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Characterization of the gene encoding the human LW blood group protein in
LW+ and LW- phenotypes
P Hermand, PY Le Pennec, P Rouger, JP Cartron and P Bailly
INSERM U76, Institut National de la Transfusion Sanguine, Paris, France.
The LW blood group is carried by a 42-kD glycoprotein that belongs to the
family of intercellular adhesion molecules. The LW gene is organized into
three exons spanning an HindIII fragment of approximately 2.65 kb. The
exon/intron architecture correlates to the structural domains of the
protein and resembles that of other Ig superfamily members except that the
signal peptide and the first Ig- like domain are encoded by the first exon.
The 5'UT region (nucleotides -289 to +9) includes potential binding sites
for various transcription factors (Ets, CACC, SP1, GATA-1, AP2) and
exhibited a significant transcriptional activity after transfection in the
erythroleukemic K562 cells. No obvious abnormality of the LW gene,
including the 5'UT region, has been detected by sequencing polymerase chain
reaction- amplified genomic DNA from RhD+ or RhD- donors and from an Rhnull
variant that lacks the Rh and LW proteins on red blood cells. However, a
deletion of 10 bp in exon 1 of the LW gene was identified in the genome of
an LW (a- b-) individual (Big) deficient for LW antigens but carrying a
normal Rh phenotype. The 10-bp deletion generates a premature stop codon
and encodes a truncated protein without transmembrane and cytoplasmic
domain. No detectable abnormality of the LW gene or transcript could be
detected in another LW(a- b-) individual (Nic), suggesting the
heterogeneity of these phenotypes.
Volume 87,
Issue 7,
pp. 2962-2967,
04/01/1996
Copyright © 1996 by The American Society of Hematology
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