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J Biol Chem, Vol. 273, Issue 27, 16686-16693, July 3, 1998
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From The Lutheran antigens are recently
characterized glycoproteins in which the extracellular region contains
five immunoglobulin like domains, suggesting some recognition function.
A recent abstract suggests that the Lutheran glycoproteins (Lu gps) act
as erythrocyte receptors for soluble laminin (Udani, M., Jefferson, S.,
Daymont, C., Zen, Q., and Telen, M. J. (1996) Blood
88, Suppl. 1, 6 (abstr.)). In the present report, we provided the
definitive proof of the laminin receptor function of the Lu gps by
demonstrating that stably transfected cells (murine L929 and human K562
cell lines) expressing the Lu gps bound laminin in solution and
acquired adhesive properties to laminin-coated plastic dishes but not
to fibronectin, vitronectin, transferrin, fibrinogen, or fibrin.
Furthermore, expression of either the long-tail (85 kDa) or the
short-tail (78 kDa) Lu gps, which differ by the presence or the absence
of the last 40 amino acids of the cytoplasmic domain, respectively, conferred to transfected cells the same laminin binding capacity. We
also confirmed by flow cytometry analysis that the level of laminin
binding to red cells is correlated with the level of Lu antigen
expression. Indeed, Lunull cells did not bind to laminin, whereas sickle cells from most patients homozygous for hemoglobin S
overexpressed Lu antigens and exhibited an increased binding to
laminin, as compared with normal red cells. Laminin binding to normal
and sickle red cells as well as to Lu transfected cells was totally
inhibited by a soluble Lu-Fc chimeric fragment containing the
extracellular domain of the Lu gps. During in vitro
erythropoiesis performed by two-phase liquid cultures of human
peripheral blood, the appearance of Lu antigens in late erythroid
differentiation was concomitant with the laminin binding capacity of
the cultured erythroblasts. Altogether, our results demonstrated that
long-tail and short-tail Lu gps are adhesion molecules that bind
equally well laminin and strongly suggested that these glycoproteins
are the unique receptors for laminin in normal and sickle mature red cells as well as in erythroid progenitors.
INSERM U76,
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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