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首页> 外文期刊>Biochemistry >OXIDIZED LOW-DENSITY LIPOPROTEIN STIMULATES PROTEIN KINASE C (PKC) AND INDUCES EXPRESSION OF PKC-ISOTYPES VIA PROSTAGLANDIN-H-SYNTHASE IN P388D(1) MACROPHAGE-LIKE CELLS
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OXIDIZED LOW-DENSITY LIPOPROTEIN STIMULATES PROTEIN KINASE C (PKC) AND INDUCES EXPRESSION OF PKC-ISOTYPES VIA PROSTAGLANDIN-H-SYNTHASE IN P388D(1) MACROPHAGE-LIKE CELLS

机译：氧化的低密度脂蛋白刺激蛋白激酶C（PKC），并通过前列腺素-H-合酶在P388D（1）巨噬细胞样细胞中诱导PKC同种型的表达

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摘要

Treatment of cells with LPS-free oxLDL significantly enhanced protein kinase C (PKC) activity in cell extracts from P383D(1) macrophage-like cells as determined by phosphorylation of histone H1 or Ac-MBP[4-14] substrate peptide. This effect was abolished by the PKC inhibitors H-7 and bisindolylmaleimide I while pertussis toxin failed to block stimulation. The phosphotransferase activity was also increased by acetylated LDL (acLDL) and maleylated albumin (malBSA), the oxLDL effect was inhibited by chloroquine which also blocked oxLDL-induced stimulation of tyrosine kinase activity. Marginal stimulation of PKC activity was observed when lipid extracts from oxLDL were used, indicating that uptake via scavenger receptors (SR) is mandatory. Polyinosinic acid (poly I) exhibited a concentration-dependent inhibition of the oxLDL-induced effect suggesting that SR II/I but not CD36 interactions are critical to PKC activation. Modified (lipo)proteins increased the concentration of diacylglycerol and differentially affected the levels of individual PKC isoenzymes predominantly in the cytosolic fraction. Changes of activity induced by oxLDL could be primarily assigned to alterations of the activities and levels of the isoenzymes beta and delta. Treatment with oxLDL, acLDL, and malBSA was also accompanied by increased production of prostaglandins as well as by an enhanced level of cyclooxygenase 2 (COX 2) as determined by Western blot analysis. Effecs of oxLDL on PKC activity/expression was supressed by the cyclooxygenase inhibitors indomethacin, by pre-exposure to the inhibitor of both lipoxygenase and cyclooxygenase, 2,2-dimethyl-6-(4-chlorophenyl)-7-phenyl-2,2-dihydro-1H-pyrrolizine-5-ylac etic acid (ML 3000), and by treatment with the specific COX 2-inhibitor N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide (NS-398). These results indicate that oxLDL, acLDL, and malBSA exhibit a COX 2-dependent and isotype specific effect on PKC in P388D(1) cells following uptake via SR II/I and subsequent lysosomal degradation.
机译：通过组蛋白H1或Ac-MBP [4-14]底物肽的磷酸化测定，用无LPS的oxLDL处理细胞显着增强了P383D（1）巨噬细胞样细胞的细胞提取物中的蛋白激酶C（PKC）活性。 PKC抑制剂H-7和双吲哚基马来酰亚胺I取消了该作用，而百日咳毒素未能阻止刺激。乙酰化的LDL（acLDL）和马来酰化的白蛋白（malBSA）也增加了磷酸转移酶的活性，氯喹抑制了oxLDL的作用，氯喹也阻断了oxLDL诱导的酪氨酸激酶活性的刺激。当使用oxLDL的脂质提取物时，观察到PKC活性的边缘刺激，这表明必须通过清除剂受体（SR）摄取。聚肌苷酸（poly I）对oxLDL诱导的效应表现出浓度依赖性抑制作用，表明SR II / I而非CD36相互作用对PKC激活至关重要。修饰的（脂）蛋白增加了二酰基甘油的浓度，并主要影响胞浆级分中各个PKC同工酶的水平。 oxLDL诱导的活性变化可以主要归因于同工酶β和δ活性和水平的改变。 oxLDL，acLDL和malBSA的治疗还伴随着前列腺素的产生增加以及环氧化酶2（COX 2）的水平升高（通过Western印迹分析确定）。 oxLDL对PKC活性/表达的影响被环氧合酶抑制剂吲哚美辛抑制，通过预先暴露于脂氧合酶和环氧合酶抑制剂2,2-二甲基-6-（4-氯苯基）-7-苯基-2,2 -二氢-1H-吡咯嗪-5-丁酸（ML 3000），并用特定的COX 2抑制剂N-（2-环己氧基-4-硝基苯基）甲磺酰胺（NS-398）处理。这些结果表明oxLDL，acLDL和malBSA在通过SR II / I吸收并随后溶酶体降解后，对P388D（1）细胞中的PKC具有COX 2依赖性和同种型特异性作用。

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