Expression and localization of an aquaporin-1 homologue in the avian kidney and lower intestinal tract.

In birds, the kidneys and lower intestine function in osmoregulation. A 271-amino acid homologue to aquaporin-1 (AQP-1) was isolated from the kidneys, cecae, proximal and distal rectum, and coprodeum of the lower intestine in the house sparrow (Passer domesticus). This protein has six transmembrane domains connected by two cytoplasmic loops and three extracellular loops. It exhibits 94%, 88%, and 78% homology to AQP-1 sequences of chicken, human and toad, respectively. Many of the highly conserved amino acids that are characteristic of AQP-1 are found in the sparrow sequence. RT-PCR was performed and the presence of AQP-1 mRNA was detected in the kidney and all four regions of the lower intestine. Immunoblots of total protein identified a 28-kDa non-glycosylated AQP-1 band and a 56-kDa glycosylated AQP-1 band in the kidney and all four regions of the lower intestine. Immunohistochemistry demonstrated the presence of the AQP-1 protein within both the renal cortex and medulla. In the lower intestine, the protein was present in the proximal rectum, distal rectum, and in the coprodeum. As AQP-1 functions to allow water movement across mammalian cell membranes, its presence in water-permeable cells in a bird suggests it may have a similar function.