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High endothelial cells synthesize and degrade sLex. Putative implications for L‐selectin‐dependent recognition
Author(s) -
Majuri Marja-Leena,
Räbinä Jarkko,
Niittymäki Jaana,
Tiisala Sinikka,
Mattila Pirkko,
Aavik Einari,
Miyasaka Masayuki,
Renkonen Ossi,
Renkonen Risto
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00834-0
Subject(s) - sialyl lewis x , fucosylation , fucosyltransferase , sialidase , epitope , selectin , glycoprotein , chemistry , lymphocyte homing receptor , cell culture , l selectin , microbiology and biotechnology , high endothelial venules , biochemistry , enzyme , cell , antigen , biology , fucose , immunology , cell adhesion molecule , cell adhesion , neuraminidase , genetics , receptor
L‐selectin guides lymphocytes into peripheral lymphoid tissues by recognizing glycoprotein ligands decorated with 6‐sulfated sialyl Lewis x (sulfo sLex). Here we have used a rat peripheral lymph node high endothelial cell line (Ax) to study in detail the synthesis, expression and degradation of sLex epitope. We show here that Ax cells possess active α(1,3)fucosyltransferase Fuc‐TVII, the enzyme responsible for the final fucosylation of sialyl‐ N ‐acetyllactosamine during sLex synthesis, and express sLex on the cell surface. Furthermore, these cells degrade sLex, primarily by desialylating it to neutral Lex epitopes by α(2,3)sialidase(s).