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Publication : Molecular characterization of a broad selectivity neutral solute channel.

First Author  Tsukaguchi H Year  1998
Journal  J Biol Chem Volume  273
Issue  38 Pages  24737-43
PubMed ID  9733774 Mgi Jnum  J:69559
Mgi Id  MGI:1934822 Doi  10.1074/jbc.273.38.24737
Citation  Tsukaguchi H, et al. (1998) Molecular characterization of a broad selectivity neutral solute channel. J Biol Chem 273(38):24737-43
abstractText  In all living cells, coordination of solute and water movement across cell membranes is of critical importance for osmotic balance. The current concept is that these processes are of distinct biophysical nature. Here we report the expression cloning of a liver cDNA encoding a unique promiscuous solute channel (AQP9) that confers high permeability for both solutes and water. AQP9 mediates passage of a wide variety of non-charged solutes including carbamides, polyols, purines, and pyrimidines in a phloretin- and mercury-sensitive manner, whereas amino acids, cyclic sugars, Na+, K+, Cl-, and deprotonated monocarboxylates are excluded. The properties of AQP9 define a new evolutionary branch of the major intrinsic protein family of aquaporin proteins and describe a previously unknown mechanism by which a large variety of solutes and water can pass through a single pore, enabling rapid cellular uptake or exit of metabolites with minimal osmotic perturbation.
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