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cotransport and associated gene
products in mouse DCT
1 Department of Anatomy and 3 Franz Volhard Clinic, Medical Faculty of the Charité, Humboldt University, 13353 Berlin, Germany; and 2 Department of Internal Medicine, Oregon Health Sciences University, Portland, Oregon 97201
First published August 8, 2001; 10.1152/ajprenal.00148.2001.
The
mammalian distal nephron develops a complex assembly of specialized cell types to accomplish the fine adjustment of urinary electrolyte composition. The epithelia of the distal convoluted tubule
(DCT), the connecting tubule (CNT), and the cortical collecting duct
(CCD) show an axial structural heterogeneity that has been functionally
elucidated by the localization of proteins involved in transepithelial
ion transport. We compared the distribution of the thiazide-sensitive
Na+-Cl
cotransporter (TSC), basolateral
Na+/Ca2+ exchanger (Na/Ca), cytosolic
calcium-binding proteins calbindin D28K and parvalbumin,
and the key enzyme for selective aldosterone actions,
11
-hydroxysteroid-dehydrogenase 2 (11HSD2), in the distal convolutions of the mouse. In the mouse, as opposed to the rat, we
found no clear subsegmentation of the DCT into a proximal (DCT1) and a
distal (DCT2) portion. The TSC was expressed along the entire DCT. Na/Ca and calbindin D28K were similarly expressed
along most of the DCT, with minor exceptions in the initial portion of
the DCT. Both were also present in the CNT. Parvalbumin was found in
the entire DCT, with an occasional absence from short end portions of
the DCT, and was not present in CNT. 11HSD2 was predominantly located
in the CNT and CCD. Short end portions of DCT only occasionally showed
the 11HSD2 signal. We also observed an overlap of 11HSD2 immunoreactivity and mRNA staining. Our observations will have implications in understanding the physiological effects of gene disruption and targeting experiments in the mouse.
distal convoluted tubule; connecting tubule; sodium-calcium
exchanger; calbindin; parvalbumin; 11
-hydroxysteroid-dehydrogenase
type 2
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