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10.1158/1541-7786.MCR-16-0103 http://scihub22266oqcxt.onion/10.1158/1541-7786.MCR-16-0103 C5136311!5136311 !27655130     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27655130 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Mol+Cancer+Res 2016 ; 14 (12 ): 1288-1299 Nephropedia Template TP {{tp|p=27655130 |t=2016. Oncofetal Chondroitin Sulfate Glycosaminoglycans Are Key Players in Integrin Signaling and Tumor Cell Motility |pdf=|usr=}}{{27655130 }} gab.com Text Oncofetal Chondroitin Sulfate Glycosaminoglycans Are Key Players in Integrin Signaling and Tumor Cell Motility JO: Mol Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=27655130 #FOAvip Many tumors express proteoglycans modified with oncofetal chondroitin sulfate glycosaminoglycan chains (ofCS), which are normally restricted to the placenta. However, the role of ofCS in cancer is largely unknown. The function of ofCS in cancer was analyzed using the recombinant ofCS-binding VAR2CSA protein (rVAR2) derived from the malaria parasite, Plasmodium falciparum We demonstrate that ofCS plays a key role in tumor cell motility by affecting canonical integrin signaling pathways. Binding of rVAR2 to tumor cells inhibited the interaction of cells with extracellular matrix (ECM) components, which correlated with decreased phosphorylation of Src kinase. Moreover, rVAR2 binding decreased migration, invasion, and anchorage-independent growth of tumor cells in vitro Mass spectrometry of ofCS-modified proteoglycan complexes affinity purified from tumor cell lines on rVAR2 columns revealed an overrepresentation of proteins involved in cell motility and integrin signaling, such as integrin-?1 (ITGB1) and integrin-?4 (ITGA4). Saturating concentrations of rVAR2 inhibited downstream integrin signaling, which was mimicked by knockdown of the core chondroitin sulfate synthesis enzymes ?-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1). The ofCS modification was highly expressed in both human and murine metastatic lesions in situ and preincubation or early intravenous treatment of tumor cells with rVAR2 inhibited seeding and spreading of tumor cells in mice. This was associated with a significant increase in survival of the animals. These data functionally link ofCS modifications with cancer cell motility and further highlights ofCS as a novel therapeutic cancer target. IMPLICATIONS: The cancer-specific expression of ofCS aids in metastatic phenotypes and is a candidate target for therapy. Mol Cancer Res; 14(12); 1288-99. ©2016 AACR. Twit Text FOAVip Oncofetal Chondroitin Sulfate Glycosaminoglycans Are Key Players in Integrin Signaling and Tumor Cell Motility ????Mol Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=27655130 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27655130 #FOAvip English Wikipedia <ref>{{Cite pmid|27655130 }}</ref> Oncofetal Chondroitin Sulfate Glycosaminoglycans Are Key Players in Integrin Signaling and Tumor Cell Motility #MMPMID27655130 Clausen TM ; Pereira MA ; Al Nakouzi N ; Oo HZ ; Agerbæk MØ ; Lee S ; Ørum-Madsen MS ; Kristensen AR ; El-Naggar A ; Grandgenett PM ; Grem JL ; Hollingsworth MA ; Holst PJ ; Theander T ; Sorensen PH ; Daugaard M ; Salanti A Mol Cancer Res 2016[Dec]; 14 (12 ): 1288-1299 PMID27655130 show ga Many tumors express proteoglycans modified with oncofetal chondroitin sulfate glycosaminoglycan chains (ofCS), which are normally restricted to the placenta. However, the role of ofCS in cancer is largely unknown. The function of ofCS in cancer was analyzed using the recombinant ofCS-binding VAR2CSA protein (rVAR2) derived from the malaria parasite, Plasmodium falciparum We demonstrate that ofCS plays a key role in tumor cell motility by affecting canonical integrin signaling pathways. Binding of rVAR2 to tumor cells inhibited the interaction of cells with extracellular matrix (ECM) components, which correlated with decreased phosphorylation of Src kinase. Moreover, rVAR2 binding decreased migration, invasion, and anchorage-independent growth of tumor cells in vitro Mass spectrometry of ofCS-modified proteoglycan complexes affinity purified from tumor cell lines on rVAR2 columns revealed an overrepresentation of proteins involved in cell motility and integrin signaling, such as integrin-?1 (ITGB1) and integrin-?4 (ITGA4). Saturating concentrations of rVAR2 inhibited downstream integrin signaling, which was mimicked by knockdown of the core chondroitin sulfate synthesis enzymes ?-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1). The ofCS modification was highly expressed in both human and murine metastatic lesions in situ and preincubation or early intravenous treatment of tumor cells with rVAR2 inhibited seeding and spreading of tumor cells in mice. This was associated with a significant increase in survival of the animals. These data functionally link ofCS modifications with cancer cell motility and further highlights ofCS as a novel therapeutic cancer target. IMPLICATIONS: The cancer-specific expression of ofCS aids in metastatic phenotypes and is a candidate target for therapy. Mol Cancer Res; 14(12); 1288-99. ©2016 AACR. |Animals [MESH] |Antigens, Protozoan/*genetics/metabolism [MESH] |Carcinoma, Lewis Lung/metabolism [MESH] |Cell Line, Tumor [MESH] |Chondroitin Sulfates/genetics/*metabolism [MESH] |Humans [MESH] |Integrins/*metabolism [MESH] |Melanoma, Experimental/metabolism [MESH] |Mice [MESH] |Neoplasm Metastasis [MESH] |Neoplasms/*metabolism/*pathology [MESH] |Pancreatic Neoplasms/metabolism/pathology [MESH]Oncofetal Chondroitin Sulfate Glycosaminoglycans Are Key Players in In(epmc).pdf DeepDyve Pubget Overpricing