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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Changes in the expression of proteins associated with aerobic glycolysis and cell migration are involved in tumorigenic ability of two glioma cell lines

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Author(s):
Ramao, Anelisa [1, 2, 3] ; Gimenez, Marcela [1, 2, 3] ; Laure, Helen Julie [1, 2, 3] ; Izumi, Clarice [1, 2, 3] ; dos Santos Vida, Rodrigo Cesar [1, 2, 3] ; Oba-Shinjo, Sueli [4] ; Nagahashi Marie, Suely Kazue [4] ; Rosa, Jose Cesar [1, 2, 3]
Total Authors: 8
Affiliation:
[1] Univ Sao Paulo, Prot Chem Ctr, Sch Med Ribeirao Preto, BR-14049 Ribeirao Preto, SP - Brazil
[2] Univ Sao Paulo, Dept Mol & Cell Biol & Pathogen Bioagents, Sch Med Ribeirao Preto, BR-14049 Ribeirao Preto, SP - Brazil
[3] Fundacao Hemoctr Ribeirao Preto, Ctr Cellular Therapy & Hemotherapy Ribeirao Preto, Ribeirao Preto, SP - Brazil
[4] Univ Sao Paulo, Dept Neurol, Sch Med Sao Paulo, Sao Paulo - Brazil
Total Affiliations: 4
Document type: Journal article
Source: PROTEOME SCIENCE; v. 10, SEP 3 2012.
Web of Science Citations: 18
Abstract

Background: The most frequent and malignant brain cancer is glioblastoma multiforme (GBM). In gliomas, tumor progression and poor prognosis are associated with the tumorigenic ability of the cells. U87MG cells (wild-type p53) are known to be tumorigenic in nude mice, but T98G cells (mutant p53) are not tumorigenic. We investigated the proteomic profiling of these two cell lines in order to gain new insights into the mechanisms that may be involved in tumorigenesis. Results: We found 24 differentially expressed proteins between T98G and U87MG cells. Gene Ontology supports the notion that over-representation of differentially expressed proteins is involved in glycolysis, cell migration and stress oxidative response. Among those associated with the glycolysis pathway, TPIS and LDHB are up-regulated in U87MG cells. Measurement of glucose consumption and lactate production suggests that glycolysis is more effective in U87MG cells. On the other hand, G6PD expression was 3-fold higher in T98G cells and this may indicate a shift to the pentose-phosphate pathway. Moreover, GRP78 expression was also three-fold higher in T98G than in U87MG cells. Under thapsigargin treatment both cell lines showed increased GRP78 expression and the effect of this agent was inversely correlated to cell migration. Quantitative RT-PCR and immunohistochemistry of GRP78 in patient samples indicated a higher level of expression of GRP78 in grade IV tumors compared to grade I and non-neoplastic tissues, respectively. Conclusions: Taken together, these results suggest an important role of proteins involved in key functions such as glycolysis and cell migration that may explain the difference in tumorigenic ability between these two glioma cell lines and that may be extrapolated to the differential aggressiveness of glioma tumors. (AU)

FAPESP's process: 98/14247-6 - Center for Research on Cell-Based Therapy
Grantee:Marco Antonio Zago
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 04/12133-6 - Search for molecular markers related to the diagnosis and prognosis of tumors of the central nervous system
Grantee:Suely Kazue Nagahashi Marie
Support type: Research Projects - Thematic Grants