@article{ChakrabortyChenBornhorstetal.2015,
  author    = {Chakraborty, Sudipta and Chen, Pan and Bornhorst, Julia and Schwerdtle, Tanja and Schumacher, Fabian and Kleuser, Burkhard and Bowman, Aaron B. and Aschner, Michael A.},
  title     = {Loss of pdr-1/parkin influences Mn homeostasis through altered ferroportin expression in C-elegans},
  series = {Metallomics : integrated biometal science},
  volume    = {7},
  journal   = {Metallomics : integrated biometal science},
  number    = {5},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1756-5901},
  doi       = {10.1039/c5mt00052a},
  pages     = {847 -- 856},
  year      = {2015},
  language  = {en}
}
@article{CarpinteiroBeckerJaptoketal.2015,
  author    = {Carpinteiro, Alexander and Becker, Katrin Anne and Japtok, Lukasz and Hessler, Gabriele and Keitsch, Simone and Pozgajova, Miroslava and Schmid, Kurt W. and Adams, Constantin and M{\"u}ller, Stefan and Kleuser, Burkhard and Edwards, Michael J. and Grassme, Heike and Helfrich, Iris and Gulbins, Erich},
  title     = {Regulation of hematogenous tumor metastasis by acid sphingomyelinase},
  series = {EMBO molecular medicine},
  volume    = {7},
  journal   = {EMBO molecular medicine},
  number    = {6},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {1757-4676},
  pages     = {714 -- 734},
  year      = {2015},
  abstract  = {Metastatic dissemination of cancer cells is the ultimate hallmark of malignancy and accounts for approximately 90\% of human cancer deaths. We investigated the role of acid sphingomyelinase (Asm) in the hematogenous metastasis of melanoma cells. Intravenous injection of B16F10 melanoma cells into wild-type mice resulted in multiple lung metastases, while Asm-deficient mice (Smpd1(-/-) mice) were protected from pulmonary tumor spread. Transplanting wild-type platelets into Asm-deficient mice reinstated tumor metastasis. Likewise, Asm-deficient mice were protected from hematogenous MT/ret melanoma metastasis to the spleen in a mouse model of spontaneous tumor metastasis. Human and mouse melanoma cells triggered activation and release of platelet secretory Asm, in turn leading to ceramide formation, clustering, and activation of 51 integrins on melanoma cells finally leading to adhesion of the tumor cells. Clustering of integrins by applying purified Asm or C-16 ceramide to B16F10 melanoma cells before intravenous injection restored trapping of tumor cells in the lung in Asm-deficient mice. This effect was revertable by arginine-glycine-aspartic acid peptides, which are known inhibitors of integrins, and by antibodies neutralizing 1 integrins. These findings indicate that melanoma cells employ platelet-derived Asm for adhesion and metastasis.},
  language  = {en}
}
@article{BrunoCencettiPerticietal.2015,
  author    = {Bruno, Gennaro and Cencetti, Francesca and Pertici, Irene and Japtok, Lukasz and Bernacchioni, Caterina and Donati, Chiara and Bruni, Paola},
  title     = {CTGF/CCN2 exerts profibrotic action in myoblasts via the up-regulation of sphingosine kinase-1/S1P(3) signaling axis: Implications in the action mechanism of TGF beta},
  series = {Biochimica et biophysica acta : Molecular and cell biology of lipids},
  volume    = {1851},
  journal   = {Biochimica et biophysica acta : Molecular and cell biology of lipids},
  number    = {2},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1388-1981},
  doi       = {10.1016/j.bbalip.2014.11.011},
  pages     = {194 -- 202},
  year      = {2015},
  abstract  = {The matricellular protein connective tissue growth factor (CTGF/CCN2) is recognized as key player in the onset of fibrosis in various tissues, including skeletal muscle. In many circumstances, CTGF has been shown to be induced by transforming growth factor beta (TGF beta) and accounting, at least in part, for its biological action. In this study it was verified that in cultured myoblasts CTGF/CCN2 causes their transdifferentiation into myofibroblasts by up-regulating the expression of fibrosis marker proteins alpha-smooth muscle actin and transgelin. Interestingly, it was also found that the profibrotic effect exerted by CTGF/CCN2 was mediated by the sphingosine kinase (SK)-1/S1P(3) signaling axis specifically induced by the treatment with the profibrotic cue. Following CTGF/CCN2-induced up-regulation, S1P(3) became the SIP receptor subtype expressed at the highest degree, at least at mRNA level, and was thus capable of readdressing the sphingosine 1-phosphate signaling towards fibrosis rather than myogenic differentiation. Another interesting finding is that CTGF/CCN2 silencing prevented the TGF beta-dependent up-regulation of SKI/S1P(3) signaling axis and strongly reduced the profibrotic effect exerted by TGF beta, pointing at a crucial role of endogenous CTGF/CCN2 generated following TGF beta challenge in the transmission of at least part of its profibrotic effect These results provide new insights into the molecular mechanism by which CTGF/CCN2 drives its biological action and strengthen the concept that SK1/S1P(3) axis plays a critical role in the onset of fibrotic cell phenotype. (C) 2014 Elsevier B.V. All rights reserved.},
  language  = {en}
}
@phdthesis{Bendadani2015,
  author    = {Bendadani, Carolin},
  title     = {1-Methylpyren: Biotransformation und Gentoxizit{\"a}t},
  school      = {Universit{\"a}t Potsdam},
  pages     = {188},
  year      = {2015},
  language  = {en}
}
@phdthesis{Baumeier2015,
  author    = {Baumeier, Christian},
  title     = {Dietary and Pharmacological Strategies for the Prevention and Treatment of Type 2 Diabetes in a Diabetes-Susceptible Mouse Model},
  school      = {Universit{\"a}t Potsdam},
  pages     = {148},
  year      = {2015},
  language  = {en}
}
@article{BaierPurschkeSchmittetal.2015,
  author    = {Baier, Daniel and Purschke, Benedict and Schmitt, Christophe and Rawel, Harshadrai Manilal and Knorr, Dietrich},
  title     = {Effect of high pressure - low temperature treatments on structural characteristics of whey proteins and micellar caseins},
  series = {Food chemistry},
  volume    = {187},
  journal   = {Food chemistry},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0308-8146},
  doi       = {10.1016/j.foodchem.2015.04.049},
  pages     = {354 -- 363},
  year      = {2015},
  abstract  = {In this study, structural changes in micellar caseins and whey proteins due to high pressure - low temperature treatments (HPLT) were investigated and compared to changes caused by high pressure treatments at room temperature. Whey protein isolate (WPI) solutions as well as micellar casein (MC) dispersions and mixtures were treated at 500 MPa (pH 7.0 and 5.8) at room temperature, -15 degrees C and -35 degrees C. Surface hydrophobicity and accessible thiol groups remained nearly unchanged after HPLT treatments whereas HP treatments at room temperature caused an unfolding of the WPI, resulting in an increase in surface hydrophobicity and exposure of the thiol groups. For HPLT treatments, distinct changes in the secondary structure (increase in the amount of beta-sheets) were observed while the tertiary structure remained unchanged. Large flocs, stabilized by hydrophobic interactions and hydrogen bonds, were formed in casein containing samples due to HPLT treatments. Depending on the pH and the applied HPLT treatment parameters, these interactions differed significantly from the interactions determined in native micelles. (C) 2015 Elsevier Ltd. All rights reserved.},
  language  = {en}
}