Immune regulation by the ST6Gal sialyltransferase

被引：307

作者：

Hennet, T

Chui, D

Paulson, JC

Marth, JD

机构：

[1] Univ Calif San Diego, Howard Hughes Med Inst, Div Cellular & Mol Med, La Jolla, CA 92093 USA

[2] Univ Calif San Diego, Glycobiol Program, La Jolla, CA 92093 USA

[3] Cytel Corp, San Diego, CA 92121 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1998年 / 95卷 / 08期

关键词：

D O I：

10.1073/pnas.95.8.4504

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The ST6Gal sialyltransferase controls production of the Sia alpha 2-6Gal beta 1-4GlcNAc (Sia6LacNAc) trisaccharide, which is the ligand for the lectin CD22. Binding of CD22 to Sia6GLacNAc is implicated in regulating lymphocyte adhesion and activation. We have investigated mice that lack ST6Gal and report that they are viable, yet exhibit hallmarks of severe immunosuppression unlike CD22-deficient mice. Notably, Sia6LacNAc-deficient mice display reduced serum IgM levels, impaired B cell proliferation in response to IgM and CD40 crosslinking, and attenuated antibody production to T-independent and T-dependent antigens. Deficiency of ST6Gal was further found to alter phosphotyrosine accumulation during signal transduction from the B lymphocyte antigen receptor. These studies reveal that the ST6Gal sialyltransferase and corresponding production of the Sia6LacNAc oligosaccharide are essential in promoting B lymphocyte activation and immune function.

引用

页码：4504 / 4509

页数：6