Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0017638 (glioma)
 30,880 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The composition of glycosphingolipid on human cultured glioma cell line U 251 and rat glioma cell line C6 was analysed by high performance thin layer chromatography. As a result, the major gangliosides were simple gangliosides such as GM3 (U 251: 7.7%, C6: 84.3%), GM2 (U 251: 32.6%) and SPG (U 251: 30.0%) on glioma cells whereas the major neutral glycosphingolipids were CDH, CTH and globoside. After treatment with neuraminidase 2.92 nmol/mg dry weight and 3.73 nmol/mg dry weight of sialic acid were freed from U 251 cells and C6 cell, but only 8.11% (U 251 cell) and 11.24% (C 6 cell) of these sialic acids originated from glycolipid, and thus the major part of sialic acid might be released from glycoprotein of the cells. The gangliosides that react to neuraminidase are SPG, GD1a and GD1b in U 251 cells and are GM1a and little GM3 in C 6 cells. The biolabelling study using N-acetyl-14C-mannosamine as a precursor of sialic acid demonstrated that the precursor was mainly incorporated into both or either of GM3 and SPG in the acidic glycolipid fraction. In addition, no significant change on proliferation and morphology of glioma cells after neuraminidase treatment was observed in this study.
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PMID:[The composition of glycosphingolipids and the effect of neuraminidase on cultured glioma cell lines]. 276 99

Y-box binding protein 1 (YB-1) is manifested as its involvement in cell proliferation and differentiation and malignant cell transformation. Overexpression of YB-1 is associated with glioma progression and patient survival. The aim of this study is to investigate the influence of YB-1 knockdown on glioma cell progression and reveal the mechanisms of YB-1 knockdown on glioma cell growth, migration, and apoptosis. It was found that the knockdown of YB-1 decreased the mRNA and protein levels of YB-1 in U251 glioma cells. The knockdown of YB-1 significantly inhibited cell proliferation, colony formation, and migration in vitro and tumor growth in vivo. Proteome and phosphoproteome data revealed that YB-1 is involved in glioma progression through regulating the expression and phosphorylation of major proteins involved in cell cycle, adhesion, and apoptosis. The main regulated proteins included CCNB1, CCNDBP1, CDK2, CDK3, ADGRG1, CDH-2, MMP14, AIFM1, HO-1, and BAX. Furthermore, it was also found that YB-1 knockdown is associated with the hypo-phosphorylation of ErbB, mTOR, HIF-1, cGMP-PKG, and insulin signaling pathways, and proteoglycans in cancer. Our findings indicated that YB-1 plays a key role in glioma progression in multiple ways, including regulating the expression and phosphorylation of major proteins associated with cell cycle, adhesion, and apoptosis.
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PMID:Effect and mechanism of YB-1 knockdown on glioma cell growth, migration, and apoptosis. 3204 13