ST6Gal唾液酸转移酶的免疫调节作用。
Immune regulation by the ST6Gal sialyltransferase.
作者信息
Hennet T, Chui D, Paulson J C, Marth J D
机构信息
Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, and the Glycobiology Program, 9500 Gilman Drive 0625, University of California at San Diego, La Jolla, CA 92093, USA.
出版信息
Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4504-9. doi: 10.1073/pnas.95.8.4504.
The ST6Gal sialyltransferase controls production of the Siaalpha2-6Galbeta1-4GlcNAc (Sia6LacNAc) trisaccharide, which is the ligand for the lectin CD22. Binding of CD22 to Sia6LacNAc 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.
ST6Gal唾液酸转移酶控制Siaα2-6Galβ1-4GlcNAc（Sia6LacNAc）三糖的产生，该三糖是凝集素CD22的配体。CD22与Sia6LacNAc的结合与调节淋巴细胞粘附和激活有关。我们研究了缺乏ST6Gal的小鼠，并报告它们是可存活的，但与CD22缺陷小鼠不同，表现出严重免疫抑制的特征。值得注意的是，Sia6LacNAc缺陷小鼠的血清IgM水平降低，对IgM和CD40交联的B细胞增殖受损，以及对非T依赖性和T依赖性抗原的抗体产生减弱。进一步发现ST6Gal的缺乏会改变B淋巴细胞抗原受体信号转导过程中的磷酸酪氨酸积累。这些研究表明，ST6Gal唾液酸转移酶和Sia6LacNAc寡糖的相应产生对于促进B淋巴细胞激活和免疫功能至关重要。
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