The recent discovery of aquaporins, a family of highly conserved water channel proteins, which are expressed in both eukaryotes and prokaryotes, has provoked a re-evaluation of the physiology of water transport in all organisms. So far, seven distinct aquaporins have been characterised in mammals, but highly homologous family members have also been found in amphibians, insects, plants and bacteria. These transmembrane proteins serve to facilitate water transport down osmotic gradients with low activation energy. Alterations in channel expression, cellular targeting and perhaps channel permeability regulate membrane water transport. Naturally occurring and experimentally produced mutations in aquaporins cause a variety of perturbations of water homeostasis. Manipulation of aquaporin expression may have a therapeutic role in several disease processes including cardiac failure and the ascites associated with liver disease.