The N-terminal half of membrane CD14 is a functional cellular lipopolysaccharide receptor
Autor: | Suganya Viriyakosol, Theo N. Kirkland |
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Rok vydání: | 1996 |
Předmět: |
Lipopolysaccharides
Lipopolysaccharide Recombinant Fusion Proteins CD14 Molecular Sequence Data Immunology Lipopolysaccharide Receptors CHO Cells Biology Microbiology Cell membrane Mice chemistry.chemical_compound Cell surface receptor Cricetinae medicine Animals Humans 5-HT5A receptor Receptor Base Sequence CD55 Antigens Monocyte Chinese hamster ovary cell Molecular biology Peptide Fragments Infectious Diseases medicine.anatomical_structure chemistry Parasitology Research Article |
Zdroj: | Infection and Immunity. 64:653-656 |
ISSN: | 1098-5522 0019-9567 |
DOI: | 10.1128/iai.64.2.653-656.1996 |
Popis: | CD14, a glycosylphosphatidylinositol-anchored protein on the surface of monocytes, macrophages, and polymorphonuclear leukocytes, is a receptor for lipopolysaccharide (LPS). It was recently reported that an N-terminal 152-amino-acid fragment of soluble CD14 was an active soluble lipopolysaccharide receptor (T. S. -C. Juan, M. J. Kelley, D. A. Johnson, L. A. Busse, E. Hailman, S. D. Wright, and H. S. Lichenstein, J. Biol. Chem. 270:1382-1387, 1995). To determine whether the N-terminal half of the membrane CD14 was a functional LPS receptor on the cell membrane, we engineered a chimeric gene coding for amino acids 1 to 151 of CD14 fused to the C-terminal region of decay-accelerating factor and expressed it in Chinese hamster ovary cells and 70Z/3 cells. We found that the chimeric, truncated CD14 is a fully functional LPS receptor in both cell lines. |
Databáze: | OpenAIRE |
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