Mutations in
            <i>aquaporin-1</i>
            in Phenotypically Normal Humans Without Functional CHIP Water Channels

Gregory M. Preston, Barbara L. Smith, Mark L. Zeidel, John J. Moulds, Peter Agre

doi:10.1126/science.7521540

Mutations in <i>aquaporin-1</i> in Phenotypically Normal Humans Without Functional CHIP Water Channels

DOI Web Site 被引用文献13件

Gregory M. Preston

Departments of Biological Chemistry and Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Barbara L. Smith

Departments of Biological Chemistry and Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Mark L. Zeidel

Department of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213, USA.
John J. Moulds

Gamma Biologicals, Houston, TX 77092, USA.
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>