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PRDM14 Promotes the Migration of Human Non-small Cell Lung Cancer Through Extracellular Matrix Degradation in vitro
BACKGROUND: As a novel molecular markerof non-small cell lung cancer (NSCLC), PRDI-BF1 and RIZ homology domain containing protein 14 (PRDM14) is over-expressed in NSCLC tumor tissues. Extracellular matrix degradation mediated by the balance between matrix metalloproteinases (MMPs) and tissue inhibit...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Medknow Publications & Media Pvt Ltd
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4837869/ https://www.ncbi.nlm.nih.gov/pubmed/25635434 http://dx.doi.org/10.4103/0366-6999.150109 |
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author | Bi, Hong-Xia Shi, Han-Bing Zhang, Ting Cui, Ge |
author_facet | Bi, Hong-Xia Shi, Han-Bing Zhang, Ting Cui, Ge |
author_sort | Bi, Hong-Xia |
collection | PubMed |
description | BACKGROUND: As a novel molecular markerof non-small cell lung cancer (NSCLC), PRDI-BF1 and RIZ homology domain containing protein 14 (PRDM14) is over-expressed in NSCLC tumor tissues. Extracellular matrix degradation mediated by the balance between matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMPs) is one of the most important mechanism in lung cancer metastasis. This study aimed to determine if PRDM14 promoted the migration of NSCLC cells through extracellular matrix degradation mediated by change of MMP/TIMP expression. METHODS: The expression of PRDM14 was down-regulated in human cell line A 549 after transfection with lentiviral vector-mediated short-hairpin ribonucleic acids (shRNAs) which targeted the PRDM14 promoter. Cellular migration of shRNA-infected cells was detected by a scratch wound healing assay and transwell cell migration assay. Expression levels of MMP1, MMP2, TIMP1, and TIMP2 were measured by quantitative real-time polymerase chain reaction (RT-PCR). RESULTS: Migration of PRDM14-shRNA-infected cells was significantly inhibited relative to control cells as measured by the scratch wound healing (P < 0.05) and transwell cell migration assays (P < 0.01). The expression of MMP1 in A549 cells infected by PRDM14-shRNA was down-regulated significantly (P < 0.01), whereas the expression of TIMP1 and TIMP2 was up-regulated significantly (P < 0.01). CONCLUSIONS: PRDM14 accelerates A549 cells migration in vitro through extracellular matrix degradation. PRDM14 is considered as a potential therapeutic target in metastatic NSCLC. |
format | Online Article Text |
id | pubmed-4837869 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Medknow Publications & Media Pvt Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-48378692016-05-02 PRDM14 Promotes the Migration of Human Non-small Cell Lung Cancer Through Extracellular Matrix Degradation in vitro Bi, Hong-Xia Shi, Han-Bing Zhang, Ting Cui, Ge Chin Med J (Engl) Original Article BACKGROUND: As a novel molecular markerof non-small cell lung cancer (NSCLC), PRDI-BF1 and RIZ homology domain containing protein 14 (PRDM14) is over-expressed in NSCLC tumor tissues. Extracellular matrix degradation mediated by the balance between matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMPs) is one of the most important mechanism in lung cancer metastasis. This study aimed to determine if PRDM14 promoted the migration of NSCLC cells through extracellular matrix degradation mediated by change of MMP/TIMP expression. METHODS: The expression of PRDM14 was down-regulated in human cell line A 549 after transfection with lentiviral vector-mediated short-hairpin ribonucleic acids (shRNAs) which targeted the PRDM14 promoter. Cellular migration of shRNA-infected cells was detected by a scratch wound healing assay and transwell cell migration assay. Expression levels of MMP1, MMP2, TIMP1, and TIMP2 were measured by quantitative real-time polymerase chain reaction (RT-PCR). RESULTS: Migration of PRDM14-shRNA-infected cells was significantly inhibited relative to control cells as measured by the scratch wound healing (P < 0.05) and transwell cell migration assays (P < 0.01). The expression of MMP1 in A549 cells infected by PRDM14-shRNA was down-regulated significantly (P < 0.01), whereas the expression of TIMP1 and TIMP2 was up-regulated significantly (P < 0.01). CONCLUSIONS: PRDM14 accelerates A549 cells migration in vitro through extracellular matrix degradation. PRDM14 is considered as a potential therapeutic target in metastatic NSCLC. Medknow Publications & Media Pvt Ltd 2015-02-05 /pmc/articles/PMC4837869/ /pubmed/25635434 http://dx.doi.org/10.4103/0366-6999.150109 Text en Copyright: © 2015 Chinese Medical Journal http://creativecommons.org/licenses/by-nc-sa/3.0 This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 License, which allows others to remix, tweak, and build upon the work non-commercially, as long as the author is credited and the new creations are licensed under the identical terms. |
spellingShingle | Original Article Bi, Hong-Xia Shi, Han-Bing Zhang, Ting Cui, Ge PRDM14 Promotes the Migration of Human Non-small Cell Lung Cancer Through Extracellular Matrix Degradation in vitro |
title | PRDM14 Promotes the Migration of Human Non-small Cell Lung Cancer Through Extracellular Matrix Degradation in vitro |
title_full | PRDM14 Promotes the Migration of Human Non-small Cell Lung Cancer Through Extracellular Matrix Degradation in vitro |
title_fullStr | PRDM14 Promotes the Migration of Human Non-small Cell Lung Cancer Through Extracellular Matrix Degradation in vitro |
title_full_unstemmed | PRDM14 Promotes the Migration of Human Non-small Cell Lung Cancer Through Extracellular Matrix Degradation in vitro |
title_short | PRDM14 Promotes the Migration of Human Non-small Cell Lung Cancer Through Extracellular Matrix Degradation in vitro |
title_sort | prdm14 promotes the migration of human non-small cell lung cancer through extracellular matrix degradation in vitro |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4837869/ https://www.ncbi.nlm.nih.gov/pubmed/25635434 http://dx.doi.org/10.4103/0366-6999.150109 |
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