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Am J Physiol Cell Physiol 277: C899-C912, 1999;
0363-6143/99 $5.00
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Vol. 277, Issue 5, C899-C912, November 1999

Mouse K-Cl cotransporter KCC1: cloning, mapping, pathological expression, and functional regulation

Wanfang Su1, Boris E. Shmukler1, Marina N. Chernova1, Alan K. Stuart-Tilley1, Lucia de Franceschi6, Carlo Brugnara2,5, and Seth L. Alper1,3,4

1 Molecular Medicine and Renal Units, Beth Israel Deaconess Medical Center, Boston 02215; 2 Department of Laboratory Medicine, The Children's Hospital, Boston 02115; Departments of 3 Medicine, 4 Cell Biology, and 5 Pathology, Harvard Medical School, Boston, Massachusetts 02215; and 6 Department of Clinical and Experimental Medicine, University of Verona, Verona, Italy

Although K-Cl cotransporter (KCC1) mRNA is expressed in many tissues, K-Cl cotransport activity has been measured in few cell types, and detection of endogenous KCC1 polypeptide has not yet been reported. We have cloned the mouse erythroid KCC1 (mKCC1) cDNA and its flanking genomic regions and mapped the mKCC1 gene to chromosome 8. Three anti-peptide antibodies raised against recombinant mKCC1 function as immunoblot and immunoprecipitation reagents. The tissue distributions of mKCC1 mRNA and protein are widespread, and mKCC1 RNA is constitutively expressed during erythroid differentiation of ES cells. KCC1 polypeptide or related antigen is present in erythrocytes of multiple species in which K-Cl cotransport activity has been documented. Erythroid KCC1 polypeptide abundance is elevated in proportion to reticulocyte counts in density-fractionated cells, in bleeding-induced reticulocytosis, in mouse models of sickle cell disease and thalassemia, and in the corresponding human disorders. mKCC1-mediated uptake of 86Rb into Xenopus oocytes requires extracellular Cl-, is blocked by the diuretic R(+)-[2-n-butyl-6,7-dichloro-2-cyclopentyl-2,3-dihydro-1-oxo-1H-indenyl-5-yl-)oxy]acetic acid, and exhibits an erythroid pattern of acute regulation, with activation by hypotonic swelling, N-ethylmaleimide, and staurosporine and inhibition by calyculin and okadaic acid. These reagents and findings will expedite studies of KCC1 structure-function relationships and of the pathobiology of KCC1-mediated K-Cl cotransport.

red blood cells; sickle cell disease; thalassemia; SC disease; SAD1


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