Peanut agglutinin specifically binds to a sperm region between the nucleus and mitochondria in tunicates and sea urchins.
Peanut agglutinin specifically binds to a sperm region between the nucleus and mitochondria in tunicates and sea urchins.
复制标题
花生凝集素与被囊类动物和海胆的细胞核和线粒体之间的精子区域特异性结合。
DOI：
10.1002/mrd.22982
复制
发表时间：
2018
影响因子：
2.5
通讯作者：
Sawada H.
中科院分区：
文献类型：
--
作者：
Nakazawa S;Shirae-Kurabayashi M;Sawada H.
花生凝集素（PNA）是一种确定的哺乳动物顶体标记物。然而，我们观察到PNA在海鞘精子的细胞核旁特异性地结合到一个独特的细胞内结构。在这里，我们描述了海洋无脊椎动物精子中的PNA结合结构。在海鞘、海胆和尾尾鱼的精子中，与线粒体和细胞核之间的区域结合的PNA。然而，在三种海鞘中，PNA结合物质未被钙离子载体离子霉素暴露，这表明它与顶体结构不同。相反，海鞘PNA结合区是通过离子霉素诱导的精子反应与线粒体一起从精子头部脱落的。海鞘PNA结合物质似乎可以与SDS溶解，但不能与Triton X-100溶解，这说明了它的洗涤剂抗性。凝集素、PHA‐L4、SSA和MAL‐I在与PNA‐结合区相似的区域被检测到，这表明它含有多种聚糖。PNA结合区域的位置和部分成分与已知的内质网（ER）衍生结构相似，尽管ER标记蛋白concanavalin A聚集在与PNA结合区域相邻但不重叠的区域。因此，我们得出结论，海鞘精子具有非顶体，抗Triton，富含聚糖的细胞内结构，可能在被囊动物和海胆的繁殖中发挥普遍作用，因为它存在于广泛的分类范围内。
Peanut agglutinin (PNA) is an established marker of the mammalian acrosome. However, we observed that PNA specifically binds to a unique intracellular structure alongside the nucleus in ascidian sperm. Here, we characterize the PNA‐binding structure in sperm of marine invertebrates. PNA bound to the region between the mitochondrion and nucleus in spermatozoa of ascidians, sea urchins, and an appendicularian. However, PNA‐binding substances were not exposed by the calcium ionophore ionomycin in three ascidian species, indicating that it is a distinct structure from the acrosome. Instead, the ascidian PNA‐binding region was shed with the mitochondrion from the sperm head via an ionomycin‐induced sperm reaction. The ascidian PNA‐binding substance appeared to be solubilized with SDS, but not Triton X–100, describing its detergent resistance. Lectins, PHA‐L4, SSA, and MAL‐I were detected at an area similar to the PNA‐binding region, suggesting that it contains a variety of glycans. The location and some of the components of the PNA‐binding region were similar to known endoplasmic reticulum (ER)‐derived structures, although the ER marker concanavalin A accumulated at an area adjacent to but not overlapping the PNA‐binding region. Therefore, we conclude that ascidian sperm possess a non‐acrosomal, Triton‐resistant, glycan‐rich intracellular structure that may play a general role in reproduction of tunicates and sea urchins given its presence across a wide taxonomic range.