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Laboratory of Molecular Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China
Stimulated endothelial cells and activated platelets express
P-selectin, which reacts with P-selectin glycoprotein ligand-1 (PSGL-1)
for leukocyte rolling on the stimulated endothelial cells and
heterotypic aggregation of the activated platelets on leukocytes.
P-selectin also binds to several cancer cells in vitro and promotes the
growth and metastasis of human colon carcinoma in vivo. The
P-selectin/PSGL-1 interaction requires tyrosine sulfation. However, it
is unknown whether sulfation is necessary for P-selectin binding to
somatic cancer cells. In this study, we show that P-selectin mediated
adhesion of Acc-M cells, a cell line derived from a human adenoid
cystic carcinoma of salivary gland. These cells had a moderate
expression of heparan sulfate-like proteoglycans, but had no detectable
expressions of PSGL-1, CD24, Lewisx, and sialyl
Lewisx. Treatment with sodium chlorate (a sulfation
biosynthesis inhibitor), but not
4-methylumbelliferyl-
-D-xyloside (a proteoglycan
biosynthesis inhibitor) or heparinases, reduced adhesion of these cells
to P-selectin. Sodium chlorate also inhibited the P-selectin
precipitation of the 
160-, 54-, and 36-kDa molecules from the
cell surface of Acc-M cells. Furthermore, P-selectin could bind to
human breast carcinoma ZR-75-30 cells in a sulfation-dependent manner.
Our results thus indicate that sulfation is essential for adhesion of
nonblood-borne, epithelial-like human cancer cells to
P-selectin.
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