Related Experiment Video
Updated: Feb 14, 2026

In Vitro Assays to Evaluate the Migration, Invasion, and Proliferation of Immortalized Human First-trimester Trophoblast Cell Lines
Published on: March 5, 2019
TRIM59 promotes cell proliferation, migration and invasion in human hepatocellular carcinoma cells
Abstract:
The human tripartite motif (TRIM) 59 has been implicated in tumorigenesis of many types of cancer. However, the biological function and molecular mechanism of TRIM59 in hepatocellular carcinoma (HCC) remains unknown. In our study, the purpose was to investigate the impact of TRIM59 on the biologic behavior of HCC cells. We observed that TRIM59 was highly expressed in HCC cells compared with a normal human hepatocyte cell line. Lentivirus-mediated knocking down of TRIM59 significantly suppressed the proliferation, migration and invasion of HCC cells, whereas overexpression of TRIM59 enhanced cell growth and metastasis. Furthermore, our study showed that silencing of TRIM59 decreased the expression of E-cadherin and increased N-cadherin and vimentin expression, whereas TRIM59 overexpression had the opposite effects on the above proteins. Finally, we found that p53 protein expression level was regulated by TRIM59, so we proposed that TRIM59 may enhance HCC cell proliferation and metastasis through p53 signaling pathway. In summary, these data indicated that TRIM59 may be a potential biomarker and therapeutic target for the treatment of hepatocellular carcinoma.
More Related Videos
10:35Generation of Subcutaneous and Intrahepatic Human Hepatocellular Carcinoma Xenografts in Immunodeficient Mice
Published on: September 25, 2013
10:18Exploring the Potential of Mesenchymal Stem Cell Sheet on The Development of Hepatocellular Carcinoma In Vivo
Published on: September 11, 2018
Related Concept Videos
Cell Migration
Cell Migration
Cells Coordinate Growth and Proliferation
Cancer Cell Migration through Invadopodia
Chemotaxis and Direction of Cell Migration
Role of Myosin in Cell Migration
Myosin II is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction....