Incorporation of arylphorins (LSP-1) and LSP-2 like protein into the integument of Ceratitis capitata during pupariation

Sotiris Tsakas, Panagiotis G. Katsoris, Kostas Bourtzis, Vassilis J. Marmaras
{"title":"Incorporation of arylphorins (LSP-1) and LSP-2 like protein into the integument of Ceratitis capitata during pupariation","authors":"Sotiris Tsakas,&nbsp;Panagiotis G. Katsoris,&nbsp;Kostas Bourtzis,&nbsp;Vassilis J. Marmaras","doi":"10.1016/0020-1790(91)90104-M","DOIUrl":null,"url":null,"abstract":"<div><p>The arylphorins and LSP-2 like polypeptide were detected by immunoblotting analysis during development in the integument of <em>C. capitata</em>. <em>In vitro</em> translation of total RNA from fat body and integument during pupariation, clearly revealed that the polypeptides under consideration were exclusively synthesized in the fat body. Furthermore, <em>in vitro</em> experiments demonstrated that radiolabeled arylphorins and LSP-2 like polypeptide were taken up by the integument, in an undegraded state. Immunofluorescence experiments in cross sections of wandering stage larvae and white pupae revealed that the LSP-2 like polypeptide was mainly localized in the epidermal cells, and a very weak signal was also given by the cuticle. Furthermore, the presented results indicated that a small portion of the extracted proteins exist in high molecular weight aggregate(s).</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 5","pages":"Pages 507-515"},"PeriodicalIF":0.0000,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90104-M","citationCount":"7","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Insect Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/002017909190104M","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 7

Abstract

The arylphorins and LSP-2 like polypeptide were detected by immunoblotting analysis during development in the integument of C. capitata. In vitro translation of total RNA from fat body and integument during pupariation, clearly revealed that the polypeptides under consideration were exclusively synthesized in the fat body. Furthermore, in vitro experiments demonstrated that radiolabeled arylphorins and LSP-2 like polypeptide were taken up by the integument, in an undegraded state. Immunofluorescence experiments in cross sections of wandering stage larvae and white pupae revealed that the LSP-2 like polypeptide was mainly localized in the epidermal cells, and a very weak signal was also given by the cuticle. Furthermore, the presented results indicated that a small portion of the extracted proteins exist in high molecular weight aggregate(s).

在羽化过程中,芳基蛋白(LSP-1)和LSP-2样蛋白进入头状certis的被膜
采用免疫印迹法检测了香菇被皮发育过程中芳烃蛋白和LSP-2样多肽的含量。体外翻译脂肪体和被膜的总RNA,清楚地表明所考虑的多肽完全是在脂肪体中合成的。此外,体外实验表明,放射性标记的芳基蛋白和LSP-2样多肽被被膜吸收,处于未降解状态。游离期幼虫和白色蛹的横断面免疫荧光实验显示,LSP-2样多肽主要定位于表皮细胞,角质层也发出极弱的信号。此外,本文的结果表明,提取的蛋白质中有一小部分存在高分子量聚集体。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信