Mechanism of Lysophosphatidylcholine-Induced Lysosome Destabilization |
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Authors: | Jin-Shan Hu Ying-Bin Li Jiong-Wei Wang Lin Sun Guo-Jiang Zhang |
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Institution: | (1) Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, People’s Republic of China;(2) School of Science, Hebei University of Technology, Tianjin, 300130, People’s Republic of China;(3) Capital Normal University, Beijing, 100037, People’s Republic of China;(4) Institute of Cell Biology, Beijing Normal University, Beijing, 100875, People’s Republic of China |
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Abstract: | Lysosomal destabilization is critical for the organelle and living cells. Phospholipase A2 (PLA2) was shown to be able to destabilize lysosomes under some conditions. By what mechanism the enzyme affects lysosomal stability
is not fully studied. In this study, we investigated the effects of lysophosphatidylcholine (lysoPC), a PLA2-produced lipid metabolite, on lysosomal ion permeability, osmotic sensitivity and stability. By measuring lysosomal β-hexosaminidase
free activity, membrane potential, proton leakage and their enzyme latency loss in hypotonic sucrose medium, we established
that lysoPC could increase the lysosomal permeability to both potassium ions and protons and enhance lysosomal osmotic sensitivity.
These changes in lysosomal membrane properties promoted entry of potassium ions into lysosomes via K+/H+ exchange. The resultant osmotic imbalance across the membranes led to losses of lysosomal integrity. The enhancement of lysosomal
osmotic sensitivity caused the lysosomes to become more liable to destabilization in osmotic shock. These results suggest
that lysoPC may play a key role in PLA2-induced lysosomal destabilization. |
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Keywords: | Lysosome Lysophosphatidylcholine Ion permeability Osmotic sensitivity |
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