References 1. Chou, C. L, T. Ma, B. Yang, M. A. Knepper, and A. S. Verkman. Fourfold reduction of water permeability in inner medullary collecting duct of aquaporin-4 knockout mice. Am. J. Physiol. 274 (Cell Physiol. 43): C549–C554, 1998. 2. Ma, T., B. Yang, A. Gillespie, E. J. Carlson, C. J. Epstein, and A. S. Verkman. Severely impaired urinary concentrating ability in transgenic mice lacking ...

Aquaporin-3 (AQP3) and aquaporin-4 (AQP4) are homologous proteins expressed in the basolateral plasma membrane of kidney collecting duct principal cells, where they mediate the exit pathway for apically reabsorbed water. Although both proteins are localized to the same plasma membrane domain, it is unknown if they are sorted together in the Golgi, or arrive in the same or different vesicles at ...

The goal of this work is to investigate whether and how non-invasive MRI methods can contribute to studying the role of Aquaporin-4 in water transport in the brain. Aquaporin 4 (AQP-4) is the predominant water channel protein in the neocortex and cerebellum. It is concentrated in the astrocyte end-feet membranes, adjacent to blood vessels to facilitate fast, selective and activity dependent wat...

In the present paper we explored the capacity of yeast Saccharomyces cerevisiae as host for heterologous expression of human Aquaporin-1. Aquaporin-1 cDNA was expressed from a galactose inducible promoter situated on a plasmid with an adjustable copy number. Human Aquaporin-1 was C-terminally tagged with yeast enhanced GFP for quantification of functional expression, determination of sub-cellul...