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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1996-10-4
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pubmed:abstractText |
Discovery of aquaporin water channel proteins has provided insight into the molecular mechanism of membrane water permeability. The distribution of known mammalian aquaporins predicts roles in physiology and disease. Aquaporin-1 mediates proximal tubule fluid reabsorption, secretion of aqueous humor and cerebrospinal fluid, and lung water homeostasis. Aquaporin-2 mediates vasopressin-dependent renal collecting duct water permeability; mutations or downregulation can cause nephrogenic diabetes insipidus. Aquaporin-3 in the basolateral membrane of the collecting duct provides an exit pathway for reabsorbed water. Aquaporin-4 is abundant in brain and probably participates in reabsorption of cerebrospinal fluid, osmoregulation, and regulation of brain edema. Aquaporin-5 mediates fluid secretion in salivary and lacrimal glands and is abundant in alveolar epithelium of the lung. Specific regulation of membrane water permeability will likely prove important to understanding edema formation and fluid balance in both normal physiology and disease.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AQP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/AQP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/AQP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/AQP4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporin 2,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporin 3,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporin 4,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporin 6,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporins,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Group Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels
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pubmed:status |
MEDLINE
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pubmed:issn |
0066-4278
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
619-48
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8815812-Animals,
pubmed-meshheading:8815812-Aquaporin 1,
pubmed-meshheading:8815812-Aquaporin 2,
pubmed-meshheading:8815812-Aquaporin 3,
pubmed-meshheading:8815812-Aquaporin 4,
pubmed-meshheading:8815812-Aquaporin 6,
pubmed-meshheading:8815812-Aquaporins,
pubmed-meshheading:8815812-Blood Group Antigens,
pubmed-meshheading:8815812-Cell Membrane Permeability,
pubmed-meshheading:8815812-Humans,
pubmed-meshheading:8815812-Ion Channels,
pubmed-meshheading:8815812-Water-Electrolyte Balance
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pubmed:year |
1996
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pubmed:articleTitle |
Pathophysiology of the aquaporin water channels.
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pubmed:affiliation |
Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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