ArticleJournal of leukocyte biology2015
The granulocyte orphan receptor CEACAM4 is able to trigger phagocytosis of bacteria.
Article in Journal of leukocyte biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Neutrophil CEACAMs and the Inflammatory Response toJournal of innate immunity · 2026Review
- The role of CEACAMs in neutrophil function.European journal of clinical investigation · 2024Review
- Proteomic Profile Regulated by the Immunomodulatory Jusvinza Drug in Neutrophils Isolated from Rheumatoid Arthritis Patients.Biomedicines · 2024Article
- Transcriptional pathways of terminal differentiation in high- and low-density blood granulocytes in sepsis.Journal of inflammation (London, England) · 2024Article
- Key sunitinib-related biomarkers for renal cell carcinoma.Cancer medicine · 2021Article
- Imaging Flow Cytometry Analysis of CEACAM Binding to Opa-Expressing Neisseria gonorrhoeae.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2020Article
- Polar bear evolution is marked by rapid changes in gene copy number in response to dietary shift.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- CEACAM3-A Prim(at)e Invention for Opsonin-Independent Phagocytosis of Bacteria.Frontiers in immunology · 2019Review
- Alternative splicing after gene duplication drives CEACAM1-paralog diversification in the horse.BMC evolutionary biology · 2018Article
- Moraxella catarrhalis induces CEACAM3-Syk-CARD9-dependent activation of human granulocytes.Cellular microbiology · 2016Article
- Immunoreceptors on neutrophils.Seminars in immunology · 2016Review
- Observational
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human granulocytes express several glycoproteins of the CEACAM family. One family member, CEACAM3, operates as a single-chain phagocytic receptor, initiating the detection, internalization, and destruction of a limited set of gram-negative bacteria. In contrast, the function of CEACAM4, a closely related protein, is completely unknown. This is mainly a result of a lack of a specific ligand for CEACAM4. By generating chimeric proteins containing the extracellular bacteria-binding domain of CEACAM3 and the transmembrane and cytoplasmic part of CEACAM4 (CEACAM3/4) we demonstrate that this chimeric receptor can trigger efficient phagocytosis of attached particles. Uptake of CEACAM3/4-bound bacteria requires the intact ITAM of CEACAM4, and this motif is phosphorylated by Src family PTKs upon receptor clustering. Furthermore, SH2 domains derived from Src PTKs, PI3K, and the adapter molecule Nck are recruited and associate directly with the phosphorylated CEACAM4 ITAM. Deletion of this sequence motif or inhibition of Src PTKs blocks CEACAM4-mediated uptake. Together, our results suggest that this orphan receptor of the CEACAM family has phagocytic function and prompt efforts to identify CEACAM4 ligands.
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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.