ArticleThe Journal of experimental medicine2003
Targeting platelet-leukocyte interactions: identification of the integrin Mac-1 binding site for the platelet counter receptor glycoprotein Ibalpha.
Article in The Journal of experimental medicine, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 116 citations in OpenAlex.
- Targeting the interactions between neutrophils and microglia: a novel strategy for anti-inflammatory treatment of stroke.Acta pharmacologica Sinica · 2026Review
- Immobilized IgG-containing immune complexes require platelets to recruit neutrophils during inflammation.The Journal of clinical investigation · 2026Article
- Integrin-Mediated Leukocyte Recruitment in Atherosclerosis: A Mechanistic Review of β2 Integrins and VLA-4 Signaling Pathways.Journal of inflammation research · 2026Review
- Casein kinase I isoforms contribute to platelet activation and thrombogenesis via RIPK3-MLKL signaling.Communications biology · 2025Article
- 1,8-Cineole inhibits platelet-leukocyte aggregate formation by reducing P-selectin expression.Frontiers in pharmacology · 2025Article
- Integrin αM promotes macrophage alternative M2 polarization in hyperuricemia-related chronic kidney disease.MedComm · 2024Article
- Neutrophil Extracellular DNA Traps in Response to Infection or Inflammation, and the Roles of Platelet Interactions.International journal of molecular sciences · 2024Review
- The role of platelets in sepsis: A review.Biomolecules & biomedicine · 2024Review
- Unraveling the Intricate Web: Complement Activation Shapes the Pathogenesis of Sepsis-Induced Coagulopathy.Journal of innate immunity · 2024Review
- The role of platelets in immune-mediated inflammatory diseases.Nature reviews. Immunology · 2023Review
- Exploring the Role of Serotonin as an Immune Modulatory Component in Cardiovascular Diseases.International journal of molecular sciences · 2023Review
- Coagulation Disorders in Sepsis and COVID-19-Two Sides of the Same Coin? A Review of Inflammation-Coagulation Crosstalk in Bacterial Sepsis and COVID-19.Journal of clinical medicine · 2023Review
- Platelet-monocyte aggregates: molecular mediators of thromboinflammation.Frontiers in cardiovascular medicine · 2023Review
- Platelet Extracellular Vesicles: Beyond the Blood.Arteriosclerosis, thrombosis, and vascular biology · 2021Review
- The Promiscuous Profile of Complement Receptor 3 in Ligand Binding, Immune Modulation, and Pathophysiology.Frontiers in immunology · 2021Review
- MD Simulations on a Well-Built Docking Model Reveal Fine Mechanical Stability and Force-Dependent Dissociation of Mac-1/GPIbα Complex.Frontiers in molecular biosciences · 2021Article
- Inflammatory Cell Recruitment in Cardiovascular Disease.Frontiers in cell and developmental biology · 2021Review
- FcγRIIA expression accelerates nephritis and increases platelet activation in systemic lupus erythematosus.Blood · 2020Article
- Platelets Disseminate Extracellular Vesicles in Lymph in Rheumatoid Arthritis.Arteriosclerosis, thrombosis, and vascular biology · 2020Article
- Co-Nanoencapsulation of Vitamin DInflammation · 2019Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
The firm adhesion and transplatelet migration of leukocytes on vascular thrombus are dependent on the interaction of the leukocyte integrin Mac-1 (alphaMbeta2, CD11b/CD18) and the platelet counter receptor glycoprotein (GP) Ibalpha. Previous studies have established a central role for the I domain, a stretch of approximately 200 amino acids within the alphaM subunit, in the binding of GP Ibalpha. This study was undertaken to establish the molecular basis of GP Ibalpha recognition by alphaMbeta2. The P201-K217 sequence, which spans an exposed loop and amphipathic alpha4 helix in the three-dimensional structure of the alphaMI domain, was identified as the binding site for GP Ibalpha. Mutant cell lines in which the alphaMI domain segments P201-G207 and R208-K217 were switched to the homologous, but non-GP Ibalpha binding, alphaL domain segments failed to support adhesion to GP Ibalpha. Mutation of amino acid residues within P201-K217, H210-A212, T213-I215, and R216-K217 resulted in the loss of the binding function of the recombinant alphaMI domains to GP Ibalpha. Synthetic peptides duplicating the P201-K217, but not scrambled versions, directly bound GP Ibalpha and inhibited alphaMbeta2-dependent adhesion to GP Ibalpha and adherent platelets. Finally, grafting critical amino acids within the P201-K217 sequence onto alphaL, converted alphaLbeta2 into a GP Ibalpha binding integrin. Thus, the P201-K217 sequence within the alphaMI domain is necessary and sufficient for GP Ibalpha binding. These observations provide a molecular target for disrupting leukocyte-platelet complexes that promote vascular inflammation in thrombosis, atherosclerosis, and angioplasty-related restenosis.
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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.