Expression of the CD15 differentiation antigen (3-fucosyl-N-acetyl-lactosamine, LeX) on putative neutrophil adhesion molecules CR3 and NCA-160
| Autor: | M Albrechtsen, Michael A. Kerr, S C Stocks |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Neutrophils
Antigens Differentiation Myelomonocytic Lewis X Antigen Complement receptor CD15 Lymphocyte Activation Biochemistry Epitopes Mice Carcinoembryonic antigen Antigen Antigens CD Antigens Neoplasm Animals Humans Molecular Biology Glycoproteins chemistry.chemical_classification biology T-cell receptor Cell Membrane Antibodies Monoclonal Cell Biology Molecular biology Antigens Differentiation Receptors Complement Up-Regulation N-Formylmethionine Leucyl-Phenylalanine Membrane glycoproteins chemistry Complement C3b biology.protein Receptors Complement 3b Antibody Glycoprotein Cell Adhesion Molecules Trisaccharides Research Article |
| Zdroj: | The Biochemical journal. 268(2) |
| ISSN: | 0264-6021 |
| Popis: | The expression of the carbohydrate antigen 3-fucosyl-N-acetyl-lactosamine (CD15, LeX) on human neutrophil glycoproteins has been studied by immunoprecipitation and immunoblotting by using monoclonal antibody MC2. The antigen is expressed on membrane glycoproteins of approximate molecular mass 165 and 105 kDa. These glycoproteins include the complement receptor and adhesion molecule, CR3, in which the β-chain (CD18, 105 kDa) shows much greater expression than the alpha-chain (CD11b, 165 kDa). Most of the 165 kDa CD15 antigen is accounted for by expression on the carcinoembryonic antigen (CEA)-related molecule NCA160. Other members of this family, NCA95, NCA90 and NCA55, which are also found in neutrophils, do not express the CD15 antigen. There is a marked increase in the surface expression of CD15, CR3 and the antigen recognized by anti-CEA antibodies upon activation of neutrophils by the chemotactic peptide N-formylmethionyl-leucylphenylalanine. |
| Databáze: | OpenAIRE |
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