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10.1074/jbc.M114.594721 http://scihub22266oqcxt.onion/10.1074/jbc.M114.594721 C4256351!4256351 !25331943     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25331943 &cmd=llinks): Failed to open stream: HTTP request failed! 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Nicotinamide phosphoribosyltransferase promotes epithelial-to-mesenchymal transition as a soluble factor independent of its enzymatic activity |pdf=|usr=}}{{25331943 }} gab.com Text Nicotinamide phosphoribosyltransferase promotes epithelial-to-mesenchymal transition as a soluble factor independent of its enzymatic activity JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25331943 #FOAvip Boosting NAD(+) biosynthesis with NAD(+) intermediates has been proposed as a strategy for preventing and treating age-associated diseases, including cancer. However, concerns in this area were raised by observations that nicotinamide phosphoribosyltransferase (NAMPT), a key enzyme in mammalian NAD(+) biosynthesis, is frequently up-regulated in human malignancies, including breast cancer, suggesting possible protumorigenic effects for this protein. We addressed this issue by studying NAMPT expression and function in human breast cancer in vivo and in vitro. Our data indicate that high NAMPT levels are associated with aggressive pathological and molecular features, such as estrogen receptor negativity as well as HER2-enriched and basal-like PAM50 phenotypes. Consistent with these findings, we found that NAMPT overexpression in mammary epithelial cells induced epithelial-to-mesenchymal transition, a morphological and functional switch that confers cancer cells an increased metastatic potential. However, importantly, NAMPT-induced epithelial-to-mesenchymal transition was found to be independent of NAMPT enzymatic activity and of the NAMPT product nicotinamide mononucleotide. Instead, it was mediated by secreted NAMPT through its ability to activate the TGF? signaling pathway via increased TGF?1 production. These findings have implications for the design of therapeutic strategies exploiting NAD(+) biosynthesis via NAMPT in aging and cancer and also suggest the potential of anticancer agents designed to specifically neutralize extracellular NAMPT. Notably, because high levels of circulating NAMPT are found in obese and diabetic patients, our data could also explain the increased predisposition to cancer of these subjects. Twit Text FOAVip Nicotinamide phosphoribosyltransferase promotes epithelial-to-mesenchymal transition as a soluble factor independent of its enzymatic activity ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25331943 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25331943 #FOAvip English Wikipedia <ref>{{Cite pmid|25331943 }}</ref> Nicotinamide phosphoribosyltransferase promotes epithelial-to-mesenchymal transition as a soluble factor independent of its enzymatic activity #MMPMID25331943 Soncini D ; Caffa I ; Zoppoli G ; Cea M ; Cagnetta A ; Passalacqua M ; Mastracci L ; Boero S ; Montecucco F ; Sociali G ; Lasiglič D ; Damonte P ; Grozio A ; Mannino E ; Poggi A ; D'Agostino VG ; Monacelli F ; Provenzani A ; Odetti P ; Ballestrero A ; Bruzzone S ; Nencioni A J Biol Chem 2014[Dec]; 289 (49 ): 34189-204 PMID25331943 show ga Boosting NAD(+) biosynthesis with NAD(+) intermediates has been proposed as a strategy for preventing and treating age-associated diseases, including cancer. However, concerns in this area were raised by observations that nicotinamide phosphoribosyltransferase (NAMPT), a key enzyme in mammalian NAD(+) biosynthesis, is frequently up-regulated in human malignancies, including breast cancer, suggesting possible protumorigenic effects for this protein. We addressed this issue by studying NAMPT expression and function in human breast cancer in vivo and in vitro. Our data indicate that high NAMPT levels are associated with aggressive pathological and molecular features, such as estrogen receptor negativity as well as HER2-enriched and basal-like PAM50 phenotypes. Consistent with these findings, we found that NAMPT overexpression in mammary epithelial cells induced epithelial-to-mesenchymal transition, a morphological and functional switch that confers cancer cells an increased metastatic potential. However, importantly, NAMPT-induced epithelial-to-mesenchymal transition was found to be independent of NAMPT enzymatic activity and of the NAMPT product nicotinamide mononucleotide. Instead, it was mediated by secreted NAMPT through its ability to activate the TGF? signaling pathway via increased TGF?1 production. These findings have implications for the design of therapeutic strategies exploiting NAD(+) biosynthesis via NAMPT in aging and cancer and also suggest the potential of anticancer agents designed to specifically neutralize extracellular NAMPT. Notably, because high levels of circulating NAMPT are found in obese and diabetic patients, our data could also explain the increased predisposition to cancer of these subjects. |*Gene Expression Regulation, Neoplastic [MESH] |Animals [MESH] |Breast Neoplasms/*genetics/metabolism/pathology [MESH] |Cell Line, Tumor [MESH] |Cell Proliferation [MESH] |Cytokines/antagonists & inhibitors/*genetics/metabolism [MESH] |Epithelial-Mesenchymal Transition/*genetics [MESH] |Female [MESH] |Humans [MESH] |NAD/metabolism [MESH] |Neoplasm Proteins/antagonists & inhibitors/*genetics/metabolism [MESH] |Neoplasm Staging [MESH] |Nicotinamide Phosphoribosyltransferase/antagonists & inhibitors/*genetics/metabolism [MESH] |RNA, Small Interfering/genetics/metabolism [MESH] |Receptor, ErbB-2/genetics/metabolism [MESH] |Receptors, Estrogen/deficiency/genetics [MESH] |Signal Transduction [MESH]Nicotinamide phosphoribosyltransferase promotes epithelial-to-mesenchy(epmc).pdf DeepDyve Pubget Overpricing