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 Blood, 15 December 2008, Vol. 112, No. 13, pp. 5212-5218.
Prepublished online as a Blood First Edition Paper on September 26, 2008; DOI 10.1182/blood-2008-03-146068.

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RED CELLS

Adhesive activity of Lu glycoproteins is regulated by interaction with spectrin

Xiuli An1, Emilie Gauthier1, Xihui Zhang1, Xinhua Guo1, David J. Anstee2, Narla Mohandas1, and Joel Anne Chasis3

1 Red Cell Physiology Laboratory, New York Blood Center, NY; 2 Bristol Institute for Transfusion Sciences, Bristol, United Kingdom; and 3 Life Sciences Division, University of California Lawrence Berkeley National Laboratory

The Lutheran (Lu) and Lu(v13) blood group glycoproteins function as receptors for extracellular matrix laminins. Lu and Lu(v13) are linked to the erythrocyte cytoskeleton through a direct interaction with spectrin. However, neither the molecular basis of the interaction nor its functional consequences have previously been delineated. In the present study, we defined the binding motifs of Lu and Lu(v13) on spectrin and identified a functional role for this interaction. We found that the cytoplasmic domains of both Lu and Lu(v13) bound to repeat 4 of the {alpha} spectrin chain. The interaction of full-length spectrin dimer to Lu and Lu(v13) was inhibited by repeat 4 of {alpha}-spectrin. Further, resealing of this repeat peptide into erythrocytes led to weakened Lu-cytoskeleton interaction as demonstrated by increased detergent extractability of Lu. Importantly, disruption of the Lu-spectrin linkage was accompanied by enhanced cell adhesion to laminin. We conclude that the interaction of the Lu cytoplasmic tail with the cytoskeleton regulates its adhesive receptor function.


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