title: Alpha-enolase as a potential cancer prognostic marker promotes cell growth, migration, and invasion in glioma.
abstract: BACKGROUND
  The success of using glycolytic inhibitors for cancer treatment relies on better understanding the roles of each frequently deregulated glycolytic genes in cancer. This report analyzed the involvement of a key glycolytic enzyme, alpha-enolase (ENO1), in tumor progression and prognosis of human glioma.
  
  
  METHODS
  ENO1 expression levels were examined in glioma tissues and normal brain (NB) tissues. The molecular mechanisms of ENO1 expression and its effects on cell growth, migration and invasion were also explored by 3-[4,5-dimethylthiazol-2-yl]-2,5 diphenyl tetrazolium bromide (MTT) assay, Transwell chamber assay, Boyden chamber assay, Western blot and in vivo tumorigenesis in nude mice.
  
  
  RESULTS
  ENO1 mRNA and protein levels were upregulated in glioma tissues compared to NB. In addition, increased ENO1 was associated disease progression in glioma samples. Knocking down ENO1 expression not only significantly decreased cell proliferation, but also markedly inhibited cell migration and invasion as well as in vivo tumorigenesis. Mechanistic analyses revealed that Cyclin D1, Cyclin E1, pRb, and NF-κB were downregulated after stable ENO1 knockdown in glioma U251 and U87 cells. Conversely, knockdown of ENO1 resulted in restoration of E-cadherin expression and suppression of mesenchymal cell markers, such as Vimentin, Snail, N-Cadherin, β-Catenin and Slug. Furthermore, ENO1 suppression inactivated PI3K/Akt pathway regulating the cell growth and epithelial-mesenchymal transition (EMT) progression.
  
  
  CONCLUSIONS
  Overexpression of ENO1 is associated with glioma progression. Knockdown of ENO1 expression led to suppressed cell growth, migration and invasion progression by inactivating the PI3K/Akt pathway in glioma cells.
authors.forename: Ye
authors.initials: Y
authors.lastname: Song
authors.forename: Qisheng
authors.initials: Q
authors.lastname: Luo
authors.forename: Hao
authors.initials: H
authors.lastname: Long
authors.forename: Zheng
authors.initials: Z
authors.lastname: Hu
authors.forename: Tianshi
authors.initials: T
authors.lastname: Que
authors.forename: Xi'an
authors.initials: X
authors.lastname: Zhang
authors.forename: Zhiyong
authors.initials: Z
authors.lastname: Li
authors.forename: Gang
authors.initials: G
authors.lastname: Wang
authors.forename: Liu
authors.initials: L
authors.lastname: Yi
authors.affiliation: Department of Neurosurgery, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, PR China. narcissus_jane@163.com.
authors.forename: Zhen
authors.initials: Z
authors.lastname: Liu
authors.forename: WeiYi
authors.initials: W
authors.lastname: Fang
authors.forename: Songtao
authors.initials: S
authors.lastname: Qi
mesh_terms: D000818:Animals; D014408:Biomarkers, Tumor / Q000032:analysis*; D015153:Blotting, Western; D045744:Cell Line, Tumor; D002465:Cell Movement / Q000502:physiology; D049109:Cell Proliferation; D018450:Disease Progression; D055785:Gene Knockdown Techniques; D005910:Glioma / Q000201:enzymology* / Q000473:pathology*; D064593:Heterografts; D006801:Humans; D007150:Immunohistochemistry; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D008819:Mice, Nude; D009361:Neoplasm Invasiveness / Q000473:pathology; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D011379:Prognosis; D020133:Reverse Transcriptase Polymerase Chain Reaction; D014162:Transfection
chemical_list: D014408:Biomarkers, Tumor; D010751:Phosphopyruvate Hydratase