Differential Structural Requirements for Fibrinogen Binding to Platelets and to Endothelial Cells

The cytoadhesins represent a group of RGD receptors that belongs to the integrin superfamily of adhesion molecules. Members of this cytoadhesin family include the platelet GPIIb-IIIa and the vitronectin receptors. These glycoproteins share the same β-subunit, which is associated with different α sub...

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Bibliographic Details
Published in:The Journal of cell biology 1989-06, Vol.108 (6), p.2519-2527
Main Authors: Tranqui, Léone, Andrieux, Annie, Hudry-Clergeon, Gilbert, Ryckewaert, Jean-Jacques, Soyez, Serge, Chapel, Agnès, Ginsberg, Mark H., Plow, Edward F., Marguerie, Gérard
Format: Article
Language:English
Subjects:
Actin Cytoskeleton - ultrastructure
Adhesives
Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Binding, Competitive
Biological and medical sciences
Blood Platelets - metabolism
Cell Adhesion
Cells
Endothelial cells
endothelium
Endothelium, Vascular - metabolism
Fibrinogen - metabolism
Fibrosis
Fundamental and applied biological sciences. Psychology
Glycoproteins
Humans
In Vitro Techniques
Ligands
Oligopeptides - metabolism
Platelet Aggregation
Platelet Membrane Glycoproteins - metabolism
Platelets
Plows
Proteins
Receptors
Solubility
Structure-Activity Relationship
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Summary:The cytoadhesins represent a group of RGD receptors that belongs to the integrin superfamily of adhesion molecules. Members of this cytoadhesin family include the platelet GPIIb-IIIa and the vitronectin receptors. These glycoproteins share the same β-subunit, which is associated with different α subunits to form an α/β heterodimer. In the present study, we have analyzed the fine recognition specificity of the cytoadhesins from platelets and endothelial cells for the adhesive protein, fibrinogen. Two sets of synthetic peptides, RGDX peptides and peptides corresponding to the COOH terminus of the fibrinogen γ chain, were compared for their structure-function relationships in the two cellular systems. The results indicate that: (a) both RGDX and γ-chain peptides inhibit the binding of fibrinogen to platelets and endothelial cells; (b) a marked influence of the residue at the COOH- and NH2-terminal positions of each peptide set can be demonstrated on the two cell types; and (c) RGDX and γ peptides have differential effects on platelets and endothelial cells with respect to fine structural requirements. These results clearly indicate that while the platelet and endothelial cytoadhesins may interact with similar peptidic sequences, they express a different fine structural recognition.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.108.6.2519