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1 Institute of Anatomy, University of Aarhus, Aarhus, Denmark
* To whom correspondence should be addressed. E-mail: jp{at}ana.au.dk.
The electroneutral sodium bicarbonate cotransporter NBCn1 or NBC3 was originally cloned from rat aorta and from human skeletal muscle. NBCn1/NBC3 has been localized to the basolateral membrane of various epithelia, but thus far it has been impossible to detect the protein in these tissues using anti-c-terminal antibodies. Hence, an antibody was developed against the n-terminal of NBCn1 and validated by peptide recognition, immunoblotting on positive control tissues, and by binding of an approximately 180 kDa protein in rat kidney, cerebrum, cerebellum and duodenum. In addition, an approximately 180 kDa immunoreactive band appeared using samples from the aorta, heart ventricles and atria, mesenteric arteries, liver, and epididymis. Immunohistochemical analysis confirmed the previously described labeling in the kidney, duodenum and the choroid plexus. The anti-n-terminal antibody localized NBCn1 to the plasma membrane domains of endothelia and smooth muscle cells in small mesenteric and renal arteries, as well as the capillaries of the heart ventricles, spleen and salivary glands. NBCn1 was also detected in neuromuscular junctions and vasculature in skeletal muscle. Analysis of variable NBCn1 splicing by RT-PCR revealed that an n-terminal sequence, the cassette III, seems absent from cardiovascular NBCn1, and that both cassette I and III are variable in most epithelia, while cassette II is absent from epithelial NBCn1. Thus, the development of the n-terminal antibody allowed the localization of NBCn1 protein to major cardiovascular tissues where NBCn1 mRNA was previously detected. The NBCn1 is a likely candidate for mediating the reported electroneutral Na+:HCO3- cotransport in vascular smooth muscle.
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