High endothelial cells synthesize and degrade sLex. Putative implications for L-selectin-dependent recognition.

Abstract:

: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 alpha(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 alpha(2,3)sialidase(s).

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Majuri ML,Räbinä J,Niittymäki J,Tiisala S,Mattila P,Aavik E,Miyasaka M,Renkonen O,Renkonen R

doi

10.1016/s0014-5793(99)00834-0

keywords:

subject

Has Abstract

pub_date

1999-07-16 00:00:00

pages

97-100

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)00834-0

journal_volume

455

pub_type

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