Publications

Mouse K-Cl cotransporte KCC1: cloning, mapping, pathological expression and functional regulation.  (1999)

Authors:
Su, W.; Shmukler, B. E.; Chernova, M. N.; Stuart-Tilley, A. K.; De Franceschi, L.; Brugnara, C.; Alper, S. L.
Title:
Mouse K-Cl cotransporte KCC1: cloning, mapping, pathological expression and functional regulation.
Year:
1999
Type of item:
Articolo in Rivista
Tipologia ANVUR:
Articolo su rivista
Language:
Inglese
Format:
A Stampa
Referee:
Name of journal:
American Journal of Physiology
ISSN of journal:
0002-9513
N° Volume:
277
Number or Folder:
5
:
American Journal of Physiology
Page numbers:
C899-C912
Keyword:
Red blood cells; SAD1; SC disease; Sickle cell disease; Thalassemia
Short description of contents:
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 (86)Rb 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.
Web page:
https://doi.org/10.1152/ajpcell.1999.277.5.c899
Product ID:
424
Handle IRIS:
11562/424
Deposited On:
November 28, 2007
Last Modified:
November 12, 2021
Bibliographic citation:
Su, W.; Shmukler, B. E.; Chernova, M. N.; Stuart-Tilley, A. K.; De Franceschi, L.; Brugnara, C.; Alper, S. L., Mouse K-Cl cotransporte KCC1: cloning, mapping, pathological expression and functional regulation. «American Journal of Physiology» , vol. 277 , n. 51999pp. C899-C912

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