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• W1622358858 endingPage "565" @default.
• W1622358858 startingPage "558" @default.
• W1622358858 abstract "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 alpha-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 beta-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 beta-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." @default.
• W1622358858 created "2016-06-24" @default.
• W1622358858 creator A5061585695 @default.
• W1622358858 creator A5088556973 @default.
• W1622358858 date "2000-07-01" @default.
• W1622358858 modified "2023-10-01" @default.
• W1622358858 title "Heparan Sulfate-Like Proteoglycans Mediate Adhesion of Human Malignant Melanoma A375 Cells to P-Selectin Under Flow" @default.
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• W1622358858 doi "https://doi.org/10.4049/jimmunol.165.1.558" @default.
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