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Am J Physiol Renal Physiol 284: F122-F132, 2003. First published August 21, 2002; doi:10.1152/ajprenal.00161.2002
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Vol. 284, Issue 1, F122-F132, January 2003

Characterization of PMCA isoforms and their contribution to transcellular Ca2+ flux in MDCK cells

Sertac N. Kip and Emanuel E. Strehler

Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905

Plasma membrane Ca2+ ATPases (PMCAs) are ubiquitous in Ca2+-transporting organs, including the kidney. Using RT-PCR, we detected PMCA1b, PMCA2b (rare), and PMCA4b in Madin-Darby canine kidney (MDCK) cells. At the protein level, only PMCA1 and PMCA4 were readily detected and were highly enriched in the basolateral membrane. The Na+/Ca2+ exchanger NCX1 was also detected at the transcript and protein level. A functional assay measuring 45Ca2+ flux across MDCK cell monolayers under resting conditions indicated that two-thirds of apicobasolateral Ca2+ transport was provided by Na+/Ca2+ exchanger and one-third by PMCAs, as determined in Na+-free media and using various PMCA inhibitors (La3+, vanadate, calmidazolium, and trifluoroperazine). The importance of PMCA4b for basolateral Ca2+ efflux was demonstrated by overexpression of PMCA4b or antisense knockdown of endogenous PMCA4b. Overexpression of PMCA4b increased apicobasolateral Ca2+ transport to ~140%, whereas antisense treatment reduced Ca2+ flux ~45% compared with controls. The MDCK system is thus an ideal model for functional studies of the specific role and regulation of PMCA isoforms in Ca2+ reabsorption in the distal kidney.

calcium transport; kidney distal tubules; Madin-Darby canine kidney; sodium/calcium exchanger; plasma membrane calcium ATPase


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