@article{VanSteenbergenBalteauGinionetal.2017,
  author    = {Van Steenbergen, Anne and Balteau, Magali and Ginion, Audrey and Fert{\´e}, Laura and Battault, Sylvain and de Meester de Ravenstein, Christophe and Balligand, Jean-Luc and Daskalopoulos, Evangelos-Panagiotis and Gilon, Patrick and Despa, Florin and Despa, Sanda and Vanoverschelde, Jean-Louis and Horman, Sandrine and Koepsell, Hermann and Berry, Gerard and Hue, Louis and Bertrand, Luc and Beauloye, Christophe},
  title     = {Sodium-myoinositol cotransporter-1, SMIT1, mediates the production of reactive oxygen species induced by hyperglycemia in the heart},
  series = {Scientific Reports},
  volume    = {7},
  journal   = {Scientific Reports},
  doi       = {10.1038/srep41166},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-180891},
  pages     = {14},
  year      = {2017},
  abstract  = {Hyperglycemia (HG) stimulates the production of reactive oxygen species in the heart through activation of NADPH oxidase 2 (NOX2). This production is independent of glucose metabolism but requires sodium/glucose cotransporters (SGLT). Seven SGLT isoforms (SGLT1 to 6 and sodium-myoinositol cotransporter-1, SMIT1) are known, although their expression and function in the heart remain elusive. We investigated these 7 isoforms and found that only SGLT1 and SMIT1 were expressed in mouse, rat and human hearts. In cardiomyocytes, galactose (transported through SGLT1) did not activate NOX2. Accordingly, SGLT1 deficiency did not prevent HG-induced NOX2 activation, ruling it out in the cellular response to HG. In contrast, myo-inositol (transported through SMIT1) reproduced the toxic effects of HG. SMIT1 overexpression exacerbated glucotoxicity and sensitized cardiomyocytes to HG, whereas its deletion prevented HG-induced NOX2 activation. In conclusion, our results show that heart SMIT1 senses HG and triggers NOX2 activation. This could participate in the redox signaling in hyperglycemic heart and contribute to the pathophysiology of diabetic cardiomyopathy.},
  language  = {en}
}
@article{SalkerSinghZengetal.2017,
  author    = {Salker, Madhuri S. and Singh, Yogesh and Zeng, Ni and Chen, Hong and Zhang, Shaqiu and Umbach, Anja T. and Fakhri, Hajar and Kohlhofer, Ursula and Quintanilla-Martinez, Leticia and Durairaj, Ruban R. Peter and Barros, Flavio S. V. and Vrljicak, Pavle and Ott, Sascha and Brucker, Sara Y. and Wallwiener, Diethelm and Madunić, Ivana Vrhovac and Breljak, Davorka and Sabolić, Ivan and Koepsell, Hermann and Brosens, Jan J. and Lang, Florian},
  title     = {Loss of endometrial sodium glucose cotransporter SGLT1 is detrimental to embryo survival and fetal growth in pregnancy},
  series = {Scientific Reports},
  volume    = {7},
  journal   = {Scientific Reports},
  doi       = {10.1038/s41598-017-11674-3},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-173814},
  year      = {2017},
  abstract  = {Embryo implantation requires a hospitable uterine environment. A key metabolic change that occurs during the peri-implantation period, and throughout early pregnancy, is the rise in endometrial glycogen content. Glycogen accumulation requires prior cellular uptake of glucose. Here we show that both human and murine endometrial epithelial cells express the high affinity Na\(^+\)-coupled glucose carrier SGLT1. Ussing chamber experiments revealed electrogenic glucose transport across the endometrium in wild type (\(Slc5a1^{+/+}\)) but not in SGLT1 defcient (\(Slc5a1^{-/-}\)) mice. Endometrial glycogen content, litter size and weight of offspring at birth were signifcantly lower in \(Slc5a1^{-/-}\) mice. In humans, \(SLC5A1\) expression was upregulated upon decidualization of primary endometrial stromal cells. Endometrial \(SLC5A1\) expression during the implantation window was attenuated in patients with recurrent pregnancy loss when compared with control subjects. Our fndings reveal a novel mechanism establishing adequate endometrial glycogen stores for pregnancy. Disruption of this histiotrophic pathway leads to adverse pregnancy outcome.},
  language  = {en}
}