دورية أكاديمية
GPVI (Glycoprotein VI) Interaction With Fibrinogen Is Mediated by Avidity and the Fibrinogen αC-Region.
| العنوان: | GPVI (Glycoprotein VI) Interaction With Fibrinogen Is Mediated by Avidity and the Fibrinogen αC-Region. |
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| المؤلفون: | Xu RG; Discovery and Translational Science Department, Institute of Cardiovascular and Metabolic Medicine (R.-G.X., J.S.G., S.R.B., H.R.M., C.D., R.A.S.A.)., Gauer JS; Discovery and Translational Science Department, Institute of Cardiovascular and Metabolic Medicine (R.-G.X., J.S.G., S.R.B., H.R.M., C.D., R.A.S.A.)., Baker SR; Discovery and Translational Science Department, Institute of Cardiovascular and Metabolic Medicine (R.-G.X., J.S.G., S.R.B., H.R.M., C.D., R.A.S.A.).; Department of Physics, Wake Forest University, Winston Salem, NC (S.R.B.)., Slater A; Institute of Cardiovascular Sciences, College of Medical and Dental Sciences, University of Birmingham, United Kingdom (A.S., E.M.M., S.P.W.)., Martin EM; Institute of Cardiovascular Sciences, College of Medical and Dental Sciences, University of Birmingham, United Kingdom (A.S., E.M.M., S.P.W.)., McPherson HR; Discovery and Translational Science Department, Institute of Cardiovascular and Metabolic Medicine (R.-G.X., J.S.G., S.R.B., H.R.M., C.D., R.A.S.A.)., Duval C; Discovery and Translational Science Department, Institute of Cardiovascular and Metabolic Medicine (R.-G.X., J.S.G., S.R.B., H.R.M., C.D., R.A.S.A.)., Manfield IW; School of Molecular and Cellular Biology, Faculty of Biological Sciences (I.W.M.), University of Leeds, United Kingdom., Bonna AM; Department of Biochemistry, University of Cambridge, United Kingdom (A.M.B.)., Watson SP; Institute of Cardiovascular Sciences, College of Medical and Dental Sciences, University of Birmingham, United Kingdom (A.S., E.M.M., S.P.W.)., Ariëns RAS; Discovery and Translational Science Department, Institute of Cardiovascular and Metabolic Medicine (R.-G.X., J.S.G., S.R.B., H.R.M., C.D., R.A.S.A.). |
| المصدر: | Arteriosclerosis, thrombosis, and vascular biology [Arterioscler Thromb Vasc Biol] 2021 Mar; Vol. 41 (3), pp. 1092-1104. Date of Electronic Publication: 2021 Jan 21. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Lippincott Williams & Wilkins Country of Publication: United States NLM ID: 9505803 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1524-4636 (Electronic) Linking ISSN: 10795642 NLM ISO Abbreviation: Arterioscler Thromb Vasc Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 1998- : Baltimore, Md. : Lippincott Williams & Wilkins Original Publication: Dallas, TX : American Heart Association, c1995- |
| مواضيع طبية MeSH: | Fibrinogen/*metabolism , Peptide Fragments/*blood , Platelet Membrane Glycoproteins/*metabolism, Animals ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Fibrin Fibrinogen Degradation Products/chemistry ; Fibrin Fibrinogen Degradation Products/metabolism ; Fibrinogen/chemistry ; Humans ; In Vitro Techniques ; Mice ; Microscopy, Atomic Force ; Peptide Fragments/chemistry ; Peptides/chemistry ; Peptides/metabolism ; Platelet Aggregation/physiology ; Platelet Membrane Glycoproteins/chemistry ; Protein Interaction Domains and Motifs ; Protein Structure, Quaternary ; Signal Transduction ; Surface Plasmon Resonance |
| مستخلص: | Objective: GPVI (glycoprotein VI) is a key molecular player in collagen-induced platelet signaling and aggregation. Recent evidence indicates that it also plays important role in platelet aggregation and thrombus growth through interaction with fibrin(ogen). However, there are discrepancies in the literature regarding whether the monomeric or dimeric form of GPVI binds to fibrinogen at high affinity. The mechanisms of interaction are also not clear, including which region of fibrinogen is responsible for GPVI binding. We aimed to gain further understanding of the mechanisms of interaction at molecular level and to identify the regions on fibrinogen important for GPVI binding. Approach and Results: Using multiple surface- and solution-based protein-protein interaction methods, we observe that dimeric GPVI binds to fibrinogen with much higher affinity and has a slower dissociation rate constant than the monomer due to avidity effects. Moreover, our data show that the highest affinity interaction of GPVI is with the αC-region of fibrinogen. We further show that GPVI interacts with immobilized fibrinogen and fibrin variants at a similar level, including a nonpolymerizing fibrin variant, suggesting that GPVI binding is independent of fibrin polymerization. Conclusions: Based on the above findings, we conclude that the higher affinity of dimeric GPVI over the monomer for fibrinogen interaction is achieved by avidity. The αC-region of fibrinogen appears essential for GPVI binding. We propose that fibrin polymerization into fibers during coagulation will cluster GPVI through its αC-region, leading to downstream signaling, further activation of platelets, and potentially stimulating clot growth. Graphic Abstract: A graphic abstract is available for this article. |
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| معلومات مُعتمدة: | 204951 United Kingdom WT_ Wellcome Trust; 204951/B/16/Z United Kingdom WT_ Wellcome Trust; 062164/Z00/Z United Kingdom WT_ Wellcome Trust; 204951/Z/16/Z United Kingdom WT_ Wellcome Trust; CH/03/003/15571 United Kingdom BHF_ British Heart Foundation |
| فهرسة مساهمة: | Keywords: fibrin; fibrinogen; glycoprotein VI; platelet aggregation; thrombosis |
| المشرفين على المادة: | 0 (Carrier Proteins) 0 (Fibrin Fibrinogen Degradation Products) 0 (Peptide Fragments) 0 (Peptides) 0 (Platelet Membrane Glycoproteins) 0 (collagen-related peptide) 0 (fibrin fragment D) 0 (fibrinogen alphaC) 0 (platelet membrane glycoprotein VI) 9001-32-5 (Fibrinogen) |
| تواريخ الأحداث: | Date Created: 20210121 Date Completed: 20210315 Latest Revision: 20220302 |
| رمز التحديث: | 20221213 |
| مُعرف محوري في PubMed: | PMC7901536 |
| DOI: | 10.1161/ATVBAHA.120.315030 |
| PMID: | 33472402 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1524-4636 |
|---|---|
| DOI: | 10.1161/ATVBAHA.120.315030 |