Abstract
Aquaporin 1, a six-transmembrane domain protein, is a water channel present in many fluid-secreting and -absorbing cells. In Xenopus oocytes injected with aquaporin 1 complementary RNA, the application of forskolin or cyclic 8-bromo- adenosine 3',5'-monophosphate increased membrane permeability to water and triggered a cationic conductance. The cationic conductance was also induced by direct injection of protein kinase A (PKA) catalytic subunit, reduced by the kinase inhibitor H7, and blocked by HgCl2, an inhibitor of aquaporin 1. The cationic permeability of the aquaporin 1 channel is activated by a cyclic adenosine monophosphate-dependent mechanism that may involve direct or indirect phosphorylation by PKA.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
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8-Bromo Cyclic Adenosine Monophosphate / pharmacology
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Animals
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Aquaporin 1
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Aquaporins*
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Cations / metabolism*
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Cell Membrane Permeability / drug effects*
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Colforsin / pharmacology*
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Cyclic AMP / metabolism*
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Cyclic AMP-Dependent Protein Kinases / antagonists & inhibitors
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Cyclic AMP-Dependent Protein Kinases / metabolism
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Enzyme Inhibitors / pharmacology
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Ion Channels / drug effects
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Ion Channels / genetics
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Ion Channels / metabolism*
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Isoquinolines / pharmacology
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Mercuric Chloride / pharmacology
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Oocytes
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Patch-Clamp Techniques
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Phosphorylation
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Piperazines / pharmacology
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RNA, Complementary / genetics
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Water / metabolism*
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Xenopus
Substances
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Aquaporins
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Cations
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Enzyme Inhibitors
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Ion Channels
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Isoquinolines
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Piperazines
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RNA, Complementary
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Water
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Aquaporin 1
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Colforsin
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8-Bromo Cyclic Adenosine Monophosphate
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Mercuric Chloride
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1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
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Cyclic AMP
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Cyclic AMP-Dependent Protein Kinases