Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.

Bibliographic Collection: 
MOCA Reference, APE
Publication Type: Journal Article
Authors: Preston, G M; Carroll, T P; Guggino, W B; Agre, P
Year of Publication: 1992
Journal: Science
Volume: 256
Issue: 5055
Pagination: 385-7
Date Published: 1992 Apr 17
Publication Language: eng
ISSN: 0036-8075
Keywords: Animals, Aquaporin 1, Aquaporins, Cell Membrane Permeability, Electric Conductivity, Erythrocyte Membrane, Immunoblotting, Membrane Proteins, Mercuric Chloride, Molecular Structure, Oocytes, Osmolar Concentration, RNA, Thermodynamics, Transfection, Water, Xenopus laevis

Water rapidly crosses the plasma membrane of red blood cells (RBCs) and renal tubules through specialized channels. Although selective for water, the molecular structure of these channels is unknown. The CHIP28 protein is an abundant integral membrane protein in mammalian RBCs and renal proximal tubules and belongs to a family of membrane proteins with unknown functions. Oocytes from Xenopus laevis microinjected with in vitro-transcribed CHIP28 RNA exhibited increased osmotic water permeability; this was reversibly inhibited by mercuric chloride, a known inhibitor of water channels. Therefore it is likely that CHIP28 is a functional unit of membrane water channels.

Alternate Journal: Science
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