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Shanghai Institute of Cell Biology, Chinese Academy of Sciences, Shanghai, China
Selectins, a family of cell adhesion molecules, bind to sialylated
and fucosylated carbohydrates, such as sialyl Lewisx
(SLex) and its derivatives, as their minimal recognition
motif. Here we report that P-selectin bound to human malignant melanoma
A375 cells and mediated their adhesion under flow. However, probing
with a specific Ab failed to detect any apparent expression of
SLex. This finding was bolstered by reduced expression of
-1,3-fucosyltransferase VII mRNA and by absence of the cell surface
expression of P-selectin glycoprotein ligand-1. Instead, they expressed
heparan sulfate-like proteoglycans on their cell surfaces. Treatment
with ß-D-xyloside (a proteoglycan biosynthesis inhibitor)
or heparinases could reduce the binding of these cells to P-selectin.
In the competition assays, heparin, but not other proteoglycans, could
abolish the P-selectin recognition. Further, we found that P-selectin
could bind specifically to human tongue squamous cancer Tca-8113 cells,
which had negative staining of SLex but positive staining
of heparan sulfates. Both ß-D-xyloside and heparinases
could reduce the binding of P-selectin to Tca-8113 cells. Our results
thus indicate that heparan sulfate-like proteoglycans can mediate
adhesion of certain types of non-blood borne, "epithelial-like"
human cancer cells to P-selectin.
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