Endothelial cells and extracellular calmodulin inhibit monocyte tumor necrosis factor release and augment neutrophil elastase release
| Autor: | Charles T. Esmon, Craig W. Carson, Donald S. Houston |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Lipopolysaccharides
Umbilical Veins Calmodulin Endothelium Neutrophils Molecular Sequence Data HL-60 Cells Biology Biochemistry Umbilical vein Monocytes Cell Line medicine Extracellular Tumor Cells Cultured Animals Humans Amino Acid Sequence Molecular Biology Cells Cultured Tumor Necrosis Factor-alpha Monocyte Cell Biology Recombinant Proteins Cell biology Kinetics medicine.anatomical_structure Cross-Linking Reagents Cell culture Neutrophil elastase biology.protein Tumor necrosis factor alpha Calmodulin-Binding Proteins Cattle Endothelium Vascular Leukocyte Elastase Protein Binding Signal Transduction |
| Zdroj: | The Journal of biological chemistry. 272(18) |
| ISSN: | 0021-9258 |
| Popis: | Cultured human umbilical vein endothelial cells inhibited tumor necrosis factor-alpha release from whole blood or isolated mononuclear cells exposed to endotoxin. In contrast, the endothelial cells augmented neutrophil elastase release in the same blood. A protein with these functional properties was isolated from endothelial cell-conditioned media and, surprisingly, was identified as calmodulin. Authentic calmodulin mimicked the effect of endothelium. 125I-Calmodulin bound to a high affinity site on monocytic cell lines (Kd approximately 30 nM, in agreement with its functional activity). Cross-linking of 125I-calmodulin to monocytic cells identified a candidate calmodulin receptor. We conclude that calmodulin possesses an extracellular signaling role in addition to its intracellular regulatory functions. Calmodulin released at sites of tissue injury or possibly by specific mechanisms in the endothelium can bind to receptors, modulating the activities of inflammatory cells. |
| Databáze: | OpenAIRE |
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