 Hello, my name is Anping Chen. I'm a post-doc working in Dr. Michael Romer's lab at American Clinic, the Department of Physiology and Biomedical Engineering. Today it is my honor to have the chance to talk about our current result of the functional analysis for the coding SNPs in human SLC 2689 gene, which published in Human Mutation recently. SNC 2689 is not a chloride channel, but also a chloride bicarbonate exchanger. The non-codomized of SNC 2689 show decreased gastric acid secretion. SNC 2689 is also suggested to be a novel candidate gene associated with inner ear development, as well as in antipsychotic responses. Interestingly, SNC 2689 is localized to absciliar of the stomach and the lung. These are also tissues and members which the CFTR is located. CFTR is a chloride channel which mutants cause cystic fibrosis. Moreover, a recent G1 analysis of cystic fibrosis patients indicated that some SNPs of human SNC 2689 is associated with cystic fibrosis phenotypes. So the question is, how about the SNPs of the SNC 2689 show their respectively effect for the function of the SNC 2689? To answer this question, we performed the functional analysis for those SNPs. Now, let's talk about our funding in our experiments. This is the title for our paper in Human Mutation. This is a predicted topological model of SNC 2689 protein. It has 12 transmembrary regions, with one set of plastic C terminals with stastaman. When we started our project on 2010, there are eight SNPs in the database of NCBI. There are 170N located in N terminals, T 127N located in TM3 region, I 384T located in intracellular loop, R 575W P606R V622R is located in the stastaman variable loop, the V744M H748R SNPs located labeling to the stastaman. Hi, I'm Dr. Michael Efremero and the Mayo Clinic in Physiology and Biomedical Engineering. I'd like to give you a bit of insight into some really interesting work that Anping Chen in my lab has been working on for the past couple of years that's just been published in Human Mutations. What Anping has found is if we look at the naturally, when he looks at the naturally occurring human mutations of SNC 2689, which in my lab, being a physiology lab, we know is both a channel and a chloride bicarbonate exchanger, the wild type transporter shown in green has a certain amount of function, this is just current on the y-axis, but one mutation has a lot more function than the wild type Y70N and there are three others shown in red here that have decreased function. Yet the protein amount seems to be relatively same and all of these proteins make it out to the plasma membrane. Why do we even care about this? Well, if we think about where this protein is located in the gut and in the pancreas, it's in the apical membrane and it has these different roles. It can interact with the chloride channel that's mutated in cystic fibrosis or CFTR and rather than activating function, it inhibits function. So what's even more interesting is there's a recent study, a GWAS study, that just came out from Sun and All in Nature Genetics that shows that this SLC26A9 gene is genetically associated with the gut phenotypes in cystic fibrosis. And so the really important factor of Dr. Anping Chen's findings is that not only is CFTR changing the function of the bicarbonate and chloride transport in the epithelia, but if you layer on top of that this chloride channel and transporter, SLC26A9 in the naturally occurring SNPs, you can either increase or decrease function. And so this in part accounts for the variability that we think are seen in the cystic fibrosis phenotypes. Thank you very much.