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Articles in PresS, published online ahead of print April 16, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00112.2002
Submitted on March 21, 2002
Accepted on April 10, 2002
1 Department of Biological Chemistry, Weizmann Institute, Rehovot, Israel
2 Department of Medicine, McGill University, Montreal, Canada
3 Department of Medecine, INSERM U478, Paris, France
* To whom correspondence should be addressed. E-mail: steven.karlish{at}weizmann.ac.il.
Like the 
subunit of Na,K-ATPase, CHIF (corticosteroid hormone induced factor) is a member of the FXYD family of one trans-membrane segment proteins. Both CHIF and two splice variants of , a and b, are expressed in kidney. Immunolocalization experiments demonstrate mutually exclusive expression of CHIF and in different nephron segments. Specific co-immunoprecipitation experiments demonstrate the existence in kidney membranes of the complexes 
/ß/a, /ß/b and /ß/CHIF and exclude mixed complexes such as /ß/a/b and /ß//CHIF. CHIF has been expressed in HeLa cells harboring the rat 1 subunit of Na,K-ATPase. 86Rb flux experiments demonstrate that CHIF induces a 2-3-fold increase in apparent affinity for cytoplasmic Na but does not affect affinity for extracellular K (Rb) ions or Vmax. Measurements of Na,K-ATPase using isolated membranes show similar but smaller effects of CHIF on K Na, while K K and K ATP are unaffected. The functional effects of CHIF differ from those of described previously. An implication of these findings is that other FXYD proteins could act as tissue-specific modulators of Na,K-ATPase.
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