课题基金 / 基金详情

THE STRUCTURAL BASIS OF RELAXIN ACTION

THE STRUCTURAL BASIS OF RELAXIN ACTION
放松作用的结构基础
批准号:
3324232
负责人:
christian none schwabe
金额:
$12.37万
依托单位国家:
美国
项目类别:
财政年份:
1988
资助国家:
美国
项目状态:
已结题
起止时间:
1988-03-01 至 1991-02-28

项目摘要

项目成果

christian none schwabe的其他基金

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中文摘要
翻译
松弛素是一种卵巢多肽激素,负责 那些导致产道加宽的组织改造 在分娩前。松弛素是在黄体中产生的 是胰岛素的二硫键同系物 既没有表现出生物胰岛素活性,也没有交叉反应 针对胰岛素产生的抗体。除了参与到 分娩松弛素可能在生育中发挥作用,因为 将卵子植入子宫内膜似乎是一种 松弛素介导的过程和精子活力似乎是 在松弛素存在的情况下增强。也有报道称, 松弛素在怀孕期间表现出一种抑制胰岛素的活性。 因此有可能成为治疗妊娠的潜在药物。 糖尿病。 这里提出的研究旨在了解 松弛蛋白的结构与其各种功能的关系。这个计划 就是从化学上剖析和重建 松弛表面并测量这种修饰的效果 关于其结构的完整性和生物活性 分子。眼下的目标之一是识别受体 松弛蛋白的相互作用部位,并在 这样一种与受体的共价键可以是 已经成立了。化学识别站点已添加到 松驰素分子在它们不干扰的地方 生物活性和这些部位现在应该用来分离 共价连接的松弛素受体复合体。然后尝试将 以获得关于 松弛素受体,最终将有助于构建 松弛素受体编码序列的核苷酸探针 可能是从适当的基因库中分离出来的。
英文摘要
Relaxin is an ovarian peptide hormone that is responsible for those tissue modifications that result in birth canal widening just prior to parturition. Relaxin is produced in the corpus luteum of pregnancy or in the placenta and is a disulfide homolog of insulin that exhibits neither biological insulin activity nor crossreactivity to antibodies raised against insulin. Besides the involvement in parturition relaxin may play a role in fertility in that the implantation of an ovum into the endometrium appears to be a relaxin-mediated process and sperm motility appears to be enhanced in the presence of relaxin. It has also been reported that relaxin exhibits an insulin-sparing activity during pregnancy and thus may be a potential drug for the treatment of pregnancy diabetes. The studies proposed here are aimed at an understanding of the relationship of relaxin structure to its various functions. The plan is to chemically dissect and reconstitute various aspects of the relaxin surface and to measure the effect of such modifications on the structural integrity and the biological activity of the molecule. One of the immediate goals is to identify the receptor interaction site of relaxin and to modify this interaction site in such a way that a covalent link with the receptor may be established. Chemical recognition sites have been added to the relaxin molecule in places where they do not interfere with biological activity and these sites should now serve to isolate the covalently-linked relaxin receptor complex. Attempts will then be made to obtain partial sequence information concerning the relaxin receptor that would eventually aid in the construction of a nucleotide probe with which a relaxin receptor-coding sequence may be isolated from the appropriate gene library.
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