Complex formation of platelet membrane glycoproteins IIb and IIIa with fibrinogen.

Nachman, Ralph L.; Leung, Lawrence L.K.

doi:10.1172/jci110448

Cited by 322 publications

(125 citation statements)

References 28 publications

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“…Agonist-induced platelet aggregation is dependent on the binding of fibrinogen to GPIIb/IIIa on platelet surface membrane (Gogstad et al 1982;Nachman and Leung 1982) and ristocetin-induced platelet agglutination depends on the interaction GPIb and vWF (Gralnick and Coller 1977). However, it is uncertain whether the major membrane glycoproteins such as GPIb and GPIIb/IIIa are involved in CIPA.…”

Section: Discussionmentioning

confidence: 99%

The Mechanism of Cold-Induced Platelet Aggregation in the Presence of Heparin.

Akiyama

Takami

Yoshida

1995

Tohoku J. Exp. Med.

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Section: Discussionmentioning

confidence: 99%

The Mechanism of Cold-Induced Platelet Aggregation in the Presence of Heparin.

Akiyama

Takami

Yoshida

1995

Tohoku J. Exp. Med.

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“…The interaction of Fbg with activated platelets occurs primarily through the integrin receptor complex, glycoprotein (GP) IIb-IIIa (cqIbP3; 19,241. Two different classes of sites within the Fbg molecule have been reported to be involved in its recognition by GP IIb-IIIa.…”

mentioning

confidence: 99%

Fluorescein derivatization of fibrinogen for flow cytometric analysis of fibrinogen binding to platelets

et al. 1994

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Dog and human fibrinogen were derivatized with N-hydroxysuccinimidofluorescein and utilized for flow cytometric estimation of fibrinogen binding to activated platelets. Fluorescein-fibrinogen binding fulfilled the criteria for specific binding to platelets; the binding was saturable, dependent on agonist activation, and inhibited by unlabeled fibrinogen. In addition, EDTA and barbourin, a KGD-containing peptide, were found to inhibit the binding of fluorescein-fibrinogen. Fluorescein-fibrinogen bound to dog platelets with an apparent affinity of 0.31 p M after stimulation with either adenosine-5'-diphosphate (ADP) or plateletactivating factor. The labeled fibrinogen was also used to study the fibrinogen binding capacity of aged, biotinylated platelets. Aged platelets were indistinguishable from young platelets with regard to fibrinogen binding in response to ADP. These studies document that direct derivatization of fibrinogen with fluorescein generates a useful probe for analyzing fibrinogen binding to platelets with flow CytOmetry. 0 1994 Wiley-Liss, Inc.Key terms: Protein labeling, fluorescent tag, activated platelets, N-hydroxysuccinimido-fluorescein Fibrinogen (Fbg) is a multimeric, 340 kDa plasma protein required for platelet aggregation and clot formation; the critical nature of the fibrinogenlplatelet interaction is indicated by the bleeding tendency of patients deficient in platelet receptors responsible for fibrinogen binding (for review, see 18). The interaction of Fbg with activated platelets occurs primarily through the integrin receptor complex, glycoprotein (GP) IIb-IIIa (cqIbP3; 19,241. Two different classes of sites within the Fbg molecule have been reported to be involved in its recognition by GP IIb-IIIa. Kloczewiak et al. (13) identified the carboxy-terminal sequence on the gamma chain, y406-411, as the minimum sequence mediating Fbg binding to platelets. In addition, the Aa-chain has two RGD sequences, a recognized ligand for the integrin receptor family (1 1). The gamma chain and RGD sequences of Fbg appear to share a common binding site on glycoprotein , and synthetic peptides corresponding to these sequences can inhibit Fbg binding to platelets (27) and platelet aggregation (6). Recent observations suggest that the gamma chain dodecapeptide is responsible for the initial interaction of Fbg with activated GP IIb-IIIa (7) and that the RGD sequences might be more specifically involved in postreceptor occupancy events (26,301.The binding of Fbg to activated platelets has traditionally been analyzed with radiolabeled Fbg. Such studies document that approximately 50,000 binding sites are present on fully activated human platelets with a n apparent affinity of 0.18 pM and that this binding is totally inhibited by EDTA (25). In addition, there are several reports in the literature utilizing fluorescein isothiocyanate (FITCI-labeled anti-Fbg antibodies to detect bound fibrinogen on activated platelets by flow cytometry (FCM). These techniques have not enjoyed widespread acceptance and are complicat...

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“…Platelet glycoproteins Ilb and lIla are highly specific for megakaryocytic cells. These glycoproteins are able to form heterodimer complexes that are involved in the mechanism of platelet aggregation and in the expression of fibrinogen receptors (34,35). To further identify JB-transformed BMCs, we used monoclonal antibodies directed against gpIIbIIIa complexes (21).…”

Section: Expresson Of Platelet Glycoproteins In Jb-transformedmentioning

confidence: 99%

v-jun cooperates with v-erbB to transform the thrombocytic/megakaryocytic lineage.

Garcia

Samarut

1993

Proc. Natl. Acad. Sci. U.S.A.

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The transforming properties of v-jun, the viral counterpart of the transcription factor AP1, were investgated in avian hematopoletic cells. Two retroviruses, called JB and JBN, expressing both v-jun and v-erbB, were constructed using an avian erythroblastosls-based vector. We show that the cooperative action of both oncogenes allowed the virus to efficiently transform bone marrow cells. No such transformation was obtained with either oncogene alone. JBtransformed bone marrow cells expressed GATA-1, TAL-1, and histone H5, suggesting that they belong to the erythrocytic/thrombocytic llneage. (Thrombocytes are the avian homologues of mammal megakaryocytes.) Moreover, after induction with phorbol 12-myristate 13-acetate JB-trnformed bone marrow cells began to differentiate and synthesized hig levels of platelet glycoproteins, indicating that they were of thrombocytic origin. These results were confirmed by c-etsl analysis since this transcription factor, specifically found in cells with megakaryocytic but not erythrocytic features, was clearly detected in these cells.

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Complex formation of platelet membrane glycoproteins IIb and IIIa with fibrinogen.

Cited by 322 publications

References 28 publications

The Mechanism of Cold-Induced Platelet Aggregation in the Presence of Heparin.

The Mechanism of Cold-Induced Platelet Aggregation in the Presence of Heparin.

Fluorescein derivatization of fibrinogen for flow cytometric analysis of fibrinogen binding to platelets

v-jun cooperates with v-erbB to transform the thrombocytic/megakaryocytic lineage.

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