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黑寡妇蜘蛛α-拉托毒素:一种突触前神经毒素,与胰岛素促分泌激素的胰高血糖素样肽-1家族具有结构同源性。

Black widow spider alpha-latrotoxin: a presynaptic neurotoxin that shares structural homology with the glucagon-like peptide-1 family of insulin secretagogic hormones.

作者信息

Holz G G, Habener J F

机构信息

Diabetes Unit, Howard Hughes Medical Institute, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA.

出版信息

Comp Biochem Physiol B Biochem Mol Biol. 1998 Oct;121(2):177-84. doi: 10.1016/s0305-0491(98)10088-3.

Abstract

alpha-Latrotoxin is a presynaptic neurotoxin isolated from the venom of the black widow spider Latrodectus tredecimguttatus. It exerts toxic effects in the vertebrate central nervous system by depolarizing neurons, by increasing [Ca2+]i and by stimulating uncontrolled exocytosis of neurotransmitters from nerve terminals. The actions of alpha-latrotoxin are mediated, in part, by a GTP-binding protein-coupled receptor referred to as CIRL or latrophilin. Exendin-4 is also a venom toxin, and it is derived from the salivary gland of the Gila monster Heloderma suspectum. It acts as an agonist at the receptor for glucagon-like peptide-1(7-36)-amide (GLP-1), thereby stimulating secretion of insulin from pancreatic beta-cells of the islets of Langerhans. Here is reported a surprising structural homology between alpha-latrotoxin and exendin-4 that is also apparent amongst all members of the GLP-1-like family of secretagogic hormones (GLP-1, glucagon, vasoactive intestinal polypeptide, secretin, pituitary adenylyl cyclase activating polypeptide). On the basis of this homology, we report the synthesis and initial characterization of a chimeric peptide (Black Widow GLP-1) that stimulates Ca2+ signaling and insulin secretion in human beta-cells and MIN6 insulinoma cells. It is also reported here that the GTP-binding protein-coupled receptors for alpha-latrotoxin and exendin-4 share highly significant structural similarity in their extracellularly-oriented amino-termini. We propose that molecular mimicry has generated conserved structural motifs in secretagogic toxins and their receptors, thereby explaining the evolution of defense or predatory strategies that are shared in common amongst distantly related species including spiders, lizards, and snakes. Evidently, the toxic effects of alpha-latrotoxin and exendin-4 are explained by their ability to interact with GTP-binding protein-coupled receptors that normally mediate the actions of endogenous hormones or neuropeptides.

摘要

α-拉托毒素是一种从黑寡妇蜘蛛(间斑寇蛛)毒液中分离出来的突触前神经毒素。它通过使神经元去极化、增加细胞内钙离子浓度([Ca2+]i)以及刺激神经末梢不受控制地释放神经递质,对脊椎动物中枢神经系统产生毒性作用。α-拉托毒素的作用部分是由一种称为CIRL或亲拉毒素的GTP结合蛋白偶联受体介导的。艾塞那肽-4也是一种毒液毒素,它源自希拉毒蜥的唾液腺。它作为胰高血糖素样肽-1(7-36)酰胺(GLP-1)受体的激动剂,从而刺激胰岛β细胞分泌胰岛素。本文报道了α-拉托毒素和艾塞那肽-4之间惊人的结构同源性,这种同源性在GLP-1样促分泌激素家族(GLP-1、胰高血糖素、血管活性肠多肽、促胰液素、垂体腺苷酸环化酶激活多肽)的所有成员中也很明显。基于这种同源性,我们报道了一种嵌合肽(黑寡妇GLP-1)的合成及初步表征,该嵌合肽可刺激人β细胞和MIN6胰岛素瘤细胞中的Ca2+信号传导和胰岛素分泌。本文还报道,α-拉托毒素和艾塞那肽-4的GTP结合蛋白偶联受体在其细胞外的氨基末端具有高度显著的结构相似性。我们提出,分子模拟在促分泌毒素及其受体中产生了保守的结构基序,从而解释了在包括蜘蛛、蜥蜴和蛇等远缘物种中共同存在的防御或捕食策略的进化。显然,α-拉托毒素和艾塞那肽-4的毒性作用是由于它们与通常介导内源性激素或神经肽作用的GTP结合蛋白偶联受体相互作用的能力所致。

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