Background： As a novel molecular markerof non-small cell lung cancer （NSCLC）, PRDI-BFI and R1Z homology domain containing protein 14 （PRDM 14） is over-expressed ill NSCLC tumor tissues. Extracellular matrix degra...Background： As a novel molecular markerof non-small cell lung cancer （NSCLC）, PRDI-BFI and R1Z homology domain containing protein 14 （PRDM 14） is over-expressed ill 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 king 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 PRDM 14 was down-regulated in human cell line A 549 after transfection with lentiviral vector-mediated short-hairpin ribonucleic acids （shRNAs） which targeted the PRDM 14 promoter. Cellular migration ofshRNA-infected cells was detected by a scratch wound healing assay and transwell cell rnigration assay. Expression levels of MMP1, MMP2, TIMP1, and TIMP2 were measured by quantitative real-time polymerase chain reaction （RT-PCR）. Results： Migration of PRDM 14-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 MMPI in A549 cells infected by PRDMI4-shRNA was down-regulated significantly （P 〈 0.01 ）, whereas the expression ofTIMP 1 and TIMP2 was up-regulated significantly （P 〈 0.01 ）. Conclusions： PRDM 14 accelerates A549 cells migration in vitro through extracellular matrix degradation. PRDM 14 is considered as a potential therapeutic target in metastatic NSCLC.展开更多
文摘Background： As a novel molecular markerof non-small cell lung cancer （NSCLC）, PRDI-BFI and R1Z homology domain containing protein 14 （PRDM 14） is over-expressed ill 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 king 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 PRDM 14 was down-regulated in human cell line A 549 after transfection with lentiviral vector-mediated short-hairpin ribonucleic acids （shRNAs） which targeted the PRDM 14 promoter. Cellular migration ofshRNA-infected cells was detected by a scratch wound healing assay and transwell cell rnigration assay. Expression levels of MMP1, MMP2, TIMP1, and TIMP2 were measured by quantitative real-time polymerase chain reaction （RT-PCR）. Results： Migration of PRDM 14-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 MMPI in A549 cells infected by PRDMI4-shRNA was down-regulated significantly （P 〈 0.01 ）, whereas the expression ofTIMP 1 and TIMP2 was up-regulated significantly （P 〈 0.01 ）. Conclusions： PRDM 14 accelerates A549 cells migration in vitro through extracellular matrix degradation. PRDM 14 is considered as a potential therapeutic target in metastatic NSCLC.
