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We begin with the history of aquaporin zero (AQP0), the most prevalent membrane protein in the eye lens, from the early days when AQP0 was a protein of unknown function known as Major Intrinsic Protein 26. We progress through its joining the aquaporin family as a water channel in its own right and discuss how regulation of its water permeability by pH and calcium came to be discovered experimentally and linked to lens homeostasis and development. We review the development of molecular dynamics (MD) simulations of lipid bilayers and membrane proteins, including aquaporins, with an emphasis on simulation studies that have elucidated the mechanisms of water conduction, selectivity, and proton exclusion by aquaporins in general. We also review experimental and theoretical progress toward understanding why mammalian AQP0 has a lower water permeability than other aquaporins and the evolution of our present understanding of how its water permeability is regulated by pH and calcium. Finally, we discuss how MD simulations have elucidated the nature of lipid interactions with AQP0.
This article was published in the following journal.
Name: Chemical reviews
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Aquaporin 4 is the major water-selective channel in the CENTRAL NERVOUS SYSTEM of mammals.
Aquaporin 5 is a water-specific channel protein that is expressed primarily in alveolar, tracheal, and upper bronchial EPITHELIUM. It plays an important role in maintaining water HOMEOSTASIS in the LUNGS and may also regulate release of SALIVA and TEARS in the SALIVARY GLANDS and the LACRIMAL GLAND.
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