Long non-coding RNA LINK-A promotes glioma cell growth and invasion via lactate dehydrogenase A

Oncol Rep. 2017 Sep;38(3):1525-1532. doi: 10.3892/or.2017.5806. Epub 2017 Jul 12.

Abstract

Long non-coding RNAs (lncRNAs) have recently been identified in mammals as new modulators of cancer origin and progression participating in various cellular pro-cesses. Long intergenic non-coding RNA for kinase activation (LINK-A), belonging to one of the intergenic lncRNAs, was reported to regulate signaling pathways correlated with triple-negative breast cancer. However, the expression and the functional role of LINK-A in glioma are still unclear. In the present study, we demonstrated that LINK-A was upregulated in human glioma cells compared with the expression noted in normal astrocytes. Knockdown of LINK-A inhibited cell proliferation, migration and invasion in U87 and U251 glioma cells. In addition, we found that lactate dehydrogenase A (LDH-A) was regulated by LINK-A, and enforced expression of LDH-A promoted glycolysis and proliferation in glioma cells. More importantly, we found that LDH-A was involved in the LINK-A-mediated proliferation and invasion of glioma cells. Collectively, these results provide new evidence of an important role for LINK-A in the development of glioma.

MeSH terms

  • Apoptosis / genetics
  • Brain Neoplasms / genetics
  • Cell Line, Tumor
  • Cell Movement / genetics*
  • Cell Proliferation / genetics*
  • Down-Regulation / genetics
  • Gene Expression Regulation, Neoplastic / genetics
  • Glioma / genetics*
  • Humans
  • Isoenzymes / genetics
  • L-Lactate Dehydrogenase / genetics*
  • Lactate Dehydrogenase 5
  • Neoplasm Invasiveness / genetics*
  • RNA Interference / physiology
  • RNA, Long Noncoding / genetics*
  • Signal Transduction / genetics
  • Transcriptional Activation / genetics
  • Triple Negative Breast Neoplasms / genetics
  • Up-Regulation / genetics

Substances

  • Isoenzymes
  • LINK-A long non-coding RNA, human
  • RNA, Long Noncoding
  • L-Lactate Dehydrogenase
  • Lactate Dehydrogenase 5