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J. Biol. Chem., Vol. 269, Issue 45, 27973-27978, Nov, 1994
M Soleimani, G Singh, GL Bizal, SR Gullans and JA McAteer
Recent cloning experiments have identified the existance of four distinct
Na+/H+ exchanger isoforms designated as NHE-1, NHE-2, NHE-3, and NHE-4. The
cellular distribution, subcellular localization, and regulation of one of
these isoforms, NHE-2, in the kidney remains unknown. Northern
hybridization showed that NHE-2, along with NHE-1, is expressed in cultured
renal medullary collecting duct (mIMCD-3) cells. Acid-stimulated, dimethyl
amiloride-sensitive 22Na+ uptake and sodium- dependent pHi recovery
occurred only from the basolateral surface of the cells, indicating
localization of Na+/H+ exchanger to the basolateral membrane domain.
Incubation of IMCD cells in high osmolality media (510 mosm/liter) for 72 h
stimulated the Na+/H+ exchanger activity by 59% (p < 0.001). NHE-1 mRNA
abundance decreased, whereas NHE-2 mRNA increased in high osmolality media.
Incubation of IMCD cells in acid media (pH 7.1) for 48 h did not affect the
Na+/H+ exchanger activity compared with control (pH 7.4) (p > 0.05).
Northern hybridization, however, indicated that NHE-1 mRNA increased,
whereas NHE-2 mRNA decreased in acid media. In conclusion, mIMCD-3 cells
express NHE-1 and NHE-2 mRNAs. The cell functional studies in mIMCD-3 cells
strongly suggest that NHE-2, along with NHE-1, is expressed in the
basolateral membrane domain. They further demonstrate differential
regulation of NHE-1 and NHE-2 mRNAs in response to acidosis and high
osmolality and suggest that NHE-2 may be involved in volume regulation of
IMCD cells.
Na+/H+ exchanger isoforms NHE-2 and NHE-1 in inner medullary collecting duct cells. Expression, functional localization, and differential regulation
Department of Medicine, Indiana University School of Medicine, Indianapolis.
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