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10.1158/1541-7786.MCR-17-0352 http://scihub22266oqcxt.onion/10.1158/1541-7786.MCR-17-0352 C6059807!6059807 !28778876     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28778876 &cmd=llinks): Failed to open stream: HTTP request failed! 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Heparan Sulfate Glycosaminoglycans in Glioblastoma Promote Tumor Invasion |pdf=|usr=}}{{28778876 }} gab.com Text Heparan Sulfate Glycosaminoglycans in Glioblastoma Promote Tumor Invasion JO: Mol Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=28778876 #FOAvip Glioblastoma (GBM) is the most common primary malignant brain tumor of adults and confers a poor prognosis due, in part, to diffuse invasion of tumor cells. Heparan sulfate (HS) glycosaminoglycans, present on the cell surface and in the extracellular matrix, regulate cell signaling pathways and cell-microenvironment interactions. In GBM, the expression of HS glycosaminoglycans and the enzymes that regulate their function are altered, but the actual HS content and structure are unknown. However, inhibition of HS glycosaminoglycan function is emerging as a promising therapeutic strategy for some cancers. In this study, we use liquid chromatography-mass spectrometry analysis to demonstrate differences in HS disaccharide content and structure across four patient-derived tumorsphere lines (GBM1, 5, 6, 43) and between two murine tumorsphere lines derived from murine GBM with enrichment of mesenchymal and proneural gene expression (mMES and mPN, respectively) markers. In GBM, the heterogeneous HS content and structure across patient-derived tumorsphere lines suggested diverse functions in the GBM tumor microenvironment. In GBM5 and mPN, elevated expression of sulfatase 2 (SULF2), an extracellular enzyme that alters ligand binding to HS, was associated with low trisulfated HS disaccharides, a substrate of SULF2. In contrast, other primary tumorsphere lines had elevated expression of the HS-modifying enzyme heparanase (HPSE). Using gene editing strategies to inhibit HPSE, a role for HPSE in promoting tumor cell adhesion and invasion was identified. These studies characterize the heterogeneity in HS glycosaminoglycan content and structure across GBM and reveal their role in tumor cell invasion.Implications: HS-interacting factors promote GBM invasion and are potential therapeutic targets. Mol Cancer Res; 15(11); 1623-33. ©2017 AACR. Twit Text FOAVip Heparan Sulfate Glycosaminoglycans in Glioblastoma Promote Tumor Invasion ????Mol Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=28778876 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28778876 #FOAvip English Wikipedia <ref>{{Cite pmid|28778876 }}</ref> Heparan Sulfate Glycosaminoglycans in Glioblastoma Promote Tumor Invasion #MMPMID28778876 Tran VM ; Wade A ; McKinney A ; Chen K ; Lindberg OR ; Engler JR ; Persson AI ; Phillips JJ Mol Cancer Res 2017[Nov]; 15 (11 ): 1623-1633 PMID28778876 show ga Glioblastoma (GBM) is the most common primary malignant brain tumor of adults and confers a poor prognosis due, in part, to diffuse invasion of tumor cells. Heparan sulfate (HS) glycosaminoglycans, present on the cell surface and in the extracellular matrix, regulate cell signaling pathways and cell-microenvironment interactions. In GBM, the expression of HS glycosaminoglycans and the enzymes that regulate their function are altered, but the actual HS content and structure are unknown. However, inhibition of HS glycosaminoglycan function is emerging as a promising therapeutic strategy for some cancers. In this study, we use liquid chromatography-mass spectrometry analysis to demonstrate differences in HS disaccharide content and structure across four patient-derived tumorsphere lines (GBM1, 5, 6, 43) and between two murine tumorsphere lines derived from murine GBM with enrichment of mesenchymal and proneural gene expression (mMES and mPN, respectively) markers. In GBM, the heterogeneous HS content and structure across patient-derived tumorsphere lines suggested diverse functions in the GBM tumor microenvironment. In GBM5 and mPN, elevated expression of sulfatase 2 (SULF2), an extracellular enzyme that alters ligand binding to HS, was associated with low trisulfated HS disaccharides, a substrate of SULF2. In contrast, other primary tumorsphere lines had elevated expression of the HS-modifying enzyme heparanase (HPSE). Using gene editing strategies to inhibit HPSE, a role for HPSE in promoting tumor cell adhesion and invasion was identified. These studies characterize the heterogeneity in HS glycosaminoglycan content and structure across GBM and reveal their role in tumor cell invasion.Implications: HS-interacting factors promote GBM invasion and are potential therapeutic targets. Mol Cancer Res; 15(11); 1623-33. ©2017 AACR. |Animals [MESH] |Brain Neoplasms/chemistry/*metabolism [MESH] |Cell Line, Tumor [MESH] |Chromatography, Liquid [MESH] |Gene Editing [MESH] |Glioblastoma/chemistry/*metabolism [MESH] |Glucuronidase/genetics [MESH] |Heparitin Sulfate/*chemistry/*metabolism [MESH] |Humans [MESH] |Mass Spectrometry [MESH] |Mice [MESH] |Neoplasm Invasiveness [MESH] |Neoplasm Transplantation [MESH] |Signal Transduction [MESH] |Sulfatases [MESH] |Sulfotransferases/metabolism [MESH]Heparan Sulfate Glycosaminoglycans in Glioblastoma Promote Tumor Invas(epmc).pdf DeepDyve Pubget Overpricing