The fatty-acid-binding heterocomplex FA-p34 formed by S100A8 and S100A9 is the major fatty acid carrier in neutrophils and translocates from the cytosol to the membrane upon stimulation
| Autor: | Karen Roulin, Jacques H. Veerkamp, Raymonde Hotz, Gerry Hagens, Georges Siegenthaler, Jean-Hilaire Saurat |
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| Rok vydání: | 1999 |
| Předmět: |
Neutrophils
Linoleic acid Immunoblotting Biology Ligands Fatty acid-binding protein Cell membrane chemistry.chemical_compound Cytosol Fatty acid binding medicine Animals Calgranulin B Humans Calgranulin A Electrophoresis Gel Two-Dimensional chemistry.chemical_classification Spier en vetzuurbindende eiwitten in de spier van het varken Calcium-Binding Proteins Cell Membrane S100 Proteins Fatty acid Biological Transport Cell Biology Muscle and adipocyte fatty acid-binding proteins of porcine muscle Antigens Differentiation Oleic acid medicine.anatomical_structure chemistry Biochemistry Fatty Acids Unsaturated Electrophoresis Polyacrylamide Gel Arachidonic acid Rabbits Carrier Proteins |
| Zdroj: | Experimental Cell Research, 247, 410-421 Experimental Cell Research, 247, pp. 410-421 |
| ISSN: | 0014-4827 |
| Popis: | Since no data are available concerning fatty acid (FA) transport in neutrophils we studied the presence of possible FA carriers. The kFA-p34 complex, composed of S100A8 and S100A9, has been implicated in the intracellular transport of arachidonic acid and its precursors in human keratinocytes. Here, we show that FA-p34 is the major FA carrier in human neutrophils (nFA-p34). The complex is highly expressed in resting neutrophils (2.65% of cytosolic proteins) and translocates to the membrane fraction upon stimulation with opsonized zymosan. Comparison of purified nFA-p34 with kFA-p34 shows that both complexes are composed of nearly the same subunits and possess similar binding properties for oleic acid. Densitometrical analyses of 2D gels show that n and kFA-p34 contain twice as much S100A8 and S100A9 suggesting an estimated stoichiometry of (S100A8)2S100A9. A method is described allowing to distinguish n and kFA-p34 from S100A8/S100A9 homo- and heteromer complexes that are devoid of FA-binding properties. After solvent extraction, we find by GC analysis linoleic acid as major endogenous ligand of purified kFA-p34. Our results suggest that nFA-p34, might be involved in the shuttling of unsaturated FA between the cytosol and the plasma membrane of neutrophils. |
| Databáze: | OpenAIRE |
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