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首页> 外文期刊>Biochemistry >Protein Kinase C Signaling in Adenoviral Infection
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Protein Kinase C Signaling in Adenoviral Infection

机译：腺病毒感染中的蛋白激酶C信号传导

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Activation of protein kinase C (PKC), a serine/threonine protein kinase, ubiquitously influences cellular signal transduction and has been shown to play a role in viral entry. In this study, we explored a role for PKC in human adenovirus type 37 infection of primary human corneal fibroblasts, a major target cell for infection. We sought evidence for an interaction between PKC activation and two potential downstream targets: cSrc kinase, shown previously to play a critical role in adenovirus signaling in these cells, and caveolin-1, reported earlier,to be important to entry of adenovirus type 37. Infection of fibroblasts increased PKC alpha phosphorylation and translocation of PKC alpha from the cytosol to caveolin-1 containing vesicles. Virus-induced phosphorylation of both cSrc and AKT was abolished in cell lysates pretreated with calphostin C, a chemical inhibitor of PKC. Inhibition of PKC also reduced virus associated phosphorylation of caveolin-1, while inhibition of cSrc by the chemical inhibitor PP2 reduced only caveolin-1 phosphorylation, but not PKC alpha phosphorylation, in lipid rafts. These results suggest a role for PKC alpha upstream to both cSrc and caveolin-1. Phosphorylated PKC alpha was found in the same endosomal fractions as phosphorylated cSrc, and PKC alpha was present to a greater degree in caveolin-1 pull downs from virus infected than mock infected cell lysates. Calphostin C also reduced early viral gene expression, indicating that PKC alpha activity may be required for viral entry. PKC alpha plays a central role in adenovirus infection of corneal fibroblasts and regulation of downstream molecules, including the important lipid raft component caveolin-1.
机译：丝氨酸/苏氨酸蛋白激酶蛋白激酶C（PKC）的激活普遍影响细胞信号转导，并已显示在病毒进入中起作用。在这项研究中，我们探索了PKC在人原发性角膜成纤维细胞（感染的主要靶细胞）的37型腺病毒感染中的作用。我们寻求证据证明PKC激活与两个潜在的下游靶标之间存在相互作用：先前证明cSrc激酶在这些细胞中的腺病毒信号中起关键作用，以及先前报道的Caveolin-1对37型腺病毒的进入很重要。成纤维细胞的感染增加了PKCα的磷酸化和PKCα从细胞质到含有Caveolin-1的囊泡的转运。在用钙磷蛋白C（一种PKC的化学抑制剂）预处理的细胞裂解物中，病毒诱导的cSrc和AKT磷酸化被消除。 PKC的抑制作用还降低了病毒相关的小窝蛋白1的磷酸化，而化学抑制剂PP2对cSrc的抑制作用仅减少了脂筏中的小窝蛋白1的磷酸化，但不减少PKCα的磷酸化。这些结果表明，cSrc和caveolin-1上游的PKCα均起作用。在与磷酸化的cSrc相同的内体组分中发现了磷酸化的PKCα，与被模拟感染的细胞裂解液相比，来自被病毒感染的Caveolin-1下拉序列中PKCα的含量更高。 Calphostin C还降低了早期病毒基因的表达，表明病毒进入可能需要PKC alpha活性。 PKCα在角膜成纤维细胞的腺病毒感染和下游分子（包括重要的脂筏成分Caveolin-1）的调节中起着核心作用。

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