resource
    ISSN: 0340-6245 , 2567-689X
    URL: Article
    DOI: 10.1055/s-0038-1650703
    Language: English
    Publisher: Georg Thieme Verlag KG
    Publication Date: 1996
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  • 3
    Online Resource
    Online Resource
    Polymorphisms of HPA-1 Through 6 on Platelet Membrane Glycoprotein Receptors Are Not a Genetic Risk Factor for Myocardial Infarction in the Japanese Population
    Elsevier BV ; 1997
    In:  The American Journal of Cardiology Vol. 80, No. 9 ( 1997-11), p. 1222-1224
    Details
    In: The American Journal of Cardiology, Elsevier BV, Vol. 80, No. 9 ( 1997-11), p. 1222-1224
    Type of Medium: Online Resource
    ISSN: 0002-9149
    URL: Article
    DOI: 10.1016/S0002-9149(97)00645-0
    RVK:
    XA 18500
    Language: English
    Publisher: Elsevier BV
    Publication Date: 1997
    detail.hit.zdb_id: 2019595-3
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  • 4
    Online Resource
    Online Resource
    Detection of Platelet Adhesion/Aggregation to Immobilized Ligands on Microbeads by an Aggregometer
    Georg Thieme Verlag KG ; 1996
    In:  Thrombosis and Haemostasis Vol. 76, No. 06 ( 1996), p. 1072-1079
    Details
    In: Thrombosis and Haemostasis, Georg Thieme Verlag KG, Vol. 76, No. 06 ( 1996), p. 1072-1079
    Abstract: Platelet aggregation is believed to follow platelet adhesion to vascular injury sites. We have developed a turbidimetric assay for platelet aggregation following platelet adhesion to immobilized ligands using an aggregometer. The addition of polystyrene beads coated with von Willebrand factor (vWF) or fibrinogen (Fg) to platelet suspensions caused prompt aggregation of beads and platelets, which was detected as an increase in light transmission. Electron microscopic analysis revealed that platelets adhered to the bead surfaces and that additional platelets adhered to already adhering platelets, leading to the formation of platelet aggregates. vWF-coated beads induced larger aggregates than Fg-coated beads. The interaction of vWF-coated beads with platelets was abolished by both GPIb and GPIIb-IIIa blockers, while that of Fg-coated beads was abolished by GPIIb-IIIa blockers. vWF-coated beads induced modest secretion of granules from platelets but no thromboxane B2 synthesis. Fg-coated beads induced neither reaction. However, pleckstrin phosphorylation and protein tyrosine phosphorylation was induced by both types of bead. Platelet aggregation following platelet adhesion to both types of bead was inhibited by ADP scavengers, a protein kinase C inhibitor and a tyrosine kinase inhibitor, but not by aspirin. These findings suggest that vWF- and Fg-coated beads can induce platelet aggregation following platelet adhesion through specific ligand-receptor interactions and intracellular signaling. Our simple assay using these beads may represent a useful test for immobilized ligand-induced platelet adhesion and aggregation.
    Type of Medium: Online Resource
    ISSN: 0340-6245 , 2567-689X
    URL: Article
    DOI: 10.1055/s-0038-1650708
    Language: English
    Publisher: Georg Thieme Verlag KG
    Publication Date: 1996
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