Characterization of vitellogenin and its derived yolk proteins in cloudy catshark(Scyliorhinus torazame).
Characterization of vitellogenin and its derived yolk proteins in cloudy catshark(Scyliorhinus torazame).
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云猫鲨（Scyliorhinus torazame）中卵黄蛋白原及其衍生卵黄蛋白的表征。
DOI：
10.1007/s10695-012-9706-1
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发表时间：
2013
期刊：
影响因子：
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通讯作者：
Hara A.
中科院分区：
文献类型：
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作者：
Yamane K;Yagai T;Nishimiya O;Sugawara R;Amano H;Fujita T;Hiramatsu N;Todo T;Matsubara T;Hara A.
板鳃类（鲨鱼和鳐）具有独特的生殖特征，与硬骨鱼类的情况相反，对它们蛋黄蛋白的身份、结构和物理特征知之甚少。本研究的目的是（1）检测和纯化云猫鲨（Scyliorhinus torazame）的卵黄蛋白原（Vtg;蛋黄前体）和卵黄蛋白（YPs）;（2）研究Vtg和YPs之间的关系;（3）对Vtg转录本（vtg）的一级结构进行表征和分类。通过凝胶过滤测定纯化的Vtg和推定的Vtg相关YP（卵黄脂磷蛋白：Lv，卵黄脂蛋白：Pv）的表观分子量，分别为~560、>669和~58 kDa。在SDS-PAGE后，这些纯化的产物（即，Vtg、Lv和Pv）分别出现约210、约110和约22 kDa的条带。在Western印迹上，抗纯化的Vtg、Lv和Pv的抗血清识别~210 kDa的Vtg条带。与硬骨鱼Pv相反，猫鲨Pv具有非常低的丝氨酸含量。猫鲨VtgcDNA序列（vtg）含有一个由编码Lv、Pv和β ′-c的结构域组成的开放阅读框。一项系统发育分析，考虑到基因组复制事件，将猫鲨vtg归入“vtgAB型”。结论：猫鲨kvtgAB基因至少有一种主要的Vtg蛋白是3种卵黄蛋白（Lv、Pv和β′-c）的前体，该蛋白由猫鲨kvtgAB基因转录和翻译而成。
Elasmobranchs (sharks and rays) exhibit unique reproductive characteristics and, in contrast to the situation in teleosts, very little is known about the identity, structure and physical characteristics of their egg yolk proteins. The aims of this study were to (1) detect and purify the vitellogenin (Vtg; egg yolk precursor) and yolk proteins (YPs) of the cloudy catshark (Scyliorhinus torazame), (2) examine the relationships between Vtg and YPs and (3) characterize and classify the deduced primary structure of the Vtg transcript (vtg). The apparent molecular weights of purified Vtg and putative Vtg-related YPs (lipovitellin: Lv, phosvitin: Pv) were determined by gel filtration and were ~560, >669 and ~58 kDa, respectively. Following SDS-PAGE, these purified products (i.e., Vtg, Lv and Pv) appeared as bands of ~210, ~110 and ~22 kDa, respectively. On Western blots, antisera against purified Vtg, Lv and Pv recognized the ~210 kDa Vtg band. Catshark Pv, in contrast to teleost Pvs, had a very low serine content. The catshark Vtg cDNA sequence (vtg) appeared to contain an open-reading frame consisting of domains encoding Lv, Pv and β′-component (β′-c). A phylogenetic analysis, with a consideration of genome duplication events, placed catsharkvtginto the ‘vtgABtype.’ It is concluded that at least a single major type of Vtg protein, which is transcribed and translated from catsharkvtgABgene, is the precursor of three egg yolk proteins (Lv, Pv and β′-c) in catshark.