ID 110162
Author
Saijo, Saki Department of Pathophysiology, Institute of Biomedical Sciences, Tokushima University Graduate School.
Kuwano, Yuki Department of Pathophysiology, Institute of Biomedical Sciences, Tokushima University Graduate School. Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Masuda, Kiyoshi Department of Pathophysiology, Institute of Biomedical Sciences, Tokushima University Graduate School. KAKEN Search Researchers
Nishikawa, Tatsuya Department of Pathophysiology, Institute of Biomedical Sciences, Tokushima University Graduate School. Tokushima University Educator and Researcher Directory
Rokutan, Kazuhiro Department of Pathophysiology, Institute of Biomedical Sciences, Tokushima University Graduate School. Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Nishida, Kensei Department of Pathophysiology, Institute of Biomedical Sciences, Tokushima University Graduate School. Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Keywords
SRSF7
cell cycle
p21
G1/S arrest
Content Type
Journal Article
Description
Serine/arginine-rich splicing factors (SRSFs) play wide-ranging roles in gene expression through post-transcriptional regulation as well as pre-mRNA splicing. SRSF7 was highly expressed in colon cancer tissues, and its knockdown inhibited cell growth in colon cancer cells (HCT116) in association with altered expression of 4,499 genes. The Ingenuity Pathway Analysis revealed that cell cycle-related canonical pathways were ranked as the highly enriched category in the affected genes. Western blotting confirmed that p21, a master regulator in cell cycle, was increased without any induction of p53 in SRSF7 knockdown cells. Furthermore, cyclin-dependent kinase 2 and retinoblastoma protein were remained in the hypophosphorylated state. In addition, the SRSF7 knockdown-induced cell growth inhibition was observed in p53-null HCT116 cells, suggesting that p53-independent pathways were involved in the SRSF7 knockdown-induced cell growth inhibition. The reduction of SRSF7 stabilized cyclin-dependent kinase inhibitor 1A (CDKN1A) mRNA without any activation of the CDKN1A promoter. Interestingly, SRSF7 knockdown also blocked p21 degradation. These results suggest that the reduction of SRSF7 post-transcriptionally regulates p21 induction at the multistep processes. Thus, the present findings disclose a novel, important role of SRSF7 in cell proliferation through regulating p21 levels.
Journal Title
The journal of medical investigation : JMI
ISSN
13431420
NCID
AA11166929
Volume
63
Issue
3-4
Start Page
219
End Page
226
Sort Key
219
Published Date
2016-08
EDB ID
URL ( Publisher's Version )
FullText File
language
eng
TextVersion
Publisher
departments
Medical Sciences