Mutations in <i>aquaporin-1</i> in Phenotypically Normal Humans Without Functional CHIP Water Channels
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- Gregory M. Preston
- Departments of Biological Chemistry and Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
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- Barbara L. Smith
- Departments of Biological Chemistry and Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
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- Mark L. Zeidel
- Department of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213, USA.
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- John J. Moulds
- Gamma Biologicals, Houston, TX 77092, USA.
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- Peter Agre
- Departments of Biological Chemistry and Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
抄録
<jats:p> The gene <jats:italic>aquaporin-1</jats:italic> encodes channel-forming integral protein (CHIP), a member of a large family of water transporters found throughout nature. Three rare individuals were identified who do not express CHIP-associated Colton blood group antigens and whose red cells exhibit low osmotic water permeabilities. Genomic DNA analyses demonstrated that two individuals were homozygous for different nonsense mutations (exon deletion or frameshift), and the third had a missense mutation encoding a nonfunctioning CHIP molecule. Surprisingly, none of the three suffers any apparent clinical consequence, which raises questions about the physiological importance of CHIP and implies that other mechanisms may compensate for its absence. </jats:p>
収録刊行物
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- Science
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Science 265 (5178), 1585-1587, 1994-09-09
American Association for the Advancement of Science (AAAS)
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詳細情報
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- CRID
- 1363670320618827264
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- NII論文ID
- 80007854667
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- ISSN
- 10959203
- 00368075
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- データソース種別
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