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

FEBS Letters

Räbinä, Jarkko¹  Aavik, Einari²  Majuri, Marja-Leena¹  Miyasaka, Masayuki⁴  Niittymäki, Jaana¹  Renkonen, Risto¹  Mattila, Pirkko¹  Tiisala, Sinikka¹  Renkonen, Ossi³ 

[1] Haartman Institute, Department of Bacteriology and Immunology, P.O. Box 21, 00014 University of Helsinki, Helsinki, Finland;Haartman Institute, Transplantation laboratory, P.O. Box 21, 00014 University of Helsinki, Helsinki, Finland;Institute of Biotechnology, P.O. Box 56, University of Helsinki, Helsinki, Finland;Department of Bioregulation, Osaka University Medical School, Osaka, Japan

关键词: Endothelium;    Inflammation;    α(1;    3)fucosyltransferase;    α(2;    3)sialidase;    Sialyl Lewis x;    Fuc;    fucose;    Fuc-T;    fucosyltransferase;    Gal;    galactose;    GlcNAc;    N-acetylglucosamine;    HEV;    high endothelial venule;    Lex;    Lewis x;    NeuNAc;    N-acetylneuraminic acid;    sLex;    sialyl Lewis x;   

DOI  :  10.1016/S0014-5793(99)00834-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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).

【 授权许可】

Unknown