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J Biol Chem, Vol. 274, Issue 2, 728-734, January 8, 1999
,
, and
From the Basal cell adhesion molecule (B-CAM) and Lutheran
(LU) are two spliceoforms of a single immunoglobulin superfamily
protein containing five Ig domains and comprise the sickle (SS) red
cell receptor for laminin. We have now analyzed laminin binding to murine erythroleukemia cells transfected with various human B-CAM/LU constructs. B-CAM and LU bound equally well to laminin, indicating that
the longer cytoplasmic tail of LU is not required for binding. However,
binding of soluble laminin did require the presence of the
membrane-proximal fifth immunoglobulin superfamily (IgSF) domain of LU,
while deletion of IgSF domains 1, 2, 3, or 4 individually or together
did not abrogate laminin binding. Under flow conditions, MEL cells
expressing B-CAM, LU, and LU lacking domains 1, 2, 3, or 4 adhered to
immobilized laminin with critical shear stresses over 10 dynes/cm2. However, MEL cells expressing LU lacking
domain 5 bound to laminin poorly (critical shear stress = 2.3 dynes/cm2). Moreover, expression of only IgSF domain 5 of
LU was sufficient to mediate MEL cell adhesion to immobilized laminin
(critical shear stress >10 dynes/cm2). Finally, Scatchard
analysis showed that SS red cells had an average of 67% more B-CAM/LU
than normal red cells, and low density red cells from sickle cell
disease patients expressed 40-55% more B-CAM/LU than high density SS
red cells. B-CAM/LU copy number thus may also play a role in the
abnormal adhesion of SS red cells to laminin.
Division of Hematology and the Duke
Comprehensive Sickle Cell Center, Department of Medicine, Duke
University Medical Center, Durham, North Carolina 27710, the
¶ School of Engineering, Duke University, Durham, North
Carolina 27710, and the Glasgow and West Scotland Blood
Transfusion Service, Glasgow G2 5UA, Scotland
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