@article{BernacchioniGhiniCencettietal.2017,
  author    = {Bernacchioni, Caterina and Ghini, Veronica and Cencetti, Francesca and Japtok, Lukasz and Donati, Chiara and Bruni, Paola and Turano, Paola},
  title     = {NMR metabolomics highlights sphingosine kinase-1 as a new molecular switch in the orchestration of aberrant metabolic phenotype in cancer cells},
  series = {Molecular oncology / Federation of European Biochemical Societies},
  volume    = {11},
  journal   = {Molecular oncology / Federation of European Biochemical Societies},
  publisher = {Wiley},
  address   = {Hoboken},
  issn      = {1878-0261},
  doi       = {10.1002/1878-0261.12048},
  pages     = {517 -- 533},
  year      = {2017},
  abstract  = {Strong experimental evidence in animal and cellular models supports a pivotal role of sphingosine kinase-1 (SK1) in oncogenesis. In many human cancers, SK1 levels are upregulated and these increases are linked to poor prognosis in patients. Here, by employing untargeted NMR- based metabolomic profiling combined with functional validations, we report the crucial role of SK1 in the metabolic shift known as the Warburg effect in A2780 ovarian cancer cells. Indeed, expression of SK1 induced a high glycolytic rate, characterized by increased levels of lactate along with increased expression of the proton/monocarboxylate symporter MCT1, and decreased oxidative metabolism, associated with the accumulation of intermediates of the tricarboxylic acid cycle and reduction in CO2 production. Additionally, SK1-expressing cells displayed a significant increase in glucose uptake paralleled by GLUT3 transporter upregulation. The role of SK1 is not limited to the induction of aerobic glycolysis, affecting metabolic pathways that appear to support the biosynthesis of macromolecules. These findings highlight the role of SK1 signaling axis in cancer metabolic reprogramming, pointing out innovative strategies for cancer therapies.},
  language  = {en}
}
@article{WegerichTuranoAllegrozzietal.2009,
  author    = {Wegerich, Franziska and Turano, Paola and Allegrozzi, Marco and Moehwald, Helmuth and Lisdat, Fred},
  title     = {Cytochrome c mutants for superoxide biosensors},
  issn      = {0003-2700},
  doi       = {10.1021/Ac802571h},
  year      = {2009},
  abstract  = {The effect of introducing positive charges (lysines) in human cytochrome c (cyt c) on the redox properties and reaction rates of cyt c with superoxide radicals was studied. The mutated forms of this electron-transfer protein are used as sensorial recognition elements for the amperometric detection of the reactive oxygen radical. The proteins were prepared by site-directed mutagenesis focusing on amino acids near the heme edge. The 11 mutants of human cyt c expressed in the course of this research have been characterized by UV-vis spectroscopy, circular dichroism, and NMR spectroscopy to verify overall structure integrity as well as axial coordination of the heme iron. The mutants are investigated voltammetrically using promoter-modified gold electrodes with respect to redox activity and formal redox potential. The rate constants for the reaction with superoxide have been determined spectrophotometrically. Four mutants show a higher reaction rate with the radical as compared to the wild type. These mutants are used for the construction of superoxide sensors based on thiol-modified gold electrodes and covalently fixed proteins. We found that the E66K mutant-based electrode has a clearly higher sensitivity in comparison with the wild-type-based sensor while retaining the high selectivity and showing a good storage stability.},
  language  = {en}
}