Activity of the renal Na+-K+-2Cl- cotransporter is reduced by mutagenesis of N-glycosylation sites: role for protein surface charge in Cl- transport.

@article{Paredes2006ActivityOT,
  title={Activity of the renal Na+-K+-2Cl- cotransporter is reduced by mutagenesis of N-glycosylation sites: role for protein surface charge in Cl- transport.},
  author={A. Paredes and C. Plata and Manuel Rivera and Erika Moreno and N. V{\'a}zquez and R. Mu{\~n}oz-Clares and S. Hebert and G. Gamba},
  journal={American journal of physiology. Renal physiology},
  year={2006},
  volume={290 5},
  pages={
          F1094-102
        }
}
The renal-specific Na(+)-K(+)-2Cl(-) cotransporter NKCC2 belongs to the SLC12 gene family; it is the target for loop diuretics and the cause of type I Bartter's syndrome. Because the NKCC2 sequence contains two putative N-linked glycosylation sites, one of which is conserved with the renal Na(+)-Cl(-) cotransporter in which glycosylation affects thiazide affinity, we assessed the role of glycosylation on NKCC2 functional properties. One (N442Q or N452Q) or both (N442,452Q) N-glycosylation sites… Expand
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