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Blood, 1 January 2001, Vol. 97, No. 1, pp. 312-320
RED CELLS
Lutheran blood group glycoprotein and its newly characterized
mouse homologue specifically bind  5 chain-containing human laminin
with high affinity
Stephen F. Parsons,
Gloria Lee,
Frances A. Spring,
Thiebaut-Noel Willig,
Luanne L. Peters,
J. Aura Gimm,
Michael J. A. Tanner,
Narla Mohandas,
David J. Anstee, and
Joel Anne Chasis
From the Bristol Institute for Transfusion Sciences,
Bristol, United Kingdom; Life Sciences Division, University of
California Lawrence Berkeley National Laboratory, Berkeley CA; The
Jackson Laboratory, Bar Harbor, ME; and University of Bristol, Bristol,
United Kingdom.
Lutheran blood group glycoproteins (Lu gps) are receptors for the
extracellular matrix protein, laminin. Studies suggest that Lu gps may
contribute to vaso-occlusion in sickle cell disease and it has recently
been shown that sickle cells adhere to laminin isoforms containing the
 5 chain (laminin 10/11). Laminin 5 is present in the
subendothelium and is also a constituent of bone marrow sinusoids,
suggesting a role for the Lu/laminin interaction in erythropoiesis. The
objectives of the current study were to define more precisely the
molecular interactions of the extracellular and intracellular regions
of human Lu and to clone and characterize a mouse homologue. To this
end, complementary DNA and genomic clones for the mouse homologue were
sequenced and the mouse Lu gene mapped to a region on
chromosome 7 with conserved synteny with human 19q13.2. Mouse and human
Lu gps are highly conserved (72% identity) at the amino acid sequence
level and both mouse and human Lu gps specifically bind laminin 10/11
with high affinity. Furthermore, the first 3, N-terminal,
immunoglobulin superfamily domains of human Lu are critical for this
interaction. The results indicated that the cytoplasmic domain of BRIC
221-labeled human Lu gp is linked with the spectrin-based skeleton,
affording the speculation that this interaction may be critical for
signal transduction. These results further support a role for Lu gps in
sickle cell disease and indicate the utility of mouse models to explore
the function of Lu gp-laminin 10/11 interaction in normal
erythropoiesis and in sickle cell disease.
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