ArticleBlood2008
Ligation of erythrocyte CR1 induces its clustering in complex with scaffolding protein FAP-1.
Article in Blood, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
- CR1-mediated ATP release by human red blood cells promotes CR1 clustering and modulates the immune transfer process.The Journal of biological chemistry · 2013Trial
- Immune functions of avian erythrocytes: a comprehensive review from basic biology to pathogen-induced responses.Frontiers in immunology · 2025Review
- RBC membrane biomechanics and Plasmodium falciparum invasion: probing beyond ligand-receptor interactions.Trends in parasitology · 2022Review
- Proteomic Analysis of Potential Targets for Non-Response to Infliximab in Patients With Ulcerative Colitis.Frontiers in pharmacology · 2022Article
- No Evidence that Knops Blood Group Polymorphisms Affect Complement Receptor 1 Clustering on Erythrocytes.Scientific reports · 2017Article
- Detection of membrane-bound and soluble antigens by magnetic levitation.Lab on a chip · 2017Article
- Surface complement C3 fragments and cellular binding of microparticles in patients with SLE.Lupus science & medicine · 2017Article
- Complement Receptors in Myeloid Cell Adhesion and Phagocytosis.Microbiology spectrum · 2016Review
- Ligation of Glycophorin A Generates Reactive Oxygen Species Leading to Decreased Red Blood Cell Function.PloS one · 2016Article
- A chimeric EBV gp350/220-based VLP replicates the virion B-cell attachment mechanism and elicits long-lasting neutralizing antibodies in mice.Journal of translational medicine · 2015Article
- Human complement receptor type 1/CD35 is an Epstein-Barr Virus receptor.Cell reports · 2013Article
- Article
- Neisseria meningitidis and Escherichia coli are protected from leukocyte phagocytosis by binding to erythrocyte complement receptor 1 in human blood.Molecular immunology · 2011Article
- Complement receptor 1 gene variants are associated with erythrocyte sedimentation rate.American journal of human genetics · 2011Article
- Article
- Complement receptor 1 expression on mouse erythrocytes mediates clearance of Streptococcus pneumoniae by immune adherence.Infection and immunity · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The primary identified function of complement receptor 1 (CR1/CD35) on primate erythrocytes is to bind complement-tagged inflammatory particles including microbes and immune complexes. When erythrocytes circulate through liver and spleen, sinusoidal phagocytes remove CR1-adherent particles and erythrocytes return to the circulation. This process of immune adherence clearance is important for host defense and prevention of autoimmunity. CR1 was previously described as clustered in the human erythrocyte membrane, which was thought to be necessary for binding complement-opsonized particles. In contrast, we demonstrate that on erythrocytes CR1 is not clustered, but dispersed, and able to bind complement-tagged particles. When fresh erythrocytes are solubilized by nonionic detergent, CR1 partitions to the cytoskeleton fraction. Using a PDZ-peptide array, CR1's cytoplasmic tail, which contains 2 PDZ-motifs, binds PDZ domains 2, 3, and 5 of Fas-associated phosphatase 1 (FAP-1), a scaffolding protein. We show that FAP-1, not previously recognized as an erythroid protein, is expressed on circulating erythrocytes. CR1 and FAP-1 coimmunoprecipitate, which confirms their molecular association. Disperse CR1 on erythrocytes may be advantageous for capturing immune-complexes, while ligation-induced CR1 clustering may prevent ingestion of the erythrocyte during the immune-complex transfer to the macrophages by keeping the opsonic stimulus localized thus preventing phagocyosis.
Indexed as
Identifiers
What OpenQuestion holds
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.