Low density lipoproteins inhibit the Na+/H+ antiport in human platelets via activation of p38MAP kinase.
作者： Jerzy-Roch Nofer , Christian Noll , Renata Feuerborn , Gerd Assmann , Martin Tepel
DOI: 10.1016/J.BBRC.2005.12.070
关键词: p38 mitogen-activated protein kinases 、 Phosphorylation 、 Antiporter 、 Mitogen-activated protein kinase kinase 、 Sodium–hydrogen antiporter 、 Intracellular pH 、 Cell biology 、 MAP Kinase Kinase 3 、 Biophysics 、 Chemistry 、 Platelet activation
摘要: Low density lipoproteins (LDL) inhibit the Na+/H+ antiport and thereby sensitize platelet towards agonist. However, mechanisms underlying suppressing effect of LDL on exchange are unclear. We here show that lowering intracellular pH suppression sodium propionate-induced in presence abolished by SKF86002, a selective inhibitor p38MAP kinase (p38MAPK). The inhibitory was mimicked H2O2, which directly activates p38MAPK. Exposure platelets to or H2O2 led phosphorylation p38MAPK, its upstream regulator MAP 3/6 (MKK 3/6), downstream target heat shock protein 27 (HSP27), this abrogated SKF86002-pretreated platelets. In addition, both produced SKF86002-sensitive an oligopeptide encompassing p38MAPK sequence derived from NHE-1, major exchanger further sensitizing effects thrombin-induced activation, as reflected aggregation granule secretion, cells pretreated with SKF86002. conclude activation is required for LDL-dependent sensitization human
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