ArticleBiochemistry2010
Dynamic regulation of fibrinogen: integrin αIIbβ3 binding.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Fibrinogen in extracellular matrix remodeling: functional switching, source heterogeneity, and biomaterial translation.Frontiers in cell and developmental biology · 2026Review
- Platelet integrin αIIbβ3 plays a key role in a venous thrombogenesis mouse model.Nature communications · 2024Article
- Platelet Biorheology and Mechanobiology in Thrombosis and Hemostasis: Perspectives from Multiscale Computation.International journal of molecular sciences · 2024Review
- Crosstalk between Circulating Tumor Cells and Plasma Proteins-Impact on Coagulation and Anticoagulation.Cancers · 2023Review
- The myokine Fibcd1 is an endogenous determinant of myofiber size and mitigates cancer-induced myofiber atrophy.Nature communications · 2022Article
- Quantitative Proteomic Study Unmasks Fibrinogen Pathway in Polycystic Liver Disease.Biomedicines · 2022Article
- [Effects of material interfaces on orientation and function of fibrinogen].Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2021Article
- Review
- αIIbβ3 binding to a fibrinogen fragment lacking the γ-chain dodecapeptide is activation dependent and EDTA inducible.Blood advances · 2017Article
- The Platelet Integrin αIIbβ3 Differentially Interacts with Fibrin Versus Fibrinogen.The Journal of biological chemistry · 2016Article
- Article
- Alkylation of human hair keratin for tunable hydrogel erosion and drug delivery in tissue engineering applications.Acta biomaterialia · 2015Article
- The interaction of integrin αIIbβ3 with fibrin occurs through multiple binding sites in the αIIb β-propeller domain.The Journal of biological chemistry · 2014Article
- Elevating local concentrations of GPIIb-IIIa antagonists counteracts platelet thrombus stability.Journal of thrombosis and thrombolysis · 2013Article
- PROBINGNano LIFE · 2013Article
- Structural and functional characterization of monomeric EphrinA1 binding site to EphA2 receptor.The Journal of biological chemistry · 2012Article
- A2 adenosine receptors and vascular pathologies.Arteriosclerosis, thrombosis, and vascular biology · 2012Review
- Structure-guided design of a high-affinity platelet integrin αIIbβ3 receptor antagonist that disrupts Mg²⁺ binding to the MIDAS.Science translational medicine · 2012Article
- Adenosine and blood platelets.Purinergic signalling · 2011Article
- Transmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K⁺ channels, and integrin receptors.Annual review of biochemistry · 2011Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
This study demonstrates that two orthogonal events regulate integrin αIIbβ3's interactions with fibrinogen, its primary physiological ligand: (1) conformational changes at the αIIb-β3 interface and (2) flexibility in the carboxy terminus of fibrinogen's γ-module. The first postulate was tested by capturing αIIbβ3 on a biosensor and measuring binding by surface plasmon resonance. Binding of fibrinogen to eptifibatide-primed αIIbβ3 was characterized by a k(on) of ~2 × 10(4) L mol(-1) s(-1) and a k(off) of ~8 × 10(-5) s(-1) at 37 °C. In contrast, even at 150 nM fibrinogen, no binding was detected with resting αIIbβ3. Eptifibatide competitively inhibited fibrinogen's interactions with primed αIIbβ3 (K(i) ~0.4 nM), while a synthetic γ-module peptide (HHLGGAKQAGDV) was only weakly inhibitory (K(i) > 10 μM). The second postulate was tested by measuring αIIbβ3's interactions with recombinant fibrinogen, both normal (rFgn) and a deletion mutant lacking the γ-chain AGDV sites (rFgn γΔ408-411). Normal rFgn bound rapidly, tightly, and specifically to primed αIIbβ3; no interaction was detected with rFgn γΔ408-411. Equilibrium and transition-state thermodynamic data indicated that binding of fibrinogen to primed αIIbβ3, while enthalpy-favorable, must overcome an entropy-dominated activation energy barrier. The hypothesis that fibrinogen binding is enthalpy-driven fits with structural data showing that its γ-C peptide and eptifibatide exhibit comparable electrostatic contacts with αIIbβ3's ectodomain. The concept that fibrinogen's αIIbβ3 targeting sequence is intrinsically disordered may explain the entropy penalty that limits its binding rate. In the hemostatic milieu, platelet-platelet interactions may be localized to vascular injury sites because integrins must be activated before they can bind their most abundant ligand.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.