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Oxidized low-density lipoprotein- and lysophostidylcholine-induced Ca2+ mobilization in human endothelial cells
- Oxidized low-density lipoprotein- and lysophostidylcholine-induced Ca2+ mobilization in human endothelial cells
- Kim M.Y.; Liang G.H.; Kim J.A.; Choi S.S.; Choi S.; Suh S.H.
- Ewha Authors
- 최수승; 서석효
- SCOPUS Author ID
- 최수승; 서석효
- Issue Date
- Journal Title
- Korean Journal of Physiology and Pharmacology
- Korean Journal of Physiology and Pharmacology vol. 13, no. 1, pp. 27 - 32
- SCIE; SCOPUS; KCI
- Document Type
- The effects of oxidized low-density lipoprotein (OxLDL) and its major lipid constituent lysophosphatidylcholine (LPC) on Ca2+ entry were investigated in cultured human umbilical endothelial cells (HUVECs) using fura-2 fluorescence and patch-clamp methods. OxLDL or LPC increased intracellular Ca2+ concentration ([Ca2+]i), and the increase of [Ca2+]i by OxLDL or by LPC was inhibited by La3+ or heparin. LPC failed to increase [Ca2+]i in the presence of an antioxidant tempol. In addition, store-operated Ca2+ entry (SOC), which was evoked by intracellular Ca2+ store depletion in Ca2+-free solution using the sarcoplasmic reticulum Ca2+ pump blocker, 2, 5-di-t-butyl-1, 4-benzohydroquinone (BHQY), was further enhanced by OxLDL or by LPC. Increased SOC by OxLDL or by LPC was inhibited by U73122. In voltage-clamped cells, OxLDL or LPC increased [Ca2+]i and simultaneously activated non-selective cation (NSC) currents. LPC-induced NSC currents were inhibited by 2-APB, La3+ or U73122, and NSC currents were not activated by LPC in the presence of tempol. Furthermore, in voltage-clamped HUVECs, OxLDL enhanced SOC and evoked outward currents simultaneously. Clampinig intracellular Ca2+ to 1 υM activated large-conductance Ca2+-activated K+ (BKCa) clirrent spontaneously, and this activated BKCa current was further enhanced bv OxLDL or by LPC. From these results, we concluded that OxLDL or its main component LPC activates Ca2+-permeable Ca2+-activated NSC current and BKCa current simultaneously, thereby increasing SOC.
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