Two vitellogenins in the loliginid squid Uroteuthis edulis: Identification and specific expression in ovarian follicles
Two vitellogenins in the loliginid squid Uroteuthis edulis: Identification and specific expression in ovarian follicles
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DOI：
10.1002/mrd.22786
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发表时间：
2017-05
影响因子：
2.5
通讯作者：
Hajime Kitano;N. Nagano;K. Sakaguchi;M. Matsuyama
中科院分区：
文献类型：
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作者：
Hajime Kitano;N. Nagano;K. Sakaguchi;M. Matsuyama
卵黄发生是卵生动物常见的生理过程。卵黄蛋白原（VTG）是卵黄蛋白的前体，其分子特征、修饰和利用已在各种分类群中得到表征，以了解不同生殖模式下的卵子发生。VTG的激素调节已在无脊椎动物中进行了研究，如昆虫和甲壳类动物;相反，对头足类动物知之甚少。在这项研究中，我们分离出两个VTG基因（ue-VTG 1和ue-VTG 2）从loliginid剑尖鱿鱼，美味尾鱿，通过全面调查的转录组数据库和随后的cDNA克隆。对这两种ue-VTG的结构分析揭示了它们的独特特征，即缺乏通常在其他生物体的VTG中发现的两个结构域：von Willebrand因子D结构域（vWD）和未知功能结构域1943（DUF 1943）。卵巢中的ue-VTG 1和ue-VTG 2转录物水平，特别是在卵泡细胞中，在卵黄发生后期增加，表明卵黄积累通过涉及卵泡细胞和卵母细胞的旁分泌相互作用进行。生化纯化的卵黄蛋白的N末端氨基酸测序揭示了其来源于这两种VTG，表明两者都是卵黄蛋白的功能前体。这些结果提供的信息，是必不可少的了解卵黄合成，积累和存储在loliginid鱿鱼的生理途径。
Vitellogenenesis is a physiological process common in oviparous animals. The molecular profile, modifications, and utilization of vitellogenin (VTG), a precursor of yolk protein, have been characterized in various taxa to understand oogenesis within different modes of reproduction. Hormonal regulation of VTGs has been investigated in invertebrates, such as insects and crustaceans; conversely, little is known for cephalopods. In this study, we isolated two VTG genes (ue‐VTG1 and ue‐VTG2) from the loliginid swordtip squid, Uroteuthis edulis, via a comprehensive survey of a transcriptome database and subsequent cDNA cloning. Structural analysis of the two ue‐VTGs revealed their unique features, namely the absence of two domains usually found in VTGs from other organisms: the von Willebrand factor D domain (vWD) and the domain of unknown function 1943 (DUF1943). Levels of ue‐VTG1 and ue‐VTG2 transcripts in the ovary, specifically in follicular cells, increased during the late‐vitellogenic phase, suggesting that yolk accumulation progresses via paracrine interactions involving follicular cells and oocytes. N‐terminal amino acid sequencing of biochemically purified yolk protein revealed its origins from these two VTGs, indicating that both are functional precursors of yolk protein. These results provide information that is essential to understanding the physiological pathway of yolk synthesis, accumulation, and storage in loliginid squids.