A calpain inhibitor protects against fractalkine production in lipopolysaccharide-treated endothelial cells
Kidney Research and Clinical Practice
;
: 224-231, 2017.
Article
in English
| WPRIM
| ID: wpr-218955
ABSTRACT
BACKGROUND:
Fractalkine (CX3CL1) is a chemokine with a unique CX3C motif and is produced by endothelial cells stimulated with lipopolysaccharide (LPS), tumor necrosis factor (TNF)-α, interleukin (IL)-1, and interferon-γ. There have been several reports that the caspase/calpain system is activated in endotoxemia, which leads to cellular apoptosis and acute inflammatory processes. We aimed to determine the role of the caspase/calpain system in cell viability and regulation of fractalkine production in LPS-treated endothelial cells.METHODS:
Human umbilical vein endothelial cells (HUVECs) were stimulated with 0.01–100 μg/mL of LPS to determine cell viability. The changes of CX3CL1 expression were compared in control, LPS (1 μg/mL)-, IL-1α (1 μg/mL)-, and IL-1β (1 μg/mL)-treated HUVECs. Cell viability and CX3CL1 production were compared with 50 μM of inhibitors of caspase-1, caspase-3, caspase-9, and calpain in LPS-treated HUVECs.RESULTS:
Cell viability was significantly decreased from 1 to 100 μg/mL of LPS. Cell viability was significantly restored with inhibitors of caspase-1, caspase-3, caspase-9, and calpain in LPS-treated HUVECs. The expression of CX3CL1 was highest in IL-1β-treated HUVECs. CX3CL1 production was highly inhibited with a calpain inhibitor and significantly decreased with the individual inhibitors of caspase-1, caspase-3, and caspase-9.CONCLUSION:
The caspase/calpain system is an important modulator of cell viability and CX3CL1 production in LPS-treated endothelial cells.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Calpain
/
Cell Survival
/
Lipopolysaccharides
/
Interleukins
/
Tumor Necrosis Factor-alpha
/
Apoptosis
/
Endotoxemia
/
Endothelial Cells
/
Caspase 3
/
Caspase 9
Language:
English
Journal:
Kidney Research and Clinical Practice
Year:
2017
Type:
Article
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