Differential Localization of CEACAM-1 in Distinct Platelet Populations
- 1Department of Biopharmacy and Radiopharmacy, Medical University of Bialystok, 15-222 Bialystok, Poland
- 2Radiopharmacy Centre, Medical University of Bialystok, 15-569 Bialystok, Poland
- 3Department of Physical Chemistry, Medical University of Bialystok, 15-089 Bialystok, Poland
Abstract
Carcinoembryonic antigen-related cell adhesion molecule-1 (CEACAM-1) is a platelet receptor recognized as a negative regulator of platelet activity. During thrombus formation, platelets differentiate into distinct populations, but whether CEACAM-1 is preferentially associated with specific platelet phenotypes remains unclear. Here, we investigated CEACAM-1 localization in different platelet populations, focusing on the accessibility of its extracellular domain. In platelets adherent to poly-L-lysine, the CEACAM-1 signal was predominantly intracellular and decreased following treatment with acetylsalicylic acid (ASA), whereas glucose increased this signal. During integrin-dependent spreading on fibrinogen, CEACAM-1 was undetectable by immunofluorescence, irrespective of αIIbβ3 inhibition with tirofiban, although its presence was confirmed by Western blotting. Flow cytometry revealed that ASA reduced the percentage of CEACAM-1-positive platelets following ADP stimulation under both normoglycemic and hyperglycemic conditions. Confocal microscopy demonstrated co-localization of CEACAM-1 with phosphatidylserine (PS)-positive regions, a hallmark of the procoagulant platelet phenotype. In thrombi formed on collagen fibers under flow, ASA reduced the CEACAM-1-positive area under both conditions. However, a reduction in the ratio of CEACAM-1-positive area to PS-exposing area was observed only under normoglycemic conditions. In fibrin–platelet clots, CEACAM-1 was detected only after prolonged clot incubation and subsequent platelet permeabilization. Collectively, these findings reveal differences in CEACAM-1 localization and detectability across platelet populations and experimental settings, suggesting an association with platelet functional specialization.
Related
- Transcriptionally distinct atypical B cell populations contribute to insulin autoreactivity and show differential activation, isotype switching, and somatic hypermutation in early-stage type 1 diabetes individuals
- Differential localization of autolyzed calpains 1 and 2 in slow and fast skeletal muscles in the early phase of atrophy
- Wild Luteibacter populations exhibit climate-associated divergence and distinct genomic strategies for osmotic stress tolerance
- Recombinant Echis disintegrins reveal distinct inhibitory profiles on platelet aggregation and endothelial cell migration
- Differential Cellular Dynamics of Platelet-Derived Growth Factor Receptor β Cells and Macrophages After Complete Spinal Cord Transection in Neonatal and Juvenile Rats.
BibTeX
@article{bielicka2026differential,
title = {{Differential Localization of CEACAM-1 in Distinct Platelet Populations}},
author = {Natalia Bielicka and Adam Jan Olichwier and Tomasz Misztal and Magdalena Bruzgo-Grzybko and Izabela Suwda Kalita and Ewa Chabielska and Anna Gromotowicz-Popławska},
journal = {Cells},
year = {2026},
month = oct,
doi = {10.3390/cells15211920},
url = {https://www.mdpi.com/2073-4409/15/21/1920},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Differential Localization of CEACAM-1 in Distinct Platelet Populations
AU - Natalia Bielicka
AU - Adam Jan Olichwier
AU - Tomasz Misztal
AU - Magdalena Bruzgo-Grzybko
AU - Izabela Suwda Kalita
AU - Ewa Chabielska
AU - Anna Gromotowicz-Popławska
PY - 2026
DA - 2026/10/22
JO - Cells
DO - 10.3390/cells15211920
UR - https://www.mdpi.com/2073-4409/15/21/1920
AB - Carcinoembryonic antigen-related cell adhesion molecule-1 (CEACAM-1) is a platelet receptor recognized as a negative regulator of platelet activity. During thrombus formation, platelets differentiate into distinct populations, but whether CEACAM-1 is preferentially associated with specific platelet phenotypes remains unclear. Here, we investigated CEACAM-1 localization in different platelet populations, focusing on the accessibility of its extracellular domain. In platelets adherent to poly-L-lysine, the CEACAM-1 signal was predominantly intracellular and decreased following treatment with acetylsalicylic acid (ASA), whereas glucose increased this signal. During integrin-dependent spreading on fibrinogen, CEACAM-1 was undetectable by immunofluorescence, irrespective of αIIbβ3 inhibition with tirofiban, although its presence was confirmed by Western blotting. Flow cytometry revealed that ASA reduced the percentage of CEACAM-1-positive platelets following ADP stimulation under both normoglycemic and hyperglycemic conditions. Confocal microscopy demonstrated co-localization of CEACAM-1 with phosphatidylserine (PS)-positive regions, a hallmark of the procoagulant platelet phenotype. In thrombi formed on collagen fibers under flow, ASA reduced the CEACAM-1-positive area under both conditions. However, a reduction in the ratio of CEACAM-1-positive area to PS-exposing area was observed only under normoglycemic conditions. In fibrin–platelet clots, CEACAM-1 was detected only after prolonged clot incubation and subsequent platelet permeabilization. Collectively, these findings reveal differences in CEACAM-1 localization and detectability across platelet populations and experimental settings, suggesting an association with platelet functional specialization.
SN - 2073-4409
ER -