Qin-Qin Song, Peng Sun, Juan Song, Lin-Jun Sheng, Jin Zhang, Jun Han
{"title":"[PrP106-126肽干扰14-3-3 - β二聚体的研究]。","authors":"Qin-Qin Song, Peng Sun, Juan Song, Lin-Jun Sheng, Jin Zhang, Jun Han","doi":"","DOIUrl":null,"url":null,"abstract":"<p><strong>Objective: </strong>To investigate both PrP and PrP106-126 peptide effect on 14-3-3beta dimeration.</p><p><strong>Methods: </strong>14-3-3beta were incubated with different does recombinant PrP or PrP106-126 peptide, both 14-3-3beta dimer and polymer were separated 15% non-denaturing polyacrylamide gel electrophoresis (PAGE) and the 14-3-3 dimers were evaluated using 14-3-3beta-specific Western blotting. And then,14-3-3beta dimeration buffer were incubated with different does recombinant PrP and 250 micromol/L PrP106-126 peptide, 14-3-3beta dimer and polymer were detected by above methods. Cellular 14-3-3 dimer were also detected after PrP106-126 peptide were added to HeLa cell for 8 hours.</p><p><strong>Results: </strong>Recombinant full-length PrP facilitated the dimerization of 14-3-3beta and PrP106-126 disturbed 14-3-3beta dimeration as both have dose dependence effect. PrP antagonized PrP106-126-induced 14-3-3beta dimer with PrP protein increase in vitro. Cellular 14-3-3 dimerization also decreased after treatment of peptide PrP106-126 on HeLa cells for 8 hours.</p><p><strong>Conclusion: </strong>[corrected] Dimerization process of 14-3-3beta was promoted by full-length PrP (PrP23-231) but inhibited by peptide PrP106-126 in vitro. PrP agonized PrP106-126-induced inhibition of 14-3-3 dimeration. PrP106-126 inhibited cellular 14-3-3 dimerization.</p>","PeriodicalId":70973,"journal":{"name":"中华实验和临床病毒学杂志","volume":"27 2","pages":"109-11"},"PeriodicalIF":0.0000,"publicationDate":"2013-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Study on PrP106-126 peptide disturbed dimeration of 14-3-3beta].\",\"authors\":\"Qin-Qin Song, Peng Sun, Juan Song, Lin-Jun Sheng, Jin Zhang, Jun Han\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><strong>Objective: </strong>To investigate both PrP and PrP106-126 peptide effect on 14-3-3beta dimeration.</p><p><strong>Methods: </strong>14-3-3beta were incubated with different does recombinant PrP or PrP106-126 peptide, both 14-3-3beta dimer and polymer were separated 15% non-denaturing polyacrylamide gel electrophoresis (PAGE) and the 14-3-3 dimers were evaluated using 14-3-3beta-specific Western blotting. And then,14-3-3beta dimeration buffer were incubated with different does recombinant PrP and 250 micromol/L PrP106-126 peptide, 14-3-3beta dimer and polymer were detected by above methods. Cellular 14-3-3 dimer were also detected after PrP106-126 peptide were added to HeLa cell for 8 hours.</p><p><strong>Results: </strong>Recombinant full-length PrP facilitated the dimerization of 14-3-3beta and PrP106-126 disturbed 14-3-3beta dimeration as both have dose dependence effect. PrP antagonized PrP106-126-induced 14-3-3beta dimer with PrP protein increase in vitro. Cellular 14-3-3 dimerization also decreased after treatment of peptide PrP106-126 on HeLa cells for 8 hours.</p><p><strong>Conclusion: </strong>[corrected] Dimerization process of 14-3-3beta was promoted by full-length PrP (PrP23-231) but inhibited by peptide PrP106-126 in vitro. PrP agonized PrP106-126-induced inhibition of 14-3-3 dimeration. PrP106-126 inhibited cellular 14-3-3 dimerization.</p>\",\"PeriodicalId\":70973,\"journal\":{\"name\":\"中华实验和临床病毒学杂志\",\"volume\":\"27 2\",\"pages\":\"109-11\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2013-04-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"中华实验和临床病毒学杂志\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"中华实验和临床病毒学杂志","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Study on PrP106-126 peptide disturbed dimeration of 14-3-3beta].
Objective: To investigate both PrP and PrP106-126 peptide effect on 14-3-3beta dimeration.
Methods: 14-3-3beta were incubated with different does recombinant PrP or PrP106-126 peptide, both 14-3-3beta dimer and polymer were separated 15% non-denaturing polyacrylamide gel electrophoresis (PAGE) and the 14-3-3 dimers were evaluated using 14-3-3beta-specific Western blotting. And then,14-3-3beta dimeration buffer were incubated with different does recombinant PrP and 250 micromol/L PrP106-126 peptide, 14-3-3beta dimer and polymer were detected by above methods. Cellular 14-3-3 dimer were also detected after PrP106-126 peptide were added to HeLa cell for 8 hours.
Results: Recombinant full-length PrP facilitated the dimerization of 14-3-3beta and PrP106-126 disturbed 14-3-3beta dimeration as both have dose dependence effect. PrP antagonized PrP106-126-induced 14-3-3beta dimer with PrP protein increase in vitro. Cellular 14-3-3 dimerization also decreased after treatment of peptide PrP106-126 on HeLa cells for 8 hours.
Conclusion: [corrected] Dimerization process of 14-3-3beta was promoted by full-length PrP (PrP23-231) but inhibited by peptide PrP106-126 in vitro. PrP agonized PrP106-126-induced inhibition of 14-3-3 dimeration. PrP106-126 inhibited cellular 14-3-3 dimerization.
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