Molecular cloning and characterization of spiggin - An androgen-regulated extraorganismal adhesive with structural similarities to von Willebrand Factor-related proteins
Molecular cloning and characterization of spiggin - An androgen-regulated extraorganismal adhesive with structural similarities to von Willebrand Factor-related proteins
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DOI：
10.1074/jbc.m101142200
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发表时间：
2001-05-25
影响因子：
4.8
通讯作者：
Olsson, PE
中科院分区：
文献类型：
--
作者：
Jones, I;Lindberg, C;Olsson, PE
脊椎动物生物外结构蛋白最明确的例子之一可以在三刺棘鱼（Gasterosteus aculeatus）中找到。在繁殖的雄性中，肾脏肥大并合成一种称为“spiggin”的粘附蛋白，该蛋白从膀胱分泌到膀胱中，用作筑巢的结构线。本文描述了 spiggin 的第一个分子特征，并证明这种粘合剂是由三个不同亚基（α、β 和 γ）潜在组装而成的蛋白质复合物。这些亚基通过选择性剪接产生，11-酮雄激素诱导它们在刺鱼肾脏中表达。对每个亚基的预测氨基酸序列的分析揭示了一种模块化组织，其结构元件与冯维勒布兰德因子相关蛋白中发现的多聚化结构域相似。这些结果表明，spiggin 利用保守的多聚化机制，在雄性刺鱼的膀胱中从其组成亚基形成粘性凝集物，因此，这种新颖的生物外结构蛋白非常适合其作为粘合线的功能。
One of the most definitive examples of a vertebrate extraorganismal structural protein can be found in three-spined sticklebacks (Gasterosteus aculeatus), In the breeding male the kidney hypertrophies and synthesizes an adhesive protein called "spiggin,'" which is secreted into the urinary bladder from where it is employed as a structural thread for nest building. This paper describes the first molecular characterization of spiggin and demonstrates that this adhesive is a protein complex assembled from a potential of three distinct subunits (alpha, beta, and gamma). These subunits arise by alternative splicing, and 11-ketoandrogens induce their expression in stickleback kidneys. Analysis of the predicted amino acid sequence of each subunit reveals a modular organization whose structural elements display a similarity to the multimerization domains found within von Willebrand Factor-related proteins. These results implicate that spiggin utilizes a conserved multimerization mechanism for the formation of a viscous agglutinate from its constituent subunits in the urinary bladders of male sticklebacks, This novel extraorganismal structural protein is therefore ideally suited to its function as an adhesive thread.