The tetrapeptide analogue of the cell attachment site of fibronectin inhibits platelet aggregation and fibrinogen binding to activated platelets.
T K Gartner,J S Bennett +1 more
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TLDR
The data suggest that a region near the carboxyl-terminus of the alpha-chain of fibrinogen interacts with the fibrInogen receptor on activated platelets, and support the concept that the sequence Arg-Gly-Asp-Ser has been conserved for use in a variety of cellular adhesive processes.About:
This article is published in Journal of Biological Chemistry.The article was published on 1985-10-05 and is currently open access. It has received 431 citations till now. The article focuses on the topics: Fibrinogen receptor & Fibrinogen binding.read more
Citations
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New perspectives in cell adhesion : RGD and integrins
TL;DR: Together, the adhesion proteins and their receptors constitute a versatile recognition system providing cells with anchorage, traction for migration, and signals for polarity, position, differentiation, and possibly growth.
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RGD and other recognition sequences for integrins.
TL;DR: As the integrin-mediated cell attachment influences and regulates cell migration, growth, differentiation, and apoptosis, the RGD peptides and mimics can be used to probe integrin functions in various biological systems.
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The platelet membrane glycoprotein IIb-IIIa complex
TL;DR: The author’s website is www.hematologylibrary.org, which can be found online at http://bloodjournal.org/site/misc/rights.xhtml.
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Platelet membrane glycoprotein IIb/IIIa: member of a family of Arg-Gly-Asp--specific adhesion receptors
TL;DR: The results establish the existence of a family of adhesion receptors that recognize the sequence Arg-Gly-Asp, which corresponds to the cell adhesion site in fibronectin and is also present in the alpha chain of fibrinogen.
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Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion.
TL;DR: These studies lend support to the hypothesis that different Arg-Gly-Asp-directed adhesion receptors can recognize differences in the conformation and environment of the Arg- Gly- asp tripeptide, and they establish the feasibility of obtaining synthetic probes that are more selective for individual receptors than are the peptides modeled after the natural sequences of adhesive extracellular matrix molecules.
References
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Aggregation of blood platelets by adenosine diphosphate and its reversal.
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Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
TL;DR: The ability of fibronectin to bind cells can be accounted for by the tetrapeptide L-arginyl-glycyl- L-aspartyl-L-serine, a sequence which is part of the cell attachment domain of fibronsectin and present in at least five other proteins.
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Fibronectins: multifunctional modular glycoproteins.
TL;DR: The current understanding of the structure and properties of fibronectins is reviewed to focus on overall concepts, recent developments and promising future research directions in this rapidly expanding field.
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Exposure of platelet fibrinogen receptors by ADP and epinephrine.
Joel S. Bennett,Gaston Vilaire +1 more
TL;DR: It is demonstrated that platelet stimulation by ADP and epinephrine exposes a limited number of fibrinogen receptors on the platelet surface, and data suggest that the fibrInogen molecules bound to the Platelet as a consequence of Platelet stimulation are directly involved in the platelets aggregation response.