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J Biol Chem, Vol. 274, Issue 45, 31903-31908, November 5, 1999
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From Lu and Lu(v13) are two glycoprotein (gp) isoforms
that belong to the immunoglobulin superfamily and carry both the
Lutheran (Lu) blood group antigens and the basal cell adhesion molecule epithelial cancer antigen. Lu (85 kDa) and Lu(v13) (78 kDa) gps, which
differ only in the length of their cytoplasmic domain, are adhesion
molecules that bind laminin. In nonerythroid tissues, the Lu/basal cell
adhesion molecule antigens are predominantly expressed in the
endothelium of blood vessel walls and in the basement membrane region
of normal epithelial cells, whereas they exhibit a nonpolarized
expression in some epithelial cancers. Here, we analyzed the
polarization of Lu and Lu(v13) gps in epithelial cells by confocal
microscopy and domain-selective biotinylation assays. Differentiated
human colon carcinoma Caco-2 cells exhibited a polarized expression of
endogenous Lu antigens associated with a predominant expression of the
Lu isoform at the basolateral domain of the plasma membrane and a very
low expression of the Lu(v13) isoform at both the apical and
basolateral domains. Analysis of transfected Madin-Darby canine kidney
cells revealed a basolateral expression of Lu gp and a nonpolarized
expression of Lu(v13) gp. Delivery of Lu(v13) to both apical and
basolateral surfaces showed similar kinetics, indicating that this
isoform is directly transported to each surface domain. A dileucine
motif at position 608-609, specific to the Lu isoform, was
characterized as a dominant basolateral sorting signal that prevents Lu
gp from taking the apical delivery pathway.
INSERM U76, Institut National de la Transfusion
Sanguine, 6 rue Alexandre Cabanel, 75015 Paris, France,
§ INSERM U504, Hôpital Paul Brousse,
Villejuif, France, and the ¶ Scottish National Blood Transfusion
Service, G2 5UA Glasgow, Scotland
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