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J. Biol. Chem., Vol. 277, Issue 48, 45854-45859, November 29, 2002

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AQP3 Deficiency in Humans and the Molecular Basis of a Novel Blood Group System, GIL^*

Nathalie Roudier, Pierre Ripoche, Pierre Gane, Pierre Yves Le Pennec, Geoff Daniels^§, Jean-Pierre Cartron^¶, and Pascal Bailly

From  INSERM U76, Institut National de la Transfusion Sanguine, 6 rue Alexandre Cabanel, 75015 Paris, France and ^§ Bristol Institute for Transfusion Sciences, Bristol BS10 5ND, United Kingdom

AQP3 is a water and glycerol channel present on human erythrocytes and in various tissues. By protein and molecular biology analysis, two unrelated probands who developed alloantibodies to the high frequency antigen GIL were found to be AQP3-deficient. The defect is caused by homozygous mutation affecting the 5' donor splice site of intron 5 of the AQP3 gene. This mutation causes the skipping of exon 5 and generates a frameshift and premature stop codon. Functional studies by 90° light scattering using a stopped-flow spectrometer revealed the absence of facilitated glycerol transport across red cell membranes from the probands, but the water and urea transports were normal. Expression studies into COS-7 cells followed by flow cytometry analysis showed that only cells transfected with AQP3 cDNA strongly reacted with anti-GIL antibodies. These findings represent the first reported cases of AQP3 deficiency in humans and provide the molecular basis of a new blood group system, GIL, encoded by the AQP3 protein.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ493596, AJ493597.

The amino acid sequence of this protein can be accessed through NCBI Protein Database under NCBI accession number NM_004925.

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