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Articles in PresS, published online ahead of print October 2, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00262.2002
Submitted on June 4, 2002
Accepted on September 20, 2002
1 Medicine, Laval University, Quebec, Quebec, Canada
2 Cellular and Molecular Physiology, Yale University, New Haven, CT, USA
* To whom correspondence should be addressed. E-mail: paul.isenring{at}crhdq.ulaval.ca.
In the shark (sa), two variants of the renal Na-K-Cl cotransporter (NKCC2A and F) are produced by alternative splicing of the second transmembrane domain (tm2) region. In mammals, these splice-variants, as well as a third variant (NKCC2B) are spatially distributed along the TAL and exhibit divergent kinetic behaviors. To test whether different tm2 regions in saNKCC2 are also associated with different kinetic phenotypes, we examined the ion-dependence of 86Rb influx for shark and rabbit splice-variants expressed in Xenopus laevis oocytes. We found that in both species, "A" forms have higher cation affinities than "F" forms. In regard to Cl affinity, however, the "A-F" difference was more pronounced in rabbit, and the relationship between transport activity and [Cl] was not always sigmoidal. These results show that the tm2 of shark NKCC2 is, as in rabbit, important for Cl transport and they suggest that the ability of the distal NKCC2-expressing segment to extract Cl from the luminal fluid differs among species. In this report, we have also found that the renal NKCC2 of distant vertebrates share similar affinities for cations. This finding points to the existence of highly conserved residues that mediate the kinetic behavior of the NKCC2 splice-variants.
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