Overexpression of ERp29 in the thyrocytes of FRTL-5 cells

Cited 26 time in webofscience Cited 0 time in scopus
  • Hit : 67
  • Download : 0
DC FieldValueLanguage
dc.contributor.authorPark, Soojungko
dc.contributor.authorYou, Kwan-Heeko
dc.contributor.authorShong, Minhoko
dc.contributor.authorGoo, Tae Wonko
dc.contributor.authorYun, Eun Youngko
dc.contributor.authorKang, Seok Wooko
dc.contributor.authorKwon, O Yuko
dc.date.accessioned2023-04-16T02:00:37Z-
dc.date.available2023-04-16T02:00:37Z-
dc.date.created2023-04-12-
dc.date.created2023-04-12-
dc.date.issued2005-03-
dc.identifier.citationMOLECULAR BIOLOGY REPORTS, v.32, no.1, pp.7 - 13-
dc.identifier.issn0301-4851-
dc.identifier.urihttp://hdl.handle.net/10203/306318-
dc.description.abstractIt was previously reported that the up-regulation of ERp29 mRNA depends on the levels of thyroid stimulating hormone (TSH) in the thyrocytes of FRTL-5 cells. In order to investigate the putative new function of ERp29 as an endoplasmic molecular (ER) chaperone, an ERp29-overexpressing FRTL-5 cell line was established. This cell line had approximately three times the levels of ERp29 protein and an enhanced level of thyroglobulin (Tg) secretion. The results showed both enhanced ERp29 expression and an interaction with the other ER chaperones such as GRP94, BiP, ERp72 and calnexin. In addition, ERp29 enhanced the expression of PKR-like ER kinase (PERK), which is a transmembrane protein located in the ER membrane. These findings suggest that ERp29 assists in protein folding as well as in the secretion of the secretory/plasma membrane proteins under close co-operation with other ER chaperones and the ER stress signaler, PERK.-
dc.languageEnglish-
dc.publisherSPRINGER-
dc.titleOverexpression of ERp29 in the thyrocytes of FRTL-5 cells-
dc.typeArticle-
dc.identifier.wosid000228582500002-
dc.identifier.scopusid2-s2.0-18444402788-
dc.type.rimsART-
dc.citation.volume32-
dc.citation.issue1-
dc.citation.beginningpage7-
dc.citation.endingpage13-
dc.citation.publicationnameMOLECULAR BIOLOGY REPORTS-
dc.identifier.doi10.1007/s11033-004-3069-3-
dc.contributor.localauthorShong, Minho-
dc.contributor.nonIdAuthorPark, Soojung-
dc.contributor.nonIdAuthorYou, Kwan-Hee-
dc.contributor.nonIdAuthorGoo, Tae Won-
dc.contributor.nonIdAuthorYun, Eun Young-
dc.contributor.nonIdAuthorKang, Seok Woo-
dc.contributor.nonIdAuthorKwon, O Yu-
dc.description.isOpenAccessN-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorER chaperone-
dc.subject.keywordAuthorERp29-
dc.subject.keywordAuthorFRTL-5 cells-
dc.subject.keywordAuthorthyroglobulin-
dc.subject.keywordPlusENDOPLASMIC-RETICULUM PROTEIN-
dc.subject.keywordPlusCONGENITAL GOITER-
dc.subject.keywordPlusSTORAGE DISEASE-
dc.subject.keywordPlusTHYROGLOBULIN-
dc.subject.keywordPlusSTRESS-
dc.subject.keywordPlusCHAPERONE-
dc.subject.keywordPlusRESIDENT-
dc.subject.keywordPlusHYPOTHYROIDISM-
dc.subject.keywordPlusIDENTIFICATION-
dc.subject.keywordPlusMODEL-
Appears in Collection
MSE-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 26 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0