Aquaporin water channels: atomic structure molecular dynamics meet clinical medicine.
Aquaporin water channels: atomic structure molecular dynamics meet clinical medicine.
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DOI:
10.1172/jci0215851
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发表时间:
2002-06
期刊:
影响因子:
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通讯作者:
D. Kozono;M. Yasui;L. King;P. Agre
中科院分区:
文献类型:
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作者:
D. Kozono;M. Yasui;L. King;P. Agre
The movement of water across cell membranes is fundamental to life. Water constitutes roughly 70% of the mass of most living organisms, so the orderly distribution of water is required to maintain proper fluid balance within different anatomic compartments. Although water is known to diffuse through lipid bilayers, diffusion is not sufficiently rapid for many physiological processes. To accommodate these needs, a family of membrane channel proteins evolved for rapid transport of water across biological membranes. These proteins, termed “aquaporins,” are found in all life forms, including archaea, eubacteria, fungi, plants, and all phyla of animals. Since the discovery of the aquaporins ten years ago (1), researchers around the world have sought to learn how these proteins work. Selectivity, rates of permeation, and gating mechanisms are three properties that characterize channel proteins. Aquaporins are exquisitely selective for the transport of water — even repelling hydronium ions (H3O+). The importance of the latter is emphasized by the normal function of mammalian renal tubules, which reabsorb 99% of the water from glomerular filtrate at the same time that acid is secreted by intercalated cells. Some members of the aquaporin superfamily are permeated by a variety of small neutral solutes such as glycerol or urea (termed “aquaglyceroporins”) (2). The transport of water or glycerol through aquaporins represents facilitated diffusion driven by osmotic or concentration gradients.