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首页> 外文期刊>Biochemistry >Bombyx Adipokinetic Hormone Receptor Activates Extracellular Signal-Regulated Kinase 1 and 2 via G Protein-Dependent PKA and PKC but β-Arrestin-Independent Pathways
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Bombyx Adipokinetic Hormone Receptor Activates Extracellular Signal-Regulated Kinase 1 and 2 via G Protein-Dependent PKA and PKC but β-Arrestin-Independent Pathways

机译：Bombyx脂肪代谢激素受体通过G蛋白依赖性PKA和PKC激活细胞外信号调节的激酶1和2，但不依赖β-arrestin。

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Neuropeptides of the adipokinetic hormone (AKH) family are among the best studied hormonenpeptides. They play important roles in insect hemolymph sugar homeostasis, larval lipolysis, and storage-fatnmobilization. Mechanistic investigations have shown that, upon AKH stimulation, adipokinetic hormonenreceptor (AKHR) couples to a Gs protein and enhances adenylate cyclase activity, leading to intracellularncAMP accumulation. However, the underlying molecular mechanism by which this signaling pathwaynconnects to extracellular signal-regulated kinase 1/2 (ERK1/2) remains to be elucidated. Using HEK293 cellsnstably or transiently expressing AKHR, we demonstrated that activation of AKHR elicited transientnphosphorylation of ERK1/2. Our investigation indicated that AKHR-mediated activation of ERK1/2 wasnsignificantly inhibited by H-89 (protein kinase A inhibitor), Go6983, and GF109203X (protein kinase Cninhibitors) but not by U73122 (PLC inhibitor) or FIPI (PLD inhibitor).Moreover, AKHR-induced ERK1/2nphosphorylation was blocked by the calcium chelators EGTA and BAPTA-AM. Furthermore, ERK1/2nactivation in both transiently and stably AKHR-expressing HEK293 cells was found to be sensitive tonpretreatment of pertussis toxin, whereas AKHR-mediated ERK1/2 activation was insensitive to siRNA-ninduced knockdown of β-arrestins and to pretreatment of inhibitors of EGFR, Src, and PI3K. On the basis ofnour data, we propose that activated AKHR signals to ERK1/2 primarily via PKA- and calcium-involvednPKC-dependent pathways. Our current study provides the first in-depth study defining the mechanisms ofnAKH-mediated ERK activation through the Bombyx AKHR.
机译：脂肪代谢激素（AKH）家族的神经肽是研究最深入的激素肽之一。它们在昆虫的血淋巴糖稳态，幼虫脂解和储存脂肪固定中起重要作用。机理研究表明，在AKH刺激下，脂肪动力学激素受体（AKHR）与Gs蛋白偶联并增强腺苷酸环化酶活性，导致细胞内NCAMP积累。然而，该信号传导途径连接到细胞外信号调节激酶1/2（ERK1 / 2）的潜在分子机制仍有待阐明。使用HEK293细胞稳定或瞬时表达AKHR，我们证明了AKHR的激活引起ERK1 / 2的瞬时磷酸化。我们的研究表明，AKHR介导的ERK1 / 2活化不受H-89（蛋白激酶A抑制剂），Go6983和GF109203X（蛋白激酶Cn抑制剂）的抑制，但不受U73122（PLC抑制剂）或FIPI（PLD抑制剂）的抑制。 ，AKHR诱导的ERK1 / 2n磷酸化被钙螯合剂EGTA和BAPTA-AM阻断。此外，发现瞬时表达和稳定表达AKHR的HEK293细胞中的ERK1 / 2n激活都是百日咳毒素的敏感的ton预处理，而AKHR介导的ERK1 / 2激活对siRNA诱导的β-arrestin的敲低以及对抑制剂的预处理不敏感。 EGFR，Src和PI3K。根据数据，我们建议主要通过PKA和钙参与的PKC依赖性途径激活AKHR信号至ERK1 / 2。我们当前的研究提供了第一个深入的研究，它定义了通过Bombyx AKHR介导nAKH介导的ERK激活的机制。

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  • 来源
    《Biochemistry》 |2010年第51期|p.10862-10872|共11页
  • 作者

    Haishan Huang Xiaobai He Xiaoyan Deng Guo Li Guoyuan Ying Yi Sun Liangen Shi Jeffrey L. Benovic and Naiming Zhou;

  • 作者单位

    ‡Institute of Biochemistry, College of Life Sciences, Zijingang Campus, Zhejiang University, Hangzhou, Zhejiang 310058, China,§College of Animal Sciences, Huajia Pond Campus, Zhejiang University, Hangzhou, Zhejiang 310029, China, and ) Department ofBiochemistry, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, United States;

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