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KMID : 0613820130230081050
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Journal of Life Science
2013 Volume.23 No. 8 p.1050 ~ p.1056
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Proteomic Analysis of Protein Changes in Human Lung Cancer Epithelial Cells Following Streptococcus pneumoniae Infection
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Lee Yun-Yeong
Chung Kyung-Tae
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Abstract
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Streptococcus pneumoniae is the leading cause of community-acquired pneumonia throughout the world. The bacteria invade through lung tissue and cause sepsis, shock, and serious sequelae, including rheumatic fever and acute glomerulonephritis. However, the molecular mechanism associated with pneumonia's penetration of lung tissue and invasion of the blood stream are still unclear. We attempted to investigate the host cell response at protein levels to S. pneumoniae D39 invasion using human lung cancer epithelial cells, A549. Streptococcus pneumoniae D39 began to change the morphology of A549 cells to become round with filopodia at 2 hours post-infection. A549 cell proteins obtained at each infection time point were separated by SDS-PAGE and analyzed using MALDI-TOF. We identified several endoplasmic reticulum (ER) resident proteins such as Grp94 and Grp78 and mitochondrial proteins such as ATP synthase and Hsp60 that increased after S. pneumoniae D39 infection. Cytosolic Hsc70 and Hsp90 were, however, identified to decrease. These proteins were also confirmed by Western blot analysis. The identified ER resident proteins were known to be induced during ER stress signaling. These/ data, therefore, suggest that S. pneumoniae D39 infection may induce ER stress.
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KEYWORD
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Streptococcus pneumoniae, proteomics, molecular chaperone, ER stress, A549 cells
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