Amphibian aquaporins and adaptation to terrestrial environments: A review

In many anurans, the pelvic patch of the ventral skin and the urinary bladder are important osmoregulatory organs. Since the discovery of water channel protein, aquaporin (AQP), in mammalian erythrocytes, 17 distinct full sequences of AQP mRNAs have been identified in anurans. Phylogenetic tree of AQP proteins from amphibians and mammals suggested that anuran AQPs can be divided into six types: i.e. types 1, 2, 3, and 5, and anuran-specific types al and a2. Among them, two types of anuran AQPs (types I and a2) are localized in the skin and urinary bladder by immunohistochemistry. Tree frog type-a2 AQPs, AQP-h2 and AQP-h3, are vasotocin-regulated water channels predominant in the osmoregulatory organs. Both the AQP-h2 and AQP-h3 are expressed at the granular cells underneath the keratinized layer in the pelvic patch, whereas only AQP-h2 is detected at the granular cells in the urinary bladder. In response to vasotocin, both the molecules seem to be translocated from the cytoplasmic pool to the apical plasma membrane of the granular cells. On the other hand, type-1 AQPs, Rana FA-CHIP and Hyla AQP-h1, are detected at the endothelial cells of blood capillaries in frog osmoregulatory organs. These findings suggest that AQP-h2 and AQP-h3 are key players for transepithelial water movement, and that FA-CHIP and AQP-h1 might be important for the transport of absorbed water into the blood flow. Comparative investigation of type-a2 AQPs in anurans further revealed that AQP-h2 and -h3-like molecules might exist at the urinary bladder and the pelvic skin, respectively, in various anurans from aquatic species to arboreal dwellers. AQP-h2-like protein is also detected in the pelvic skin of terrestrial and arboreal species. It is possible that this molecule might have occurred in the pelvic skin as anurans penetrated into drier environments. (c) 2006 Elsevier Inc. All rights reserved.