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Transduction of PTEN Proteins Using the Tat Domain Modulates TGF-beta 1-Mediated Signaling Pathways and Transdifferentiation in Subconjunctival Fibroblasts
DC Field | Value | Language |
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dc.contributor.author | 이형근 | - |
dc.date.accessioned | 2014-12-19T16:59:31Z | - |
dc.date.available | 2014-12-19T16:59:31Z | - |
dc.date.issued | 2012 | - |
dc.identifier.issn | 0146-0404 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/90576 | - |
dc.description.abstract | PURPOSE: This study investigated the effects of the tumor suppressor protein PTEN (phosphatase and tensin homolog) on transforming growth factor (TGF)-β1-mediated signaling pathways and the transdifferentiation of human subconjunctival fibroblasts (SCFs) after the transduction of this protein containing a transactivator of transcription (Tat) domain. METHODS: The Tat-PTEN expression vector was constructed to express the Tat domain of HIV-1 fused to PTEN. After transduction of the fusion protein and TGF-β1 stimulation, the dose-dependent effect of the transduced Tat-PTEN fusion protein on Akt phosphorylation and the stability of the Tat-PTEN fusion protein in SCF cells were evaluated by Western blot analysis. The effect of the Tat-PTEN fusion protein on the TGF-β1-stimulated expression of α-SMA and fibronectin was also evaluated by Western blot analysis and immunocytochemistry. RESULTS: To increase the efficiency of enzyme activity and to successfully deliver this protein to cells, the authors used a PTEN fusion protein that contained the transduction domain of the Tat protein from HIV-1. By Western blot analysis, the transduced Tat-PTEN fusion protein was found to modulate TGF-β1 signaling in SCF cells and result in the suppression of Akt phosphorylation. Furthermore, the transduction of the Tat-PTEN fusion protein was found to suppress the TGF-β1-stimulated expression of α-SMA and fibronectin by Western blot analysis and immunocytochemical staining, and the effects of the transduced fusion protein could be controlled in a dose-dependent manner. CONCLUSIONS: The Tat-PTEN fusion proteins were successfully transduced into the SCF cells and induced the suppression of transdifferentiation and fibrosis through the regulation of TGF-β-mediated signaling. The ability of the Tat-PTEN fusion protein to regulate cell survival could potentially be applied to protein therapy to counteract postoperative scarring in glaucoma surgery. | - |
dc.description.statementOfResponsibility | open | - |
dc.format | application/pdf | - |
dc.relation.isPartOf | INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.title | Transduction of PTEN Proteins Using the Tat Domain Modulates TGF-beta 1-Mediated Signaling Pathways and Transdifferentiation in Subconjunctival Fibroblasts | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Ophthalmology (안과학) | - |
dc.contributor.googleauthor | Eun Jee Chung | - |
dc.contributor.googleauthor | Hyung Keun Lee | - |
dc.contributor.googleauthor | Sun-Ah Jung | - |
dc.contributor.googleauthor | Seung Jae Lee | - |
dc.contributor.googleauthor | Hee Youn Chee | - |
dc.contributor.googleauthor | Yong Ho Sohn | - |
dc.contributor.googleauthor | Joon H. Lee | - |
dc.identifier.doi | 10.1167/iovs.11-8491 | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A03303 | - |
dc.relation.journalcode | J01187 | - |
dc.identifier.eissn | 1552-5783 | - |
dc.contributor.alternativeName | Lee, Hyung Keun | - |
dc.contributor.affiliatedAuthor | Lee, Hyung Keun | - |
dc.citation.volume | 53 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 379 | - |
dc.citation.endPage | 386 | - |
dc.identifier.bibliographicCitation | INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE, Vol.53(1) : 379-386, 2012 | - |
dc.identifier.rimsid | 32845 | - |
dc.type.rims | ART | - |
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