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Peer-reviewedCC BY 4.0Cells

Differential Localization of CEACAM-1 in Distinct Platelet Populations

  1. 1Department of Biopharmacy and Radiopharmacy, Medical University of Bialystok, 15-222 Bialystok, Poland
  2. 2Radiopharmacy Centre, Medical University of Bialystok, 15-569 Bialystok, Poland
  3. 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.

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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  -