Fast and Selective Ammonia Transport by Aquaporin-8
نویسندگان
چکیده
منابع مشابه
Fast and selective ammonia transport by aquaporin-8.
The transport of ammonia/ammonium is fundamental to nitrogen metabolism in all forms of life. So far, no clear picture has emerged as to whether a protein channel is capable of transporting exclusively neutral NH(3) while excluding H(+) and NH(4)(+). Our research is the first stoichiometric study to show the selective transport of NH(3) by a membrane channel. The purified water channel protein ...
متن کاملEvidence from knockout mice against physiologically significant aquaporin 8-facilitated ammonia transport.
Aquaporin (AQP)8-facilitated transport of NH(3) has been suggested recently by increased NH(3) permeability in Xenopus oocytes and yeast expressing human or rat AQP8. We tested the proposed roles of AQP8-facilitated NH(3) transport in mammalian physiology by comparative phenotype studies in wild-type vs. AQP8-null mice. AQP8-facilitated NH(3) transport was confirmed in mammalian cell cultures e...
متن کاملThe Knockdown of Hepatocyte Aquaporin-8 by Rna Interference Induces Defective Bile Canalicular Water Transport*
Aquaporin-8 (AQP8) water channels, which are expressed in rat hepatocyte bile canalicular membranes, are involved in water transport during bile formation. Nevertheless, there is no conclusive evidence that AQP8 mediates water secretion into the bile canaliculus. In this study, we directly evaluated whether AQP8 gene silencing by RNA interference inhibits canalicular water secretion in the huma...
متن کاملKnockdown of hepatocyte aquaporin-8 by RNA interference induces defective bile canalicular water transport.
Aquaporin-8 (AQP8) water channels, which are expressed in rat hepatocyte bile canalicular membranes, are involved in water transport during bile formation. Nevertheless, there is no conclusive evidence that AQP8 mediates water secretion into the bile canaliculus. In this study, we directly evaluated whether AQP8 gene silencing by RNA interference inhibits canalicular water secretion in the huma...
متن کاملCrystal Structure of an Ammonia-Permeable Aquaporin.
Aquaporins of the TIP subfamily (Tonoplast Intrinsic Proteins) have been suggested to facilitate permeation of water and ammonia across the vacuolar membrane of plants, allowing the vacuole to efficiently sequester ammonium ions and counteract cytosolic fluctuations of ammonia. Here, we report the structure determined at 1.18 Å resolution from twinned crystals of Arabidopsis thaliana aquaporin ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2007
ISSN: 0021-9258
DOI: 10.1074/jbc.m609343200