Friedrich - Alexander - University, Erlangen - Nuremberg
Erlangen, Germany

Friedrich-Alexander-University Erlangen-Nürnberg better known as FAU is a public research university in the cities of Erlangen and Nuremberg in Bavaria, Germany. The name Friedrich-Alexander comes from the university's first founder Friedrich, Margrave of Brandenburg-Bayreuth, and its benefactor Christian Frederick Charles Alexander, Margrave of Brandenburg-Ansbach.In Germany, traditional liberal arts universities do not usually have an engineering school or department. However, FAU does have a distinct engineering faculty.FAU is the second largest state university in the state Bavaria. It has 5 faculties, 23 departments15 around 39,085 students enrolled in the university in 239 fields of study, with about 23 at the Nuremberg campus. These statistics putted FAU in the list of top 10 largest universities in Germany.In year 2013, there were 5251 students graduated from the university as well as 663 doctorates and 50 post-doctoral theses registered. Moreover, it received 171 million Euro external funding in the same year, therefore making its one of the strongest third-party funded universities in Germany.In 2006 and 2007, as part of the national excellence initiative, FAU was chosen by the German Research Foundation as one of the winners in the German Universities Excellence Initiative. FAU is also a member of DFG and the Top Industrial Managers for Europe network.In Academic Ranking of World Universities for year 2014, FAU ranked second among German universities in Engineering/Technology and Computer science group for all four ranking parameters TOP, FUN, HiCi and PUB. Wikipedia.

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PubMed | Friedrich - Alexander - University, Erlangen - Nuremberg
Type: Journal Article | Journal: The Journal of biological chemistry | Year: 2016

The epithelial sodium channel (ENaC) is a member of the ENaC/degenerin ion channel family, which also includes the bile acid-sensitive ion channel (BASIC). So far little is known about the effects of bile acids on ENaC function. ENaC is probably a heterotrimer consisting of three well characterized subunits (). In humans, but not in mice and rats, an additional -subunit exists. The aim of this study was to investigate the effects of chenodeoxycholic, cholic, and deoxycholic acid in unconjugated (CDCA, CA, and DCA) and tauro-conjugated (t-CDCA, t-CA, t-DCA) form on human ENaC in its - and -configuration. We demonstrated that tauro-conjugated bile acids significantly stimulate ENaC in the - and in the -configuration. In contrast, non-conjugated bile acids have a robust stimulatory effect only on ENaC. Bile acids stimulate ENaC-mediated currents by increasing the open probability of active channels without recruiting additional near-silent channels known to be activated by proteases. Stimulation of ENaC activity by bile acids is accompanied by a significant reduction of the single-channel current amplitude, indicating an interaction of bile acids with a region close to the channel pore. Analysis of the known ASIC1 (acid-sensing ion channel) crystal structure suggested that bile acids may bind to the pore region at the degenerin site of ENaC. Substitution of a single amino acid residue within the degenerin region of ENaC (N521C or N521A) significantly reduced the stimulatory effect of bile acids on ENaC, suggesting that this site is critical for the functional interaction of bile acids with the channel.

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