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Subcellular localization of carcinoembryonic antigen-related cell adhesion molecular 8 (CEACAM8) in human eosinophils: CEACAM8 in human eosinophils
Uppsala University, Medicinska vetenskapsområdet, Faculty of Medicine, Department of Medical Sciences, Clinical Chemistry.
Manuscript (Other academic)
URN: urn:nbn:se:uu:diva-92103OAI: oai:DiVA.org:uu-92103DiVA: diva2:165061
Available from: 2004-09-20 Created: 2004-09-20 Last updated: 2010-01-13Bibliographically approved
In thesis
1. CarcinoEmbryonic Antigen-related Cell Adhesion Molecule 8 (CEACAM8): Purification, Characterization, Cellular and Clinical Studies
Open this publication in new window or tab >>CarcinoEmbryonic Antigen-related Cell Adhesion Molecule 8 (CEACAM8): Purification, Characterization, Cellular and Clinical Studies
2004 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

A 95-kDa protein was purified from normal human granulocytes. The protein reacted with a monoclonal antibody against CEACAM8. MALDI-Tof and MS/MS analyses revealed the protein to be a CGM6 gene product. Thus, the protein was proved to be identical to CEACAM8.

An ELISA for CEACAM8 was developed with detection range of 1-64μg/L. Data are presented on the levels of CEACAM8 in the blood of healthy individuals and patients undergoing surgery, as well as in patients with acute infection. The highly elevated levels of CEACAM8 in the blood of these patients were significantly correlated with the surface expression of CEACAM8 on neutrophils and the number of circulating neutrophils, which suggests that CEACAM8 could serve as a biological marker for granulocyte activitiy in vivo.

The cellular content of CEACAM8 in neutrophils was estimated to be 82.4 ± 8.9 ng/106 cells. Subcellular localisation and mobilisation studies showed that the majority of CEACAM8 is present in the secondary granules of human neutrophils, with a small amount on the plasma membranes. Upon stimulation, CEACAM8 translocated to the plasma membranes from the secondary granules and was also released extracellularly (5.5 ± 0.7% of the total content of CEACAM8).

In eosinophils, the cellular content of CEACAM8 was estimated to be 73.8 ± 6.0 ng/106 cells. In these cells, CEACAM8 is mainly stored in secretory vesicles. Upon activation, eosinophils released 5.1 ± 1.1% of the total content of CEACAM8.

Administration of granulocyte colony-stimulating factor (G-CSF) to healthy individuals resulted in an increased content of CEACAM8 in neutrophils on day 1, and decreased on day 4. However, the content of CEACAM8 in light membrane fractions was increased on day 4. The translocation of CEACAM8 observed in vivo after G-CSF administration is probably not directly related to this cytokine but to other cytokines such as TNF-a.

Place, publisher, year, edition, pages
Uppsala: Acta Universitatis Upsaliensis, 2004. 64 p.
Comprehensive Summaries of Uppsala Dissertations from the Faculty of Medicine, ISSN 0282-7476 ; 1372
Biochemistry, human neutrophil, human eosinophil, granule proteins, CEA, CEACAM8, G-CSF, ELISA, subcellular fractionation, Biokemi
National Category
Biochemistry and Molecular Biology
urn:nbn:se:uu:diva-4534 (URN)91-554-6031-3 (ISBN)
Public defence
2004-10-15, Rosensalen, entrance 95/96, Akademiska sjukhuset, Uppsala, 13:15
Available from: 2004-09-20 Created: 2004-09-20Bibliographically approved

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