Literature DB >> 2275816

Platelet membrane glycoproteins: functions in cellular interactions.

N Kieffer1, D R Phillips.   

Abstract

The understanding of the structure and function of platelet membrane glycoproteins has been facilitated by studies showing that they belong to larger gene families of cell surface receptors involved in cellular interactions. In some instances (e.g. GP IIb-IIIa and GP Ib-IX) the study of the platelet proteins has served as a prototype for relatively newly described gene families (e.g. integrins and LRG proteins, respectively). In other instances, e.g. PECAM-1, the background of information on immunoglobulin domain-containing proteins has served to indicate functions. Receptor-ligand interactions have been characterized at the molecular level, and studies of genetic defects affecting platelet receptors have contributed significantly to understanding structure-function relationships. Gene transfection studies provide encouraging results that might lead to gene therapy. The knowledge about platelet ligand-receptor processes contributes not only to our understanding of normal platelet function, but also to a more generalized understanding of adhesive mechanisms used by many cells to interact with their environment.

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Year:  1990        PMID: 2275816     DOI: 10.1146/annurev.cb.06.110190.001553

Source DB:  PubMed          Journal:  Annu Rev Cell Biol        ISSN: 0743-4634


  34 in total

1.  Role of extracellular ionized calcium in the in vitro assessment of GPIIb/IIIa receptor antagonists.

Authors:  S S Rebello; J Huang; J D Faul; B R Lucchesi
Journal:  J Thromb Thrombolysis       Date:  2000-01       Impact factor: 2.300

2.  Proteolytic dissection of the isolated platelet fibrinogen receptor, integrin GPIIb/IIIa. Localization of GPIIb and GPIIIa sequences putatively involved in the subunit interface and in intrasubunit and intrachain contacts.

Authors:  J J Calvete; K Mann; M V Alvarez; M M López; J González-Rodríguez
Journal:  Biochem J       Date:  1992-03-01       Impact factor: 3.857

3.  A new variant of Glanzmann's thrombasthenia (Strasbourg I). Platelets with functionally defective glycoprotein IIb-IIIa complexes and a glycoprotein IIIa 214Arg----214Trp mutation.

Authors:  F Lanza; A Stierlé; D Fournier; M Morales; G André; A T Nurden; J P Cazenave
Journal:  J Clin Invest       Date:  1992-06       Impact factor: 14.808

4.  Constitutive activation of integrin alpha 4 beta 1 defines a unique stage of human thymocyte development.

Authors:  D R Salomon; C F Mojcik; A C Chang; S Wadsworth; D H Adams; J E Coligan; E M Shevach
Journal:  J Exp Med       Date:  1994-05-01       Impact factor: 14.307

5.  p42 mitogen-activated protein kinase and p90 ribosomal S6 kinase are selectively phosphorylated and activated during thrombin-induced platelet activation and aggregation.

Authors:  J Papkoff; R H Chen; J Blenis; J Forsman
Journal:  Mol Cell Biol       Date:  1994-01       Impact factor: 4.272

6.  An inherited bleeding disorder linked to a defective interaction between ADP and its receptor on platelets. Its influence on glycoprotein IIb-IIIa complex function.

Authors:  P Nurden; P Savi; E Heilmann; C Bihour; J M Herbert; J P Maffrand; A Nurden
Journal:  J Clin Invest       Date:  1995-04       Impact factor: 14.808

7.  Characterization of calcium- and integrin-binding protein 1 (CIB1) knockout platelets: potential compensation by CIB family members.

Authors:  Jan C Denofrio; Weiping Yuan; Brenda R Temple; Holly R Gentry; Leslie V Parise
Journal:  Thromb Haemost       Date:  2008-11       Impact factor: 5.249

8.  Calcium and temperature regulation of the stability of the human platelet integrin GPIIb/IIIa in solution: an analytical ultracentrifugation study.

Authors:  G A Rivas; P Usobiaga; J González-Rodriguez
Journal:  Eur Biophys J       Date:  1991       Impact factor: 1.733

9.  A functional integrin ligand on the surface of platelets: intercellular adhesion molecule-2.

Authors:  T G Diacovo; A R deFougerolles; D F Bainton; T A Springer
Journal:  J Clin Invest       Date:  1994-09       Impact factor: 14.808

Review 10.  Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.

Authors:  Allison M Whited; Paul S-H Park
Journal:  Biochim Biophys Acta       Date:  2013-04-16
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