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1 The Water and Salt Research Center, University of Aarhus, Aarhus, Denmark; Institute of Anatomy, University of Aarhus, Aarhus, Denmark
2 Department of Medicine, Harvard Medical School, Molecular and Vascular Medicine Unit and Renal Unit, Beth Israel Deaconess Medical Center, Boston, MA, USA
3 Renal Division, Emory University School of Medicine, Atlanta, GA, USA
* To whom correspondence should be addressed. E-mail: sn{at}ana.au.dk.
Three splice-variants of AE2, (AE2a, b and c) have been described in rat, but their relative distribution in rat kidney is not known. The purpose of this study was to describe the segmental and cellular distribution of the AE2 isoforms in rat kidney and to evaluate if the expression levels of these AE2 isoforms are regulated independently in response to chronic NH4Cl-loading. Two polyclonal antibodies were generated respectively recognizing an N-terminal peptide unique to AE2a and an aminoacid-sequence common to AE2a and AE2b. Antibody specificities were tested using cells transfected separately with the AE2a, AE2b and AE2c isoforms. Immunohistochemistry on sections of paraffin-embedded rat kidneys showed a distribution of AE2a/AE2b labeling in kidney similar to the distribution of AE2 in rat kidney reported previously. AE2 is highly expressed in mTAL, cTAL and macula densa. The pattern of AE2a-specific labeling differed from the pattern of AE2a/AE2b labeling in that relatively more of the total immunolabel was observed in the terminal IMCD. NH4Cl-loading (0.033 mmoles NH4Cl/g bw for 7 days) did not change the labeling of AE2 isoforms in the medulla, whereas the labeling in cortex was intensified and included more distal parts of cTAL. Immunoblotting confirmed upregulation of AE2a/b-expression in cortex. These results indicate that AE2a and AE2b are differentially expressed and regulated in rat kidney. The regulation following NH4Cl-loading of AE2b in cTAL suggests a role of AE2 in transepithelial bicarbonate reabsorption in this segment.
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