Molecular and functional characterization of adipokinetic hormone receptor and its peptide ligands in Bombyx mori.

Molecular and functional characterization of adipokinetic hormone receptor and its peptide ligands in Bombyx mori.
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家蚕脂肪运动激素受体及其肽配体的分子和功能表征

DOI:
10.1016/j.febslet.2009.03.060
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发表时间:
2009-05-06
期刊:
影响因子:
3.5
通讯作者:
Zhou, Naiming
Zhou, Naiming
中科院分区:
生物学3区
文献类型:
--
作者:
Zhu, Chenggang;Huang, Haishan;Hua, Rongsheng;Li, Guo;Yang, Dong;Luo, Jiansong;Zhang, Cunxin;Shi, Liangen;Benovic, Jeffrey L.;Zhou, Naiming

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脂肪动力激素(AKH)家族的神经肽是研究最多的激素肽之一,但其信号通路仍有待阐明。在这项研究中,我们的分子特征的信号转导的AKHR及其肽配体在HEK 293细胞。在稳定表达AKHR的HEK 293细胞中,AKH 1刺激不仅导致配体浓度依赖性的细胞内Ca 2+动员和cAMP积累,而且引起细胞外信号调节激酶1/2(ERK 1/2)途径的瞬时激活。我们观察到AKH受体在AKH 1刺激后迅速内化。我们进一步证明,AKH 2在AKHR上表现出与AKH 1相当的cAMP积累和ERK 1/2激活的高活性,而AKH 3的有效性要低得多。
Neuropeptides of the adipokinetic hormone (AKH) family are among the best studied hormone peptides, but its signaling pathways remain to be elucidated. In this study, we molecularly characterized the signaling of Bombyx AKH receptor (AKHR) and its peptide ligands in HEK293 cells. In HEK293 cells stably expressing AKHR, AKH1 stimulation not only led to a ligand concentration dependent mobilization of intracellular Ca2+ and cAMP accumulation, but also elicited transient activation of extracellular signal-regulated kinase 1/2 (ERK1/2) pathway. We observed that AKH receptor was rapidly internalized after AKH1 stimulation. We further demonstrated that AKH2 exhibited high activities in cAMP accumulation and ERK1/2 activation on AKHR comparable to AKH1, whereas AKH3 was much less effective.
DOI: 10.1016/j.bbrc.2006.03.117
发表时间: 2006-05-26
影响因子: 3.1
作者:
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通讯作者: Grimmelikhuijzen, CJP
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