Comparative functional analysis of aquaporins/glyceroporins in mammals and anurans
Open Access
- 1 July 2007
- journal article
- research article
- Published by Springer Nature in Mammalian Genome
- Vol. 18 (6-7), 452-462
- https://doi.org/10.1007/s00335-007-9041-5
Abstract
Maintenance of fluid homeostasis is critical to establishing and maintaining normal physiology. The landmark discovery of membrane water channels (aquaporins; AQPs) ushered in a new area in osmoregulatory biology that has drawn from and contributed to diverse branches of biology, from molecular biology and genomics to systems biology and evolution, and from microbial and plant biology to animal and translational physiology. As a result, the study of AQPs provides a unique and integrated backdrop for exploring the relationships between genes and genome systems, the regulation of gene expression, and the physiologic consequences of genetic variation. The wide species distribution of AQP family members and the evolutionary conservation of the family indicate that the control of membrane water flux is a critical biological process. AQP function and regulation is proving to be central to many of the pathways involved in individual physiologic systems in both mammals and anurans. In mammals, AQPs are essential to normal secretory and absorptive functions of the eye, lung, salivary gland, sweat glands, gastrointestinal tract, and kidney. In urinary, respiratory, and gastrointestinal systems, AQPs are required for proper urine concentration, fluid reabsorption, and glandular secretions. In anurans, AQPs are important in mediating physiologic responses to changes in the external environment, including those that occur during metamorphosis and adaptation from an aquatic to terrestrial environment and thermal acclimation in anticipation of freezing. Therefore, an understanding of AQP function and regulation is an important aspect of an integrated approach to basic biological research.Keywords
This publication has 118 references indexed in Scilit:
- Fast and Selective Ammonia Transport by Aquaporin-8Journal of Biological Chemistry, 2007
- Severe urinary concentrating defect in renal collecting duct-selective AQP2 conditional-knockout miceProceedings of the National Academy of Sciences, 2006
- Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar cellsBiochemical and Biophysical Research Communications, 2005
- Cyclic AMP Regulates Aquaporin 5 Expression at Both Transcriptional and Post-transcriptional Levels through a Protein Kinase A PathwayJournal of Biological Chemistry, 2003
- Molecular and cellular defects in nephrogenic diabetes insipidusPediatric Nephrology, 2001
- Structural clues in the sequences of the aquaporinsJournal of Molecular Biology, 2000
- α1-Adrenoceptor-Induced Trafficking of Aquaporin-5 to the Apical Plasma Membrane of Rat Parotid CellsBiochemical and Biophysical Research Communications, 1999
- Immunolocalization of Aquaporin Homologs in Mouse Lacrimal GlandsBiochemical and Biophysical Research Communications, 1997
- Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 proteinBiochemistry, 1992
- Evolution of the MIP family of integral membrane transport proteinsMolecular Microbiology, 1991