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Volumn 5, Issue 5, 1993, Pages 898-906

Von Willebrand factor and fibrinogen

Author keywords

[No Author keywords available]

Indexed keywords

FIBRIN; FIBRINOGEN; GLYCOPROTEIN; VON WILLEBRAND FACTOR;

EID: 0027448627     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/0955-0674(93)90041-N     Document Type: Article
Times cited : (30)

References (56)
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    • of special interest, This paper demonstrates specific expression in mammalian cells of the functional GP Ib-binding domain of vWF by recombinant technology. This is important for understanding domain assembly and folding and for future structural characterization (unlikely to be achieved with intact vWF due to its size and heterogeneity).
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    • of special interest, The results of this paper and [7⊎] exemplify the uncertainties remaining in understanding the processes leading to vWF storage in endothelial cells. The problem is relevant, because regulated release of vWF upon endothelial stimulation may be involved in pathophysiological mechanisms.
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    • of special interest, This paper and [11⊎] demonstrate a possible mechanism of platelet activation mediated by the initial interaction of vWF with GP Ib under the effect of high shear stress. The two studies present some discrepancies in the results obtained with anti-GP IIb–IIIa antibodies with regard to the role of GP IIb–IIIa in the transmembrane flux of calcium ions in platelets; these may be due to differences in epitope recognition specificity of the antibodies. GP IIb–IIIa may be spatially in proximity of a calcium channel, but not directly involved with transmembrane calcium transport.
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    • Analysis of Structure-Function Relationship in the Platelet Membrane Glycoprotein Ib-Binding Domain of von Willebrand Factor by Expression of Deletion Mutants
    • of special interest, This paper defines the minimal structures in the A1 domain capable of providing high affinity interaction with GP Ib. Interesting comparison with the results obtained with smaller synthetic peptides (see [23⊎]).
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    • A Role for von Willebrand Factor Proline Residues 702–704 in Ristocetin-Mediated Binding to Platelet Glycoprotein Ib
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    • Identification of Aspartic Acid 514 Through Glutamic Acid 542 as a Glycoprotein Ib-IX Complex Receptor Recognition Sequence in von Willebrand Factor. Mechanisms of Modulation of von Willebrand Factor by Ristocetin and Botrocetin
    • of special interest, This paper is important as it describes the identification of a limited sequence likely to contain residues involved in binding to the GP Ib receptor. Compare the affinity of interaction of the small synthetic peptides with that of larger recombinant fragments described in [18⊎].
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    • 1746 Sequence in the GPIIb–IIIa-Binding Domain of von Willebrand Factor is Involved in Platelet Adhesion and Thrombus Formation on Subendothelium
    • in press
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    • Biosynthesis of Human Fibrinogen
    • of special interest, Describes relevant experiments on the complex issue of fibrinogen biosynthesis.
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    • of special interest, Convincing visual demonstration of the spatial relationships of important domains in fibrinogen.
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    • Molecular Basis of Fibrinogen Naples Associated with Defective Thrombin Binding and Thrombophilia
    • of special interest, Another relevant study of a case of dysfibrinogenemia (see [40⊎]). The findings are relevant to understanding the structural requirements for thrombin interaction with fibrinogen. Moreover, the study demonstrates the complex regulation of coagulation at a site of vascular lesion by providing evidence that thrombin binding to fibrin is a crucial regulatory mechanism preventing physiologic hemostasis from turning into a dangerous prothrombotic event.
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    • Homocysteine and Other Sulfhydryl Compounds Enhance the Binding of Lipoprotein(a) to Fibrin: a Potential Biochemical Link Between Thrombosis, Atherogenesis, and Sulfhydryl Compound Metabolism
    • of special interest, An intriguing report linking the metabolism of sulfhydryl compounds to the interactions between coagulation mechanisms and lipid environment in blood, with the possibility of ultimate effects on the development of atherosclerosis and acute thrombosis. This is obviously an area of possible significant developments.
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    • Fibrinogen as a Cardiovassular Risk Factor: A Meta-Analysis and Review of the Literature
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    • 3: Induction of Calcium Oscillations Required for Protein-Tyrosine Phosphorylation Ligand-Induced Spreading of Stably Transfected Cells
    • of special interest, A paper contributing to a rapidly evolving area of research: the role of tyrosine kinases and their substrates in cell adhesion mechanisms.
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    • Pelletier1    Bodary2    Levinson3
  • 50
    • 0026476365 scopus 로고
    • Role of Fibrinogen α and Gamma Chain Sites in Platelet Aggregation
    • of special interest, Good reading to appreciate that the results provided by small synthetic peptides may not reflect the functional role of the corresponding sequences in a macromolecule. Indeed, while peptides containing the sequence Arg-Gly-Asp block GP IIb–IIIa receptor function, the same sequence occurring twice in fibrinogen may have little to do with how fibrinogen binds to platelets.
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    • Farrell1    Thiagarajan2    Chung3    Davie4
  • 51
    • 0027215042 scopus 로고
    • Spreading of Platelets on Fibrin is Mediated by the Amino Terminus of the Chain Including Peptide 15–42
    • (1993) Blood , vol.81 , pp. 2348-2356
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  • 53
    • 0027318675 scopus 로고
    • Fibrinogen Mediates Leukocyte Adhesion to Vascular Endothelium Through an ICAM-1-Dependent Pathway
    • of outstanding interest, Good set of experiments demonstrating a new function for ICAM-1 as a fibrinogen receptor. Intriguing from the conceptual point of view: the same pair of receptors on endothelial cells and leukocytes (ICAM-1 and Mac-1, respectively) may function with or without interposition of fibrinogen in supporting leukocyte adhesion to endothelium. The relative importance of the two mechanisms, and their possible distinct roles, remain to be clarified.
    • (1993) Cell , vol.73 , pp. 1423-1434
    • Languino1    Plescia2    Duperray3    Brian4    Plow5    Geltosky6    Altieri7
  • 54
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    • Mβ, Mac-1) and Promotes Leukocyte Adhesion
    • of special interest, Those studies characterize a distinct functional site in fibrinogen supporting interaction with leukocytes. Similar studies will have to be done to identify the fibrinogen sequence(s) involved in binding to ICAM-1 on endothelial cells (see annotation to [53⊎⊎]).
    • (1993) J Biol Chem , vol.68 , pp. 1847-1853
    • Altieri1    Plescia2    Plow3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.