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Protein arginine methyltransferase 5 is essential for growth of lung cancer cells
- Source :
- The Biochemical journal. 446(2)
- Publication Year :
- 2012
-
Abstract
- PRMT5 (protein arginine methyltransferase 5) is an enzyme that catalyses transfer of methyl groups from S-adenosyl methionine to the arginine residues of histones or non-histone proteins and is involved in a variety of cellular processes. Although it is highly expressed in some tumours, its direct role in cancer growth has not been fully investigated. In the present study, in human lung tissue samples we found that PRMT5 was highly expressed in lung cancer cells, whereas its expression was not detectable in benign lung tissues. Silencing PRMT5 expression strongly inhibited proliferation of lung adenocarcinoma A549 cells in tissue culture, and silencing PRMT5 expression in A549 cells also abolished growth of lung A549 xenografts in mice. In vitro and in vivo studies showed that the cell growth arrest induced by loss of PRMT5 expression was partially attributable to down-regulation of fibroblast growth factor receptor signalling. These results suggest that PRMT5 and its methyltransferase activity is essential for proliferation of lung cancer cells and may serve as a novel target for the treatment of lung cancer.
- Subjects :
- Protein-Arginine N-Methyltransferases
Lung Neoplasms
Arginine
Mice, Nude
Biology
Adenocarcinoma
Biochemistry
Article
Mice
Cell Line, Tumor
medicine
Animals
Humans
Receptor, Fibroblast Growth Factor, Type 3
Gene Silencing
RNA, Small Interfering
Lung cancer
Molecular Biology
Lung
Cell Proliferation
A549 cell
Protein arginine methyltransferase 5
Gene Expression Profiling
Cancer
Cell Biology
respiratory system
medicine.disease
Molecular biology
Small Cell Lung Carcinoma
Recombinant Proteins
respiratory tract diseases
Neoplasm Proteins
Tumor Burden
Cell culture
Fibroblast growth factor receptor
Cancer research
Carcinoma, Squamous Cell
Mutant Proteins
Neoplasm Transplantation
Signal Transduction
Subjects
Details
- ISSN :
- 14708728
- Volume :
- 446
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- The Biochemical journal
- Accession number :
- edsair.doi.dedup.....ab6413def82bcd75d7f858ba907d7643