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A cloned CD15s‐negative variant of HL60 cells is deficient in expression of FUT7 and does not adhere to cytokine‐stimulated endothelial cells
Author(s) -
Weston Brent W.,
Hiller Kara M.,
Mayben John P.,
Manousos George,
Nelson Curt M.,
Klein Marina B.,
Goodman Jesse L.
Publication year - 1999
Publication title -
european journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0902-4441
DOI - 10.1111/j.1600-0609.1999.tb01849.x
Subject(s) - sialyl lewis x , fucosyltransferase , cell culture , selectin , cell adhesion molecule , microbiology and biotechnology , biology , biochemistry , immunology , gene , genetics
The initial steps of leukocyte adhesion depend on selectin/ligand interactions. Surface ligands on leukocytes are often modified by addition of the sialyl Lewis x (CD15s) determinant. Biosynthesis of CD15s is dependent upon α(2,3)sialyltransferases and α(1,3)fucosyltransferases. We report the isolation of an HL60 cell line variant, HL60A2, that no longer expresses CD15s. HL60A2 cells do not adhere to cytokine‐stimulated endothelial cells. Enzymatic assays reveal that this cell line has normal α(2,3)sialyltransferase activity but is deficient in the α(1,3)fucosyltransferase responsible for biosynthesis of CD15s (FUT7). The fucosyltransferase that constructs the non‐sialylated antigen, Lewis x (CD15), is expressed at high levels (FUT4). Transcript analyses show that FUT7 and FUT4 are inversely expressed in HL60 and variant cell lines. HL60A2 cells provide a tool to study the regulation of selectin ligands and corresponding human fucosyltransferase genes.