Nature of the immunoreactive neurophysins in ectopic vasopressin-producing oat cell carcinomas of the lung. Demonstration of a putative common precursor to vasopressin and neurophysin.

Nature of the immunoreactive neurophysins in ectopic vasopressin-producing oat cell carcinomas of the lung. Demonstration of a putative common precursor to vasopressin and neurophysin.
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产生异位加压素的肺燕麦细胞癌中免疫反应性神经素的性质。

DOI:
10.1172/jci110267
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发表时间:
1981
期刊:
The Journal of clinical investigation
影响因子:
--
通讯作者:
S. Katayamá
S. Katayamá
中科院分区:
--
文献类型:
--
作者:
T. Yamaji;M. Ishibashi;S. Katayamá

文献摘要

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为了描述具有异位加压素产生的肺燕麦细胞癌中免疫反应性神经生理素的性质,通过凝胶过滤和电泳对肿瘤神经生理素进行了表征。在所有五种肿瘤组织中,通过放射免疫测定法测定了加压素和尼古丁刺激的神经素(NSN)的活性。在三个组织中检测到少量催产素以及雌激素刺激的神经素。当组织提取物在 0.2 N 乙酸中进行 Sephadex G-50 凝胶过滤时,免疫反应性 NSN 的主要部分出现在相当于 10,000 分子大小的级分中。这些组分中 NSN 的电泳迁移模式在质量上与从人垂体后叶提取的 NSN 相同。除了这种主要的神经生理素之外,分子大小为 20,000 的免疫反应性 NSN 在三种肿瘤提取物中得到一致证明。这种高分子量形式的神经素在每个肿瘤提取物中占总 NSN 免疫活性的 6.5--8.7%,并且在 6 M 盐酸胍变性条件下进行分析时,其洗脱曲线没有改变。电泳时,它迁移到丙种球蛋白区域附近;然而,峰很宽,表明它由两个以上不同的分子群组成。从与刀豆球蛋白 A 的结合来看,高分子量 NSN 的很大一部分似乎是糖蛋白。当高分子量神经素与胰蛋白酶一起孵育时,基本上所有活性都转化为分子大小为 10,000 的 NSN。此外,治疗后释放出等摩尔量的加压素,其洗脱模式与合成精氨酸加压素的洗脱模式非常相似。当使用较低浓度的胰蛋白酶时,一些 20,000 道尔顿的神经素表现出 NSN 和加压素的活性。由于本研究中使用的抗加压素血清似乎针对加压素的环部分侧,因此这些结果表明,这种 20,000 道尔顿的神经素很可能是加压素和神经素的共同前体,并且加压素可能位于前体分子的中间。
In an attempt to delineate the nature of the immunoreactive neurophysins in oat cell carcinomas of the lung with ectopic vasopressin production, tumor neurophysins were characterized by gel filtration and by electrophoresis. In all of the five tumor tissues, activities of both vasopressin and nicotine-stimulated neurophysin (NSN) determined by radioimmunoassay were demonstrated. A small amount of oxytocin as well as estrogen-stimulated neurophysin was detected in three of the tissues. When tissue extract was subjected to Sephadex G-50 gel filtration in 0.2 N acetic acid, the major portion of immunoreactive NSN emerged in the fractions corresponding to the molecular size of 10,000. The migration pattern of NSN in these fractions on electrophoresis was qualitatively the same as that of NSN extracted from human posterior pituitary glands. In addition to this major neurophysin, immunoreactive NSN with the molecular size of 20,000 was consistently demonstrated in three tumor extracts. This high molecular weight form of neurophysin represented 6.5--8.7% of total NSN immunoactivities in each tumor extract and its elution profile was not changed when analyzed under denaturating conditions in 6 M guanidine hydrochloride. On electrophoresis, it migrated near the gamma globulin region; however, the peak was broad suggesting that it consists of more than two different molecular populations. A substantial portion of the high molecular weight NSN appears to be a glycoprotein judging from its binding to concanavalin A. When the high molecular weight from of neurophysin was incubated with trypsin, essentially all of the activities were converted into NSN with the molecular size of 10,000. Moreover, an equimolar amount of vasopressin was liberated after the treatment, the elution pattern of which closely resembled that of synthetic arginine vasopressin. When a lower concentration of trypsin was used, some of the 20,000-dalton neurophysin exhibited activities of both NSN and vasopressin. Since the antivasopressin serum used in this study appeared to be directed toward the ring portion side of vasopressin, these results suggest that this 20,000-dalton neurophysin is, in all probability, a common precursor to vasopressin and neurophysin, and that vasopressin may be located in the middle of the precursor molecule.